IP Library › Granted Patent US 12,421,287
Granted Patent B2
US 12,421,287 · App. 19/022,291 · Granted Sep 23, 2025

T-cell modulatory multimeric polypeptides and methods of use thereof

Inventors: Ronald D. Seidel, III (Boston, MA); Rodolfo J. Chaparro (Cambridge, MA)
Assignee: Cue Biopharma, Inc.
C07K14/55A61K9/0019A61K35/17C07K14/005C07K14/4748C07K14/70539G01N33/5008A61K38/00A61K2039/505C07K2317/34C07K2319/30
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,421,287
App. No.
19/022,291
Granted
Sep 23, 2025
Kind
B2
Abstract

The present disclosure provides variant immunomodulatory polypeptides, and fusion polypeptides comprising the variant immunomodulatory peptides. The present disclosure provides T-cell modulatory multimeric polypeptides, and compositions comprising same, where the T-cell modulatory multimeric polypeptides comprise a variant immunomodulatory polypeptide of the present disclosure. The present disclosure provides nucleic acids comprising nucleotide sequences encoding the T-cell modulatory multimeric polypeptides, and host cells comprising the nucleic acids. The present disclosure provides methods of modulating the activity of a T cell; the methods comprise contacting the T cell with a T-cell modulatory multimeric polypeptide of the present disclosure.

Claims (25)

1. A fusion polypeptide comprising:

a) a variant IL-2 polypeptide that has an amino acid sequence having at least 98% amino acid sequence identity to the amino acid sequence set forth in SEQ ID NO:44, wherein amino acid 16 is Ala and amino acid 42 is Ala, and wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST; and

b) heterologous fusion partner comprising an antibody Fc region and an antigen-binding region of an antibody,

wherein the fusion polypeptide comprises from 500 to 700 amino acids, and

wherein the heterologous fusion partner does not comprise a major histocompatibility complex (MHC) polypeptide.

2. The fusion polypeptide of claim 1 , wherein the variant IL-2 polypeptide has an amino acid sequence having at least 99/a amino acid sequence identity to the amino acid sequence set forth in SEQ ID NO:44, wherein amino acid 16 is Ala and amino acid 42 is Ala, and wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST.

3. The fusion polypeptide of claim 1 , wherein the variant IL-2 polypeptide has the amino acid sequence set forth in SEQ ID NO:44, wherein amino acid 16 is Ala and amino acid 42 is Ala.

4. The fusion polypeptide of claim 1 , wherein the fusion polypeptide comprises from 500 to 600 amino acids.

5. The fusion polypeptide of claim 1 , wherein the fusion polypeptide comprises from 600 to 700 amino acids.

6. The fusion polypeptide of claim 2 , wherein the fusion polypeptide comprises from 500 to 600 amino acids.

7. The fusion polypeptide of claim 2 , wherein the fusion polypeptide comprises from 600 to 700 amino acids.

8. The fusion polypeptide of claim 3 , wherein the fusion polypeptide comprises from 500 to 600 amino acids.

9. The fusion polypeptide of claim 3 , wherein the fusion polypeptide comprises from 600 to 700 amino acids.

10. The fusion polypeptide of claim 4 , wherein the Fc polypeptide has at least 95% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

11. The fusion polypeptide of claim 5 , wherein the Fc polypeptide has at least 95% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

12. The fusion polypeptide of claim 6 , wherein the Fc polypeptide has at least 95% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

13. The fusion polypeptide of claim 7 , wherein the Fc polypeptide has at least 95% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

14. The fusion polypeptide of claim 8 , wherein the Fc polypeptide has at least 95% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

15. The fusion polypeptide of claim 9 , wherein the Fc polypeptide has at least 95% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

16. The fusion polypeptide of claim 4 , wherein the Fc polypeptide has at least 98% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

17. The fusion polypeptide of claim 5 , wherein the Fc polypeptide has at least 98% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

18. The fusion polypeptide of claim 6 , wherein the Fc polypeptide has at least 98% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

19. The fusion polypeptide of claim 7 , wherein the Fc polypeptide has at least 98% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

20. The fusion polypeptide of claim 8 , wherein the Fc polypeptide has at least 98% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

21. The fusion polypeptide of claim 9 , wherein the Fc polypeptide has at least 98% amino acid sequence identity to the human IgG1 Fc polypeptide of SEQ ID NO:57, wherein the percent sequence identity is determinable by a sequence alignment performed using BLAST, and wherein the IgG1 Fc polypeptide comprises one or more amino acid substitutions selected from N77A, L14A, L15A, L14F, L15E, and P111S, based on the amino acid numbering depicted in SEQ ID NO:80.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 7, 2025
From: SEIDEL, RONALD D., III; CHAPARRO, RODOLFO J.
To: CUE BIOPHARMA, INC.
Reel/Frame 070147/0707 →
Continuity (13)
Continuation 18899926 · Sep 27, 2024
Continuation 18388788 · Nov 10, 2023
Continuation 18080275 · Dec 13, 2022
Continuation 17831024 · Jun 2, 2022
Continuation 17131104 · Dec 22, 2020
Division 16812926 · Mar 9, 2020
Continuation 16741202 · Jan 13, 2020
Continuation 16462443
Provisional Application 62582132 · Nov 6, 2017
Provisional Application 62555435 · Sep 7, 2017
Provisional Application 62470774 · Mar 13, 2017
Provisional Application 62438272 · Dec 22, 2016
Related Publication 20250243253A1 · Jul 31, 2025
References Cited (400)
US 5635363A · Altman et al. · 1997 [cited by applicant]
US 6197302B1 · Hirsch et al. · 2001 [cited by applicant]
US 6211342B1 · Hirsch et al. · 2001 [cited by applicant]
US 6268411B1 · Schneck et al. · 2001 [cited by applicant]
US 6322789B1 · Vitiello et al. · 2001 [cited by applicant]
US 6600012B1 · Agrawal et al. · 2003 [cited by applicant]
US 6696304B1 · Parker · 2004 [cited by applicant]
US 7098306B2 · Economou et al. · 2006 [cited by applicant]
US 7186804B2 · Gillies · 2007 [cited by examiner]
US 7432351B1 · Chen · 2008 [cited by applicant]
US 7670595B2 · Gillies et al. · 2010 [cited by applicant]
US 8435494B2 · Gelfand · 2013 [cited by applicant]
US 8992937B2 · Hansen et al. · 2015 [cited by applicant]
US 9284349B2 · Tsunoda et al. · 2016 [cited by applicant]
US 9359424B2 · Maoult et al. · 2016 [cited by applicant]
US 9494588B2 · Springer et al. · 2016 [cited by applicant]
US 10059750B2 · Davis et al. · 2018 [cited by applicant]
US 10272042B2 · Daftarian · 2019 [cited by examiner]
US 10501521B2 · Georges · 2019 [cited by examiner]
US 10927158B2 · Seidel, III et al. · 2021 [cited by applicant]
US 10927161B2 · Seidel et al. · 2021 [cited by applicant]
US 11117945B2 · Seidel, III et al. · 2021 [cited by applicant]
US 11370821B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11377478B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11380821B2 · Jia et al. · 2022 [cited by applicant]
US 11401314B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11479595B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11505588B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11505591B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11530248B2 · Seidel, III et al. · 2022 [cited by applicant]
US 11708400B2 · Seidel, III et al. · 2023 [cited by applicant]
US 11739133B2 · Seidel, III et al. · 2023 [cited by applicant]
US 11767355B2 · Seidel, III et al. · 2023 [cited by applicant]
US 11851467B2 · Seidel, III et al. · 2023 [cited by applicant]
US 11878062B2 · Cemerski et al. · 2024 [cited by applicant]
US 11905320B2 · Seidel, III et al. · 2024 [cited by applicant]
US 11987610B2 · Seidel, III et al. · 2024 [cited by applicant]
US 12145973B2 · Seidel, III et al. · 2024 [cited by applicant]
US 12152061B2 · Seidel, III et al. · 2024 [cited by applicant]
US 12180258B2 · Seidel, III et al. · 2024 [cited by applicant]
US 20010021516A1 · Wei et al. · 2001 [cited by applicant]
US 20020006664A1 · Sabatini · 2002 [cited by applicant]
US 20020031520A1 · Economou et al. · 2002 [cited by applicant]
US 20020123108A1 · Edwards et al. · 2002 [cited by applicant]
US 20020165136A1 · Baserga et al. · 2002 [cited by applicant]
US 20030100074A1 · Yu et al. · 2003 [cited by applicant]
US 20030190614A1 · Presta et al. · 2003 [cited by applicant]
US 20030229023A1 · Oliner et al. · 2003 [cited by applicant]
US 20030235536A1 · Blumberg et al. · 2003 [cited by applicant]
US 20040038349A1 · Hilbert et al. · 2004 [cited by applicant]
US 20040132977A1 · Gantier · 2004 [cited by examiner]
US 20040161817A1 · Benton et al. · 2004 [cited by applicant]
US 20040209363A1 · Watts et al. · 2004 [cited by applicant]
US 20040234531A1 · Casares et al. · 2004 [cited by applicant]
US 20050003431A1 · Wucherpfennig et al. · 2005 [cited by applicant]
US 20050009012A1 · Holzberg et al. · 2005 [cited by applicant]
US 20050100926A1 · Chen et al. · 2005 [cited by applicant]
US 20050142142A1 · Burrows et al. · 2005 [cited by applicant]
US 20060034865A1 · Hildebrand et al. · 2006 [cited by applicant]
US 20060269515A1 · Deniz-Mize et al. · 2006 [cited by applicant]
US 20070036752A1 · Gillies et al. · 2007 [cited by applicant]
US 20070148162A1 · Bhardwaj et al. · 2007 [cited by applicant]
US 20070286843A1 · Pfizenmaier et al. · 2007 [cited by applicant]
US 20080199485A1 · Kundig et al. · 2008 [cited by applicant]
US 20080219947A1 · Linette et al. · 2008 [cited by applicant]
US 20080269070A1 · Ramseier et al. · 2008 [cited by applicant]
US 20100159594A1 · Hansen et al. · 2010 [cited by applicant]
US 20100190720A1 · Hollingsworth et al. · 2010 [cited by applicant]
US 20100226854A1 · Schøller et al. · 2010 [cited by applicant]
US 20110002956A1 · Weiner et al. · 2011 [cited by applicant]
US 20110268737A1 · Favier et al. · 2011 [cited by applicant]
US 20110318380A1 · Brix et al. · 2011 [cited by applicant]
US 20120003220A1 · Chen · 2012 [cited by applicant]
US 20120121577A1 · Weidanz et al. · 2012 [cited by applicant]
US 20120177595A1 · Wong et al. · 2012 [cited by applicant]
US 20120264161A1 · Scholler et al. · 2012 [cited by applicant]
US 20130017199A1 · Langermann · 2013 [cited by applicant]
US 20130066055A1 · Lerchen et al. · 2013 [cited by applicant]
US 20130149305A1 · Ostrand-Rosenberg · 2013 [cited by applicant]
US 20140046026A1 · Garcia et al. · 2014 [cited by applicant]
US 20140162293A1 · Springer et al. · 2014 [cited by applicant]
US 20140242077A1 · Choi et al. · 2014 [cited by applicant]
US 20150071987A1 · Selvaraj · 2015 [cited by applicant]
US 20150224186A1 · Nakagawa · 2015 [cited by applicant]
US 20150232532A1 · Ostrand-Rosenberg · 2015 [cited by applicant]
US 20150352201A1 · David et al. · 2015 [cited by applicant]
US 20150374788A1 · Paulsen et al. · 2015 [cited by applicant]
US 20160011204A1 · Almo et al. · 2016 [cited by applicant]
US 20160083477A1 · Klein et al. · 2016 [cited by applicant]
US 20160090407A1 · Hosse et al. · 2016 [cited by applicant]
US 20160114019A1 · Li et al. · 2016 [cited by applicant]
US 20160152725A1 · Cheung et al. · 2016 [cited by applicant]
US 20160175397A1 · Umana et al. · 2016 [cited by applicant]
US 20160304580A1 · Ellmark et al. · 2016 [cited by applicant]
US 20160362465A1 · Nishimura et al. · 2016 [cited by applicant]
US 20170044229A1 · Garcia et al. · 2017 [cited by applicant]
US 20170044259A1 · Ann et al. · 2017 [cited by applicant]
US 20170058015A1 · Seidel, III et al. · 2017 [cited by applicant]
US 20170304421A1 · Wang et al. · 2017 [cited by applicant]
US 20170334951A1 · O'Reilly et al. · 2017 [cited by applicant]
US 20180044404A1 · Oda et al. · 2018 [cited by applicant]
US 20180064795A1 · Sugiyama · 2018 [cited by applicant]
US 20180086832A1 · Vogelstein et al. · 2018 [cited by applicant]
US 20180127481A1 · Santamaria · 2018 [cited by applicant]
US 20180208626A1 · Scheinberg et al. · 2018 [cited by applicant]
US 20180282392A1 · Seidel, III et al. · 2018 [cited by applicant]
US 20180339030A1 · Scheinberg · 2018 [cited by applicant]
US 20190046648A1 · Seidel, III et al. · 2019 [cited by applicant]
US 20190119375A1 · Tinya et al. · 2019 [cited by applicant]
US 20190119377A1 · Spirig et al. · 2019 [cited by applicant]
US 20190352363A1 · Seidel, III et al. · 2019 [cited by applicant]
US 20200172595A1 · Seidel, III et al. · 2020 [cited by applicant]
US 20200207824A1 · Seidel, III et al. · 2020 [cited by applicant]
US 20200317747A1 · Seidel, III et al. · 2020 [cited by applicant]
US 20200369745A1 · Seidel, III et al. · 2020 [cited by applicant]
US 20210284709A1 · Brandt et al. · 2021 [cited by applicant]
US 20210393693A1 · Seidel, III et al. · 2021 [cited by applicant]
US 20220008467A1 · Seidel, III et al. · 2022 [cited by applicant]
US 20220064247A1 · Seidel, III et al. · 2022 [cited by applicant]
US 20220079985A1 · Seidel, III et al. · 2022 [cited by applicant]
US 20220143063A1 · Seidel, III et al. · 2022 [cited by applicant]
US 20220162314A1 · Yeung et al. · 2022 [cited by applicant]
US 20220251202A1 · Djuretic et al. · 2022 [cited by applicant]
US 20220409732A1 · MacDonald et al. · 2022 [cited by applicant]
US 20230117521A1 · Seidel, III et al. · 2023 [cited by applicant]
US 20230126199A1 · Hanayama et al. · 2023 [cited by applicant]
US 20230139456A1 · Cemerski et al. · 2023 [cited by applicant]
US 20240025964A1 · Seidel, III et al. · 2024 [cited by applicant]
US 20240034770A1 · Suri et al. · 2024 [cited by applicant]
US 20240067700A1 · Seidel, III et al. · 2024 [cited by applicant]
CN 1791675 · 2006 [cited by applicant]
CN 101384621 · 2009 [cited by applicant]
CN 101418309 · 2009 [cited by applicant]
CN 101448951 · 2009 [cited by applicant]
CN 101688213 · 2010 [cited by applicant]
CN 105121715 · 2015 [cited by applicant]
CN 106456733 · 2017 [cited by applicant]
CN 108431022 · 2018 [cited by applicant]
EP 2998740 · 2016 [cited by applicant]
EP 3157552 · 2019 [cited by applicant]
EP 3596118 · 2020 [cited by applicant]
JP 2000515363 · 2000 [cited by applicant]
JP 2004501364 · 2004 [cited by applicant]
JP 2005506058 · 2005 [cited by applicant]
JP 2007530021 · 2007 [cited by applicant]
JP 2009537175 · 2009 [cited by applicant]
JP 2010524506 · 2010 [cited by applicant]
JP 2012516854 · 2012 [cited by applicant]
JP 2015537043 · 2015 [cited by applicant]
WO WO1994000150A1 · 1994 [cited by applicant]
WO WO1996004314A1 · 1996 [cited by applicant]
WO WO1997028191 · 1997 [cited by applicant]
WO WO2001090747 · 2001 [cited by applicant]
WO WO2002072631 · 2002 [cited by applicant]
WO WO2002087613 · 2002 [cited by applicant]
WO WO2002093129 · 2002 [cited by applicant]
WO WO2002102299 · 2002 [cited by applicant]
WO WO2003048334 · 2003 [cited by applicant]
WO WO2004029197 · 2004 [cited by applicant]
WO WO2004040262A2 · 2004 [cited by applicant]
WO WO2004111190 · 2004 [cited by applicant]
WO WO2005017148A1 · 2005 [cited by applicant]
WO WO2005012493A2 · 2005 [cited by applicant]
WO WO2006073941A2 · 2006 [cited by applicant]
WO WO2007136778 · 2007 [cited by applicant]
WO WO2008019888 · 2008 [cited by applicant]
WO WO2008113970 · 2008 [cited by applicant]
WO WO2008116468 · 2008 [cited by applicant]
WO WO2008134461 · 2008 [cited by applicant]
WO WO2009023270 · 2009 [cited by applicant]
WO WO2010037395 · 2010 [cited by applicant]
WO WO2010037514A2 · 2010 [cited by applicant]
WO WO2010085495 · 2010 [cited by applicant]
WO WO2010091122 · 2010 [cited by applicant]
WO WO2011066342 · 2011 [cited by applicant]
WO WO2011066389 · 2011 [cited by applicant]
WO WO2012007951 · 2012 [cited by applicant]
WO WO2012107417 · 2012 [cited by applicant]
WO WO2012146628 · 2012 [cited by applicant]
WO WO2012127464 · 2012 [cited by applicant]
WO WO2012175508 · 2012 [cited by applicant]
WO WO2013003761 · 2013 [cited by applicant]
WO WO2013079174 · 2013 [cited by applicant]
WO WO2014083004 · 2014 [cited by applicant]
WO WO2014093118 · 2014 [cited by applicant]
WO WO2014145806 · 2014 [cited by applicant]
WO WO2015007903 · 2015 [cited by applicant]
WO WO2015112541 · 2015 [cited by applicant]
WO WO2015142675 · 2015 [cited by applicant]
WO WO2015164815 · 2015 [cited by applicant]
WO WO2015195531 · 2015 [cited by applicant]
WO WO2016000619 · 2016 [cited by applicant]
WO WO2016014428 · 2016 [cited by applicant]
WO WO2016025642 · 2016 [cited by applicant]
WO WO2016029043 · 2016 [cited by applicant]
WO WO2016030350 · 2016 [cited by applicant]
WO WO2016141357 · 2016 [cited by applicant]
WO WO2016154246A1 · 2016 [cited by applicant]
WO WO2016164937 · 2016 [cited by applicant]
WO WO2016168771 · 2016 [cited by applicant]
WO WO2016186177A1 · 2016 [cited by applicant]
WO WO2016198932 · 2016 [cited by applicant]
WO WO2017008844 · 2017 [cited by applicant]
WO WO2017023779 · 2017 [cited by applicant]
WO WO2017059819 · 2017 [cited by applicant]
WO WO2017120222 · 2017 [cited by applicant]
WO WO2017123644 · 2017 [cited by applicant]
WO WO2017129737A1 · 2017 [cited by applicant]
WO WO2017151818 · 2017 [cited by applicant]
WO WO2017151940 · 2017 [cited by applicant]
WO WO2017167217A1 · 2017 [cited by applicant]
WO WO2017201131 · 2017 [cited by applicant]
WO WO2017201210 · 2017 [cited by applicant]
WO WO2018052947A1 · 2018 [cited by applicant]
WO WO2018119114 · 2018 [cited by applicant]
WO WO2018129270A1 · 2018 [cited by applicant]
WO WO2018165631 · 2018 [cited by applicant]
WO WO2018170168 · 2018 [cited by applicant]
WO WO2018170475 · 2018 [cited by applicant]
WO WO2019005886A1 · 2019 [cited by applicant]
WO WO2019038230 · 2019 [cited by applicant]
WO WO2019051091 · 2019 [cited by applicant]
WO WO2019051094 · 2019 [cited by applicant]
WO WO2019051126 · 2019 [cited by applicant]
WO WO2019051127 · 2019 [cited by applicant]
WO WO2019139896 · 2019 [cited by applicant]
WO WO2019162937 · 2019 [cited by applicant]
WO WO2020132297 · 2019 [cited by applicant]
WO WO2020071551A1 · 2020 [cited by applicant]
WO WO2020132138 · 2020 [cited by applicant]
WO WO2020180501A1 · 2020 [cited by applicant]
WO WO2020181062A1 · 2020 [cited by applicant]
WO WO2020205778A1 · 2020 [cited by applicant]
WO WO2020243315 · 2020 [cited by applicant]
WO WO2020247843 · 2020 [cited by applicant]
WO WO2020257191 · 2020 [cited by applicant]
WO WO2021055594 · 2021 [cited by applicant]
WO WO2021081232 · 2021 [cited by applicant]
WO WO2021081239 · 2021 [cited by applicant]
WO WO2021127495 · 2021 [cited by applicant]
WO WO2021172596 · 2021 [cited by applicant]
WO WO2021209759 · 2021 [cited by applicant]
WO WO2021230247A1 · 2021 [cited by applicant]
WO WO2022015880 · 2022 [cited by applicant]
WO WO2022087458 · 2022 [cited by applicant]
WO WO2022099156 · 2022 [cited by applicant]
WO WO2022125694 · 2022 [cited by applicant]
WO WO2022125711 · 2022 [cited by applicant]
WO WO2022226058A1 · 2022 [cited by applicant]
WO WO2023097188A1 · 2023 [cited by applicant]
WO WO2023081718A1 · 2023 [cited by applicant]
WO WO2023137156A2 · 2023 [cited by applicant]
Balagopalan et al. (2009) “Endocytic events in TCR Signaling: Focus on Adapters in Microclusters” Immunological Reviews, 232:1 84-98. [cited by applicant]
Burtness, et al.; “Pembrolizumab Alone or With Chemotherapy for Recurrent/Metastatic Head and Neck Squamous Cell Carcinoma in KEYNOTE-048: Subgroup Analysis by Programmed Death Ligand-1 Combined Positive Score”; Journal… [cited by applicant]
Celik, et al., “The diversity of the HLA-E-restricted peptide repertoire explains the immunological impact of the Arg107Gly mismatch” Immunogenetics, vol. 68, pp. 29-41 (2016). [cited by applicant]
Chen, et al., “Fusion protein linkers: property, design and functionality”, Advanced Drug Delivery Reviews, vol. 65, No. 10, pp. 1357-1369 (Oct. 15, 2013). [cited by applicant]
Hammer, et al., “Peptide-specific recognition of human cytomegalovirus strains controls adaptive natural killer cells” Nature Immunology, vol. 19, No. 5, pp. 453-463 (May 2018). [cited by applicant]
Harrington, et al.; “Pembrolizumab With or Without Chemotherapy in Recurrent or Metastatic Head and Neck Squamous Cell Carcinoma: Updated Results of the Phase III KEYNOTE-048 Study”; Journal of Clinical Oncology; vol. 4… [cited by applicant]
Huisman, et al., “An unbiased characterization of the HLA-E and CD94/NKG2x peptide repertoire reveals peptide ligands that skew NK cell activation”, bioRxiv, Available Online at: https://doi.org/10.1101/2022.08.03.50271… [cited by applicant]
Klein, et al., “Design and characterization of structured protein linkers with differing flexibilities” Protein Engineering, Design and Selection, vol. 27, No. 10, pp. 325-330 (Oct. 2014). [cited by applicant]
Ling, et al., “Effect of VH-VL Families in Pertuzumab and Trastuzumab Recombinant Production, Her2 and FcγllA Binding”, Frontiers in Immunology, vol. 9, No. 469, 11 pages (Mar. 2018). [cited by applicant]
Pardee, et al., “Tumor-derived α-fetoprotein impairs the differentiation and T cell stimulatory activity of human dendritic cells”, Journal of Immunology, vol. 193, No. 11, pp. 5723-5732 (Dec. 1, 2014). [cited by applicant]
Powderly et al (2022) “636 A phase 1, open-label, dose escalation and expansion study of CUE-102 monotherapy in HLA-A*0201 positive patients with WT1-positive recurrent/metastatic cancers” Journal of Clinical Oncology, … [cited by applicant]
Rölle, et al., “Distinct HLA-E peptide complexes modify antibody-driven effector functions of adaptive NK cells”, vol. 24, No. 8, pp. 1967-1976, (Aug. 21, 2018). [cited by applicant]
Samanta, D. et al., 'Structural and functional characterization of a single-chain peptide-MHC molecule that modulates both naive and activated CD 8+ T cells', PNAS, (Aug. 8, 2011), vol. 108, No. 33, pp. 13682-13687, doi… [cited by applicant]
Shimasaki, et al., “NK cells for cancer immunotherapy” Nature Reviews, Drug Discovery, vol. 19, pp. 200-218, (2020). [cited by applicant]
Terakura, et al., “Generation of CD19-chimeric antigen receptor modified CD8+ T cells derived from virus-specific central memory T cells” Blood, vol. 119, No. 1, pp. 72-82 (Jan. 5, 2012). [cited by applicant]
Truscott, et al.; “Human major histocompatibility complex (M HC) class I molecules with disulfide traps secure disease-related antigenic peptides and exclude competitor peptides”; Journal of Biological Chemistry; vol. 2… [cited by applicant]
Lu, et al.; “KRAS G12V neoantigen specific T cell receptor for adoptive T cell therapy against tumors”; Nature Communications; vol. 14, No. 6389, pp. 1-16 (2023). [cited by applicant]
Pan, et al.; “Potentiation of Kras peptide cancer vaccine by avasimibe, a cholesterol modulator”; EBioMedicine; vol. 49, pp. 72-81 (Nov. 2019). [cited by applicant]
Xu, et al.; “Neoantigen-targeted TCR-T cell therapy for solid tumors: How far from clinical application”; Cancer Letters; vol. 546, No. 215840, pp. 1-12 (Oct. 10, 2022). [cited by applicant]
Botten, et al.; “Identification of Protective Lassa Virus Epitopes That Are Restricted by HLA-A2”; Journal of Virology; vol. 80, No. 17, pp. 8351-8361 (Sep. 1, 2006). [cited by applicant]
Chen, et al.; “Human papillomavirus type 16 nucleoprotein E7 is a tumor rejection antigen”; PNAS; vol. 88, No. 1, pp. 110-114 (Jan. 1, 1991). [cited by applicant]
Hedley, et al.; “The frequency and significance of WT-1 expression in serous endometrial carcinoma”; Human Pathology; vol. 45, No. 9, pp. 1879-1884 (Sep. 2014). [cited by applicant]
HLA Nomenclature; “HLA Alleles Numbers”; 2 pages (Mar. 2023). [cited by applicant]
Reche, et al.; “Definition of MHC Supertypes Through Clustering of MHC Peptide Binding Repertoires”; Nicosia, G., Cutello, V., Bentley, P.J., Timmis, J. (eds); Artificial Immune Systems, Third International Conference, … [cited by applicant]
Yao, et al.; “HPV-16 E6 and E7 protein T cell epitopes prediction analysis based on distributions of HLA-A loci across populations: An in silico approach”; Vaccine; vol. 31, No. 18, pp. 2289-2294 (Apr. 26, 2013). [cited by applicant]
Accession No. 1 IRL_A chain A Interleukin-2; 1 page (Aug. 25, 1995). [cited by applicant]
Ackerman, et al.; “Highly Avid Magnetic Bead Capture: An Efficient Selection Method for de novo Protein Engineering Utilizing yeast Surface Display”; Biotechnol. Prog.; vol. 25, No. 3, pp. 774-783 (2009). [cited by applicant]
Aina, et al.; “Identification of novel targeting peptides for human ovarian cancer cells using ‘one-bead one-compount’ combinatorial libraries”; Mol. Cancer Ther.; vol. 4, No. 5, 8 pages (May 2005). [cited by applicant]
ANONYMOUS; “Rationally engineered biologics to harness nature's cues for selective and specific immune modulation”, Powerpoint presentation; 24 pages (Feb. 1, 2021). [cited by applicant]
Arduin, et al.; “Highly reduced binding to high and low affinity mouse Fc gamma receptors by L234A/L235A and N297A Fc mutations engineered into mouse lgG2a”; Molecular Immunology; vol. 63, pp. 456-463 (Feb. 2015). [cited by applicant]
Azuma, et al.; “B7-H1 is a ubiquitous antiapoptotic receptor on cancer cells”; Immunobiology; vol. 111, No. 7, pp. 3635-3643 (Apr. 1, 2008). [cited by applicant]
Baldi, et al.; “Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives”; Biotechnol. Lett .; vol. 29, pp. 677-684 (2007). [cited by applicant]
Bowers, et al.; “Coupling mammalian cell surface display with somatic hypermutation for the discovery and maturation of human antibodies”; PNAS; vol. 108, No. 51, pp. 20455-20460 (Dec. 20, 2011). [cited by applicant]
Bresson, et al.; “Anti-CD3 and nasal proinsulin combination therapy enhances remission from recent-onset autoimmune diabetes by inducing Tregs”; The Journal of Clinical Investigation; vol. 116, No. 5, pp. 1371-1381 (May… [cited by applicant]
Brophy, et al.; “A yeast display system for engineering functional peptide-MHC complexes”; Journal of Immunological Methods; vol. 272, pp. 235-246 (2003). [cited by applicant]
Buonaguro, et al.; “Translating Tumor Antigens into Cancer Vaccines”; Clinical and Vaccine Immunology; vol. 18, No. 1, pp. 23-24 (Jan. 2011). [cited by applicant]
Büttner; “Cell-based assays for high-throughput screening”; Expert Opin. Drug Discov..; vol. 1, No. 4, pp. 301-306 (Sep. 2006). [cited by applicant]
Cafri, et al.; “Development of novel genetic cancer vaccines based on membrane-attached ß2 microglobulin”; Ann. N.Y. Acad. Sci.; vol. 1283, pp. 87-90 (2013). [cited by applicant]
Card, et al.; “A soluble single-chain T-cell receptor IL-2 fusion protein retains MHC-restricted peptide specificity and IL-2 bioactivity”; Cancer Immunol Immunother; vol. 53, pp. 345-357 (Nov. 11, 2003). [cited by applicant]
Carey, et al.; “A soluble divalent class | MHC/lgG1 fusion protein activates CD8+ T cells in vivo”; Clinical Immunology; vol. 116, pp. 65-76 (2005). [cited by applicant]
Carmenate, et al.; “Human IL-2 Mutein with Higher Antitumor Efficacy Than Wild Type IL-2”; The Journal of Immunology; vol. 190, No. 12, pp. 6230-6238 (Jun. 15, 2013). [cited by applicant]
Casares, et al.; “A Peptide-Major Histocompatibility Complex II Chimera Favors Survival of Pancreatic ß-Islets Grafted in Type 1 Diabetic Mice”; Transplantation; vol. 85, No. 12, pp. 1717-1725 (Jun. 27, 2008). [cited by applicant]
Cebecauer, et al.; “Soluble MHC-Peptide Complexes Induce Rapid Death of CD8+ CTL”; The Journal of Immunology; vol. 174, pp. 6809-6819 (2005). [cited by applicant]
Celis, et al.; “Identification of Potential CTL Epitopes of Tumor-Associated Antigen Mage-1 for Five Common HLA-A Alleles”; Molecular Immunology; vol. 31, No. 18, pp. 1423-1430 (1994). [cited by applicant]
Center for Disease Control and Prevention; “How Many Cancers Are Linked with HPV Each Year?”; 4 pages (2016). [cited by applicant]
Chames, et al.; “Bispecific antibodies for cancer therapy; The light at the end of the tunnel?” mAbs; vol. 1, No. 6, pp. 539-547 (Nov.-Dec. 2009). [cited by applicant]
Cheever, et al.; “The Prioritization of Cancer Antigens: A National Cancer Institute Pilot Project for the Acceleration of Translational Research”; Clinical Cancer Research; vol. 15, No. 17, pp. 5324-5337 (Sep. 1, 2009). [cited by applicant]
Chung, et al.; “#674 A phase 1 dose-escalation and expansion study of CUE-101, given as monotherapy and in combination with pembrolizumab in recurrent/metastatic HPV16+ head and neck cancer patients”; Poster; Presented … [cited by applicant]
Chung, et al.; “# 681 A phase 1 study of CUE-101, a novel HPV16 E7-pHLA-IL2-Fc fusion protein, as monotherapy and in combination with pembrolizumab in patients with recurrent/metastatic HPV16+ head and neck cancer”; pos… [cited by applicant]
Chung, et al.; “A phase 1 dose-escalation and expansion study of CUE-101, a novel HPV16 E7-pHLA-IL2-Fc fusion protein, given alone and in combination with pembrolizumab in patients with recurrent/metastatic HPV16+ head … [cited by applicant]
Chung, et al.; “A phase 1 dose-escalation and expansion study of CUE-101, a novel HPV16 E7-pHLA-IL2-Fc fusion protein, given as monotherapy and in combination with pembrolizumab in patients with recurrent/metastatic HPV… [cited by applicant]
Crawford, et al.; “Use of baculovirus MHC/ peptide display libraries to characterize T-cell receptor ligands”; Immunological Reviews; vol. 210, pp. 156-170 (2006). [cited by applicant]
Crisci, et al.; “Virus-like particles: The new frontier of vaccines for animal viral infections”; Veterinary Immunology and Immunopathology; vol. 148, pp. 211-225 (2012). [cited by applicant]
Czajkowsky, et al.; “Fc-fusion proteins: new developments and future perspectives”; EMBO Mol. Med.; vol. 4, pp. 1015-1028 (2012). [cited by applicant]
Das, et al.; “Generation of murine tumor cell lines deficient in MHC molecule surface expression using the CRISPR/Cas9 system”; PLoS One; vol. 12, No. 3, 19 pages (Mar. 16, 2017). [cited by applicant]
De Charette, et al.; “Turning tumour cells into antigen presenting cells: The next step to improve cancer immunotherapy?”; European Journal of Cancer; vol. 68, pp. 134-147 (Oct. 2016). [cited by applicant]
Desmond, et al.; “A systematic review of T-cell epitopes in hepatitis B virus: identification, genotypic variation and relevance to antiviral therapeutics”; Antiviral Therapy; vol. 13, pp. 161-175 (2008). [cited by applicant]
Dimasi, et al.; “The design and characterization of oligospecific antibodies for simultaneous targeting of multiple disease mediators”; Journal of Molecular Biology; 393(3): p. 672-692 (2009). [cited by applicant]
Doussal, et al.; “Phage display of peptide /major histocompatibility complex”; Journal of Immunological Methods; vol. 241, pp. 147-158 (2000). [cited by applicant]
Dulberger, et al.; “Human leukocyte antigen F (HLA-F) presents peptides and regulates immunity through interactions with NK-cell receptors”; Immunity; vol. 46, No. 6, pp. 1018-1027 (Jun. 20, 2017). [cited by applicant]
Durinovic-Bello, et al.; “DRB1*0401-restricted human T cell clone specific for the major proinsulin73-90 epitope expresses a down-regulatory T helper 2 phenotype”; PNAS; vol. 103, No. 31, pp. 11683-11688 (Aug. 1, 2006). [cited by applicant]
Edwards, et al.; “The Remarkable Flexibility of the Human Antibody Repertoire; Isolation of Over One Thousand Different Antibodies to a Single Protein, BLyS”; J. Mol. Biol .; vol. 334, pp. 103-118 (2003). [cited by applicant]
Emboss Needle; 2 pages (Feb. 10, 2022). [cited by applicant]
Engelhard; “Structure of peptides associated with MHC class I molecules”; Current Opinion in Immunology; vol. 6, pp. 13-23 (1994). [cited by applicant]
Engler, et al.; “Peptide vaccines against hepatitis B virus: from animal model to human studies”; Molecular Immunology; vol. 38, pp. 457-465 (Dec. 2001). [cited by applicant]
Favier, et al.; “Tolerogenic Function of Dimeric Forms of HLA-G Recombinant Proteins: A Comparative Study In Vivo”; PLoS One; vol. 6, No. 7, 26 pages (Jul. 2011). [cited by applicant]
Fellner; “Ipilimumab (Yervoy) Prolongs Survival In Advanced Melanoma”; Drug Forecast; vol. 37, No. 9, pp. 503-530 (Sep. 2012). [cited by applicant]
GENBANK:AEV43323.1; “Fc lgG1 heavy chain constant region, partial [Homo sapiens]”; 2 pages (Jul. 25, 2016). [cited by applicant]
GENBANK:ALM96677.1; “MHC class I antigen, partial [Homo sapiens]”; 3 pages (Nov. 11, 2015). [cited by applicant]
GENBANK:NP_001009066.1; 2 pages (2003). [cited by applicant]
GENBANK:NP_001300958.1; “programmed cell death 1 ligand 1 isoform c precursor [Homo sapiens]”; 3 pages (Jun. 9, 2021). [cited by applicant]
GENBANK:NP_068693.1; “programmed cell death 1 ligand 1 precursor [Mus musculus]”; 3 pages (Jun. 9, 2021). [cited by applicant]
GenCore AEE04235; 4 pages (2005). [cited by applicant]
Goel, et al.; “Plasticity within the Antigen-Combining Site May Manifest as Molecufar Mimicry in the Humoral Immune Response”; The Journal of Immunology; vol. 173, pp. 7358-7367 (2004). [cited by applicant]
Gojanovich, et al.; “The Use of Peptide-Major-Histocompatibility-Complex Multimers in Type 1 Diabetes Mellitus”; Journal of Diabetes Science and Technology; vol. 6, No. 3, pp. 515-524 (May 2012). [cited by applicant]
Gough, et al.; “The HLA Region and Autoimmune Disease: Associations and Mechanisms of Action”; Current Genomics; vol. 8, pp. 453-465 (2007). [cited by applicant]
Greten, et al.; “Peptide-ß2-microglobulin-MHC fusion molecules bind antigen-specific T cells and can be used for multivalent MHC-Ig complexes”; Journal of Immunological Methods; vol. 271, pp. 125-135 (2002). [cited by applicant]
Grupp, et al.; “Adoptive Cellular Therapy”; Curr Top Microbiol Immunol.; 344: p. 149-172 (2011). [cited by applicant]
Guo, et al.; “Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle”; Nature; vol. 360, pp. 364-366 (Nov. 26, 1992). [cited by applicant]
Hansen, et al.; “Phage display of peptide/major histocompatibility class | complexes”; Eur. J. Immunol .; vol. 31, pp. 32-38 (2001). [cited by applicant]
HLA Nomenclature; “HLA Alleles Numbers”; 2 pages (Mar. 17, 2015). [cited by applicant]
Huang, et al.; “Bone regeneration in a rat cranial defect with delivery of PEI-condensed plasmid DNA encoding for bone morphogenetic protein-4 (BMP-4)”; Gene Therapy; vol. 12, No. 5, p. 418 (2005). [cited by applicant]
Huang, et al.; “Cancer immunotherapy using a DNA vaccine encoding a single-chain trimer of MHC class I linked to an HPV-16 E6 immunodominant CTL epitope”; Gene Ther.; vol. 12, No. 15, pp. 1180-1186 (Aug. 2005). [cited by applicant]
Hug, et al.; “T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin”; PNAS; vol. 101, No. 28, pp. 10308-10313 (Jul. 13, 2004). [cited by applicant]
Hugues, et al.; “Generation and use of alternative multimers of peptide/MHC complexes”; Journal of Immunological Methods; vol. 268, pp. 83-92 (2002). [cited by applicant]
Johannsen, et al.; “Definition of Key Variables for the Induction of Optimal NY-ESO-1-Specific T Cells in HLA Transgene Mice”; The Journal of Immunology; vol. 185, pp. 3445-3455 (2010). [cited by applicant]
Judkowski, et al.; “Identification of MHC Class II-Restricted Peptide Ligands, Including a Glutamic Acid Decarboxylase 65 Sequence, that Stimulate Diabetogenic T Cells from Transgenic BDC2.5 Nonobese Diabetic Mice”; The… [cited by applicant]
Karaki, et al.; “Is There Still Room for Cancer Vaccines at the Era of Checkpoint Inhibitors”; Vaccines; vol. 4, No. 37, 24 pages (2016). [cited by applicant]
Karin, et al.; “Reversal of Experimental Autoimmune Encephalomyelitis by a Soluble Peptide Variant of a Myelin Basic Protein Epitope: T Cell Receptor Antagonism and Reduction of Interferon γ and Tumor Necrosis Factor α … [cited by applicant]
Khan, et al.; “Adjustable Locks and Flexible Keys: Plasticity of Epitope-Paratope Interactions in Germline Antibodies”; The Journal of Immunology; vol. 192, pp. 5398-5405 (2014). [cited by applicant]
Kim, et al.; “Single chain MHC I trimer-based DNA vaccines for protection against Listeria monocytogenes infection”; Vaccine; vol. 30, pp. 2178-2186 (2012). [cited by applicant]
Kowalski, et al.; “Delivering the Messenger: Advances in Technologies for Therapeutic mRNA Delivery”; Molecular Therapy; vol. 27, No. 4, pp. 710-728 (Feb. 18, 2019). [cited by applicant]
Krautwurst, et al.; “Identification of Ligands for Olfactory Receptors by Functional Expression of a Receptor Library”; Cell; vol. 95, pp. 917-926 (Dec. 23, 1998). [cited by applicant]
Kreiter, et al.; “Increased Antigen Presentation Efficiency by Coupling Antigens to MHC Class | Trafficking Signals”; The Journal of Immunology; vol. 180, No. 1, pp. 309-318 (Jan. 1, 2008). [cited by applicant]
Kushnir, et al.; “Virus-like particles as a highly efficient vaccine platform: Diversity of targets and production systems and advances in clinical development”; Vaccine; vol. 31, pp. 58-83 (2012). [cited by applicant]
Lazar-Molnar, et al.; “Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2”; PNAS; vol. 105, No. 30, pp. 10483-10488 (Jul. 29, 2008). [cited by applicant]
Lazar-Molnar, et al.; “The PD-1/PD-L costimulatory pathway critically affects host resistance to the pathogenic fungus Histoplasma capsulatum”; PNAS; vol. 105, No. 7, pp. 2658-2663 (Feb. 19, 2008). [cited by applicant]
Lenormand, et al.; “HLA-DQA2 and HLA-DQB2 Genes Are Specifically Expressed in Human Langerhans Cells and Encode a New HLA Class II Molecule”; The Journal of Immunology; vol. 199, No. 8, pp. 3903-3911 (Apr. 15, 2012). [cited by applicant]
Li, et al.; “Chain A, anti-connexin26 scFv,lg heavy chain, Linker, anti-connexin26 scFv,lg light chain”; Accession 5WYM_A, Front Mol Neurosci 10, 298, 3 pages (Jan. 13, 2017). [cited by applicant]
Li, et al.; “Suppression of Ongoing T Cell-Mediated Autoimmunity by Peptide-MHC Class II Dimer Vaccination”; The Journal of Immunology; vol. 183, pp. 4809-4816 (Sep. 14, 2009). [cited by applicant]
Liao, et al.; “Interleukin-2 at the Crossroads of Effector Responses, Tolerance, and Immunotherapy”; Immunity; vol. 38, No. 1, pp. 13-25 (Jan. 1, 2013). [cited by applicant]
Lin, et al.; “Reversal of type 1 diabetes by a new MHC II-peptide chimera: “Single-epitope-mediated suppression” to stabilize a polyclonal autoimmune T-cell process”; Eur. J. Immunol.; vol. 40, pp. 2277-2288 (2010). [cited by applicant]
Lin, et al.; “The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of antibodies and T cell receptors”; PNAS; vol. 105, No. 8, pp. 3011-3016 (Feb. 26, 2008). [cited by applicant]
Linard, et al.; “A ras-Mutated Peptide Targeted by CTL Infiltrating a Human Melanoma Lesion”; The Journal of Immunology; vol. 168, pp. 4802-4808 (2002). [cited by applicant]
Liu, et al.; “Attaining High Transient Titers in CHO Cells”; Genetic Engineering & Biotechnology News; vol. 35, No. 17, 3 pages (Oct. 1, 2015). [cited by applicant]
Liu, et al.; “Major Histocompatibility Complex: Interaction with Peptides”; eLS; 12 pages (Aug. 15, 2011). [cited by applicant]
Lloyd, et al.; “Modelling the human immune response: performance of a 1011 human antibody repertoire against a broad panel of therapeutically relevant antigens”; Protein Engineering, Design & Selection; vol. 22, No. 3, … [cited by applicant]
Mallone, et al.; “T Cell Recognition of Autoantigens in Human Type 1 Diabetes: Clinical Perspectives”; Clinical and Developmental Immunology; vol. 2011, 16 pages (2011). [cited by applicant]
Margalit, et al.; “Induction of Antitumor Immunity by CTL Epitopes Genetically Linked to Membrane-Anchored ß2-Microglobulin”; The Journal of Immunology; vol. 176, pp. 217-224 (2006). [cited by applicant]
Martin-Orozco, et al.; “Melanoma Cells Express ICOS Ligand to Promote the Activation and Expansion of T-Regulatory Cells”; Cancer Research; vol. 70, No. 23, pp. 9581-9590 (2010). [cited by applicant]
McAllister, et al.; “Adaptation of Recombinant HEK-293 Cells to Growth in Serum Free Suspension”; Animal Cell Technology: Products from Cells, Cells as Products; 3 pages (1999). [cited by applicant]
McNally, et al.; “CD4+CD25+ regulatory T cells control CD8+ T-cell effector differentiation by modulating IL-2 homeostasis”; PNAS; vol. 108, No. 18, pp. 7529-7534 (May 3, 2011). [cited by applicant]
Medina, et al.; “PD-1 Pathway Inhibitors: Immuno-Onology Agents for Restoring Anititumor Immune Responses”; Pharmacotherapy; vol. 36, No. 3, pp. 317-334 (Mar. 2016). [cited by applicant]
Miao, et al.; “Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells”; Nature Protocols; vol. 2, No. 10, pp. 2348-2353 (2007). [cited by applicant]
Michels, et al.; “Islet-Derived CD4 T Cells Targeting Proinsulin in Human Autoimmune Diabetes”; Diabetes; vol. 66, pp. 722-734 (Mar. 2017). [cited by applicant]
Mizukoshi, et al.; “Identification of a-fetoprotein-derived peptides recognized by cytotoxic T lymphocytes in HLA-A24+ patients with hepatocellular carcinoma”; Int. J. Cancer; vol. 118, pp. 1194-1204 (2006). [cited by applicant]
Mott, et al.; “The Solution Structure of the F42A Mutant of Human Interleukin 2”; J. Mol. Biol.; vol. 247, pp. 979-994 (1995). [cited by applicant]
Mottez, et al.; “Cells Expressing a Major Histocompatibility Complex Class I Molecule with a Single Covalently Bound Peptide Are Highly Immunogenic”; J. Exp. Med.; vol. 181, pp. 493-502 (Feb. 1995). [cited by applicant]
Motz, et al.; “Tumor Endothelium FasL Establishes a Selective Immune Barrier Promoting Tolerance in Tumors”; Nat. Med.; vol. 20, No. 6, pp. 607-615 (Jun. 2014). [cited by applicant]
Muller, et al.; “Random peptide libraries displayed on adeno-associated virus to select for targeted gene therapy vectors”; Nature Biotechnology; vol. 21, No. 9, pp. 1040-1046 (Sep. 2003). [cited by applicant]
Naidoo, et al.; “Toxicities of the anti-PD-1 and anti-PD-L1 immune checkpoint antibodies”; Annals of Oncology; vol. 26, pp. 2375-2391 (Sep. 2015). [cited by applicant]
Nielsen, et al.; “MHC Class II epitope predictive algorithms”; Immunology; vol. 130, pp. 319-328 (2010). [cited by applicant]
Oates, et al.; “ImmTACs: Novel bi-specific agents for targeted cancer therapy”; Oncolmmunology; vol. 2, No. 2, 3 pages (Feb. 2013). [cited by applicant]
Obermann, et al.; “Peptide-ß2-microglobulin-major histocompatibility complex expressing cells are potent antigen-presenting cells that can generate specific T cells”; Immunology; vol. 122, pp. 90-97 (2007). [cited by applicant]
Ochoa-Garay, et al.; “The Ability of Peptides to Induce Cytotoxic T Cells In Vitro Does Not Strongly Correlate with Their Affinity for the H-2Ld Molecule: Implications for Vaccine Design and Immunotherapy”; Molecular Im… [cited by applicant]
Oka, et al.; “Induction of WT1 (Wilms' tumor gene)-specific cytotoxic T lymphocytes by WT1 peptide vaccine and the resultant cancer regression”; PNAS; vol. 101, No. 38, pp. 13885- 13890 (Sep. 21, 2004). [cited by applicant]
Oliveira, et al.; “Design, Immune Responses and Anti-Tumor Potential of an HPV16 E6E7 Multi-Epitope Vaccine”; PLoS One; vol. 10, No. 9, 13 pages (Sep. 21, 2015). [cited by applicant]
PDB:118L_A; “Chain A, T Lymphocyte Activation Antigen Cd80” 2 pages (Dec. 27, 2012). [cited by applicant]
Peach, et al.; “Both Extracellular Immunoglobin-like Domains of CD80 Contain Residues Critical for Binding T Cell Surface Receptors CTLA-4 and CD28*”; The Journal of Biological Chemistry; vol. 270, No. 36, pp. 21181-211… [cited by applicant]
Ponstingl, et al.; “The Rule of Antibody Structure: The Primary Structure of a Monoclonal lgG1 Immunoglobulin (Myeloma Protein Nie)”; Hoppe Seylers Z Physiol Chem.; vol. 357, No. 11, pp. 1571-1604 (Nov. 1976). [English … [cited by applicant]
Poosarla, et al.; “Computational De Novo Design of Antibodies Binding to a Peptide With High Affinity”; Biotechnology & Bioengineering; vol. 114, No. 6, pp. 1331-1342 (Jun. 2017). [cited by applicant]
Preda, et al.; “Soluble, dimeric HLA DR4-peptide chimeras: An approach for detection and immunoregulation of human type-1 diabetes”; Eur. J. Immunol.; vol. 35, pp. 2763-2776 (Aug. 16, 2005). [cited by applicant]
Quayle, et al.; “CUE-101, a Novel HPV16 E7-pHLA-IL-2-Fc Fusion Protein, Enhances Tumor Antigen Specific T Cell Activation for the Treatment of HPV16-Driven Malignancies”; Clinical Cancer Research; vol. 26, No. 8, pp. 19… [cited by applicant]
Quayle, et al.; “Immuno-STAT(TM) (Selective Targeting and Alteration of T cells) Platform: Targeting Tumor Heterogeneity and Tumor Escape Mechanisms”; DOI:10.1158/1078-0432.CCR-19-3354; URL:https://www.cuebiopharma.com/… [cited by applicant]
Rabu, et al.; “Production of recombinant human trimeric CD137L (4-1BBL). Cross-linking is essential to its T cell co-stimulation activity”; The Journal of Biological Chemistry; vol. 280, No. 50, pp. 41472-41481 (Dec. 16… [cited by applicant]
Ramani, et al.; “A secreted protein microarray platform for extracellular protein interaction discovery”; Analytical Biochemistry; vol. 420, pp. 127-138 (2012). [cited by applicant]
Reche, et al.; “Sequence Variability Analysis of Human Class I and Class II MHC Molecules: Functional and Structural Correlates of Amino Acid Polymorphisms”; Journal of Molecular Biology; vol. 331, No. 3, pp. 623-641 (A… [cited by applicant]
Repana, et al.; “The Network of Cancer Genes (NCG): a comprehensive catalogue of known and candidate cancer genes from cancer sequencing screens”; Genome Biology; vol. 20, No. 1, 12 pages (2019). [cited by applicant]
Ressing, et al.; “Human CTL epitopes encoded by human papillomavirus type 16 E6 and E7 identified through in vivo and in vitro immunogenicity studies of HLA-A*0201-binding peptides”; The Journal of Immunology; vol. 154,… [cited by applicant]
Rocha-Zavaleta, et al.; “Interleukin-2 (IL-2) receptor-ßy signalling is activated by c-Kit in the absence of IL-2, or by exogenous IL-2 via JAK3/STAT5 in human papillomavirus-associated cervical cancer”; Cellular Signal… [cited by applicant]
Sang, et al.; “Long-term silencing of autoimmune diabetes and improved life expectancy by a soluble pHLA-DR4 chimera in a newly-humanized NOD-DR4/B7 mouse”; Human Vaccines & Immunotherapeutics; vol. 10, No. 3, pp. 693-6… [cited by applicant]
Schmittnaegel, et al.; “A New Class of Bifunctional Major Histocompatibility Class I Antibody Fusion Molecules to Redirect CDS T Cells”; Molecular Cancer Therapeutics; vol. 15, No. 9, pp. 2130-2142 (Sep. 2016). [cited by applicant]
Schumacher, et al.; “Neoantigens in cancer immunotherapy”; Science; vol. 348, No. 6230, pp. 69-74 (Apr. 2, 2015). [cited by applicant]
Seidel, et al.; “Peptide-HLA-based immunotherapeutics platforms for direct modulation of antigen-specific T cells”; Scientific Reports; vol. 11, No. 19220, 8 pages (Sep. 2021). [cited by applicant]
Shah, et al.; “Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects”; Journal of Visualized Experiments; vol. 84, 11 pages (2014). [cited by applicant]
Sharma, et al.; “A synthetic chimeric peptide harboring human papillomavirus 16 cytotoxic T lymphocyte epitopes shows therapeutic potential in a murine model of cervical cancer”; Immunologic Research; 58(1): p. 132-138 … [cited by applicant]
Solinas, et al.; “The rationale behind targeting the ICOS-ICOS ligand costimulatory pathway in cancer immunotherapy”; ESMO Open; vol. 5, 7 pages (Jan. 2020). [cited by applicant]
Spang, et al.; “Heterodimeric Barnase-Barstar Vaccine Molecules: Influence of One versus Two Targeting Units Specific for Antigen Presenting Cells”; PLoS One; vol. 7, No. 9, 11 pages (Sep. 2012). [cited by applicant]