IP Library Granted Patent US 12,379,375
Granted Patent B2
US 12,379,375 · App. 18/468,626 · Granted Aug 5, 2025

Methods for assessing cell surface glycosylation

Inventors: Paul Ken Kodama (Seattle, WA); Tom Kowski (Seattle, WA); Mirna Mujacic (Seattle, WA); Kenneth Mayo Prentice (Seattle, WA)
Assignee: Juno Therapeutics, Inc.
G01N33/5308C12Q1/34C12Y305/01052G01N33/502G01N2400/10G01N2570/00
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Quick Facts
Patent No.
US 12,379,375
App. No.
18/468,626
Granted
Aug 5, 2025
Kind
B2
Abstract

Provided herein are methods for assessing cell surface glycans, e.g., N-glycans, by assessing a sample of released surface glycans, and determining the presence, absence, or level of glycans present in the sample. Also provided are methods of assaying and/or evaluating a cell composition by assessing the cell surface glycan profile of the cell composition and comparing the profile to a reference sample. Methods for manufacturing and/or culturing a plurality of cell compositions having consistent surface glycan expression with low variability are also provided.

Claims (26)

1. A method of assaying a cell composition, the method comprising:

(a) (i) assessing the cell surface profile in a sample from a test cell composition comprising a plurality of cells according to a method for assessing cell surface glycans comprising:

(1) incubating the test cell composition comprising a plurality of cells under conditions to release one or more glycans from the surface of cells in the test cell composition, wherein a sample comprising one or more cell surface glycans is generated; and

(2) determining the presence, absence, identity and/or level of glycans present in the sample, thereby assessing the cell surface glycan profile of the sample; and

(a) (ii) comparing the cell surface glycan profile of the sample to the cell surface glycan profile of a reference sample; or

(b) comparing the cell surface glycan profile of a sample with the cell surface profile of a reference sample, wherein cell surface glycan profile of the sample is or has been determined according to a method for assessing cell surface glycans comprising:

(1) incubating a test cell composition comprising a plurality of cells under conditions to release one or more glycans from the surface of cells in the test cell composition, wherein a sample comprising one or more cell surface glycans is generated; and

(2) determining the presence, absence, identity and/or level of glycans present in the sample, thereby assessing the cell surface glycan profile of the sample; and

wherein the cells express a recombinant receptor or the test composition comprises cells expressing a recombinant receptor.

2. The method of claim 1 , wherein the cell surface glycan profile comprises at least 25 different species of glycans.

3. The method of claim 1 , wherein the reference sample is from a different stage of a manufacturing process for producing the test cell composition or a source cell composition from which the test composition has been derived or obtained.

4. The method of claim 3 , wherein a difference in the glycan profile between the test composition and reference sample indicates one or more differences is present in the cells among the cells produced at the different stages in the manufacturing process.

5. The method of claim 4 , wherein the one more differences is associated with a functional activity or phenotype of the cells.

6. The method of claim 1 , wherein the reference sample comprises an average or median of the presence, absence, identity and/or level of the one or more target glycan or glycans among a plurality of compositions produced by the manufacturing process.

7. The method of claim 1 , wherein the cell surface glycan profile comprises high mannose N-glycans, bisected and Sialyl Lewis N-glycans, and/or N-acetyl lactosamine containing N-glycans.

8. The method of claim 1 , wherein the cell surface glycan profile comprises a fucosylated biantennary complex glycan having no reducing end terminal galactose residues, a fucosylated biantennary complex glycan having one reducing end terminal galactose residue, a fucosylated biantennary complex glycan having two reducing end terminal galactose residues, a biantennary complex glycan having no reducing end terminal galactose residues, a biantennary complex glycan having one reducing end terminal galactose residue, a biantennary complex glycan having two reducing end terminal galactose residues, a fucosylated biantennary complex glycan having two galactose residues and one N-acetylneuraminic acid residue, a fucosylated biantennary complex glycan having two galactose residues and two N-acetylneuraminic acid residues, a biantennary complex glycan having two galactose residues and two N-acetylneuraminic acid residues, a high mannose glycan having five mannose residues, a high mannose glycan having six mannose residues, a high mannose glycan having seven mannose residues, a high mannose glycan having eight mannose residues, and/or a high mannose glycan having nine mannose residues.

9. The method of claim 1 , wherein the cell surface glycan profile comprises the glycans in Table E1 or a subset thereof.

10. The method of claim 1 , wherein the reference sample is a different cell composition.

11. The method of claim 1 , wherein the reference sample is a reference standard that indicates a release specification, a label requirement, or a compendia specification.

12. The method of claim 1 , wherein the test cell composition is released for treatment of a subject only if the cell surface glycan profile of the composition is substantially the same as the reference sample and/or if the percent of a target glycan or each of a plurality of target glycans to the total glycans present in the sample differs by no more than 25%.

13. The method of claim 3 , wherein the stage of the manufacturing process is a prior stage of the manufacturing process.

14. The method of claim 4 , wherein the difference in the glycan profile exists if the cell surface glycan profile of the composition is substantially different from the reference sample and/or if the percent of a target glycan or each of the one or more target glycans to the total glycans present in the sample differs by greater than 10% from the percent of the target glycan or each of the one or more target glycans to the total glycans present in the reference sample.

15. The method of claim 5 , wherein the functional activity or phenotype comprises one or more of masking of a cell surface marker, a metabolic activity, differentiation state, proliferative or expansion capacity, activation state, cytolytic activity, signaling activity, an adhesion property, or a homing property.

16. The method of claim 1 , wherein cells in the test cell composition comprise whole or intact cells.

17. The method of claim 1 , wherein the incubation is carried out in the presence of an N-glycosidase.

18. The method of claim 1 , wherein the cells comprise T cells that are CD4+ and/or CD8+ T cells or the test cell composition comprises T cells that are CD4+ and/or CD8+ T cells.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Sep 18, 2023
From: KODAMA, PAUL KEN; KOWSKI, TOM; MUJACIC, MIRNA; PRENTICE, KENNETH MAYO
To: JUNO THERAPEUTICS, INC.
Reel/Frame 064937/0542 →
Continuity (4)
Division 16604547
Provisional Application 62515515 · Jun 5, 2017
Provisional Application 62485897 · Apr 14, 2017
Related Publication 20240159743A1 · May 16, 2024
References Cited (192)
US 4452773A · Molday · 1984 [cited by applicant]
US 4795698A · Owen · 1989 [cited by applicant]
US 5200084A · Liberti · 1993 [cited by applicant]
US 5219740A · Miller et al. · 1993 [cited by applicant]
US 6040177A · Riddell · 2000 [cited by applicant]
US 6207453B1 · Maass et al. · 2001 [cited by applicant]
US 6410319B1 · Raubitschek et al. · 2002 [cited by applicant]
US 6451995B1 · Cheung et al. · 2002 [cited by applicant]
US 7070995B2 · Jensen · 2006 [cited by applicant]
US 7265209B2 · Jensen · 2007 [cited by applicant]
US 7354762B2 · Jensen · 2008 [cited by applicant]
US 7446179B2 · Jensen et al. · 2008 [cited by applicant]
US 7446190B2 · Sadelain et al. · 2008 [cited by applicant]
US 7446191B2 · Jensen · 2008 [cited by applicant]
US 8324353B2 · Jensen · 2012 [cited by applicant]
US 8339645B2 · Nakawaki · 2012 [cited by applicant]
US 8389282B2 · Sadelain et al. · 2013 [cited by applicant]
US 8479118B2 · Lyndersay et al. · 2013 [cited by applicant]
US 8802374B2 · Jensen · 2014 [cited by applicant]
US 8822647B2 · Jensen · 2014 [cited by applicant]
US 8911993B2 · June et al. · 2014 [cited by applicant]
US 9029081B2 · Parsons et al. · 2015 [cited by applicant]
US 9233125B2 · Davila et al. · 2016 [cited by applicant]
US 9410126B2 · Satomaa et al. · 2016 [cited by applicant]
US 11796534B2 · Kodama et al. · 2023 [cited by applicant]
US 20020131960A1 · Sadelain et al. · 2002 [cited by applicant]
US 20020150914A1 · Anderson et al. · 2002 [cited by applicant]
US 20030223994A1 · Hoogenboom et al. · 2003 [cited by applicant]
US 20040086521A1 · Karpshofer et al. · 2004 [cited by applicant]
US 20040191260A1 · Reiter et al. · 2004 [cited by applicant]
US 20060034850A1 · Weldanz et al. · 2006 [cited by applicant]
US 20070099253A1 · Erkhov et al. · 2007 [cited by applicant]
US 20070116690A1 · Yang et al. · 2007 [cited by applicant]
US 20070134806A1 · Yoshiya et al. · 2007 [cited by applicant]
US 20070176088A1 · Li · 2007 [cited by applicant]
US 20090226474A1 · Weidanz et al. · 2009 [cited by applicant]
US 20090304679A1 · Weidanz et al. · 2009 [cited by applicant]
US 20110003380A1 · Miltenyi · 2011 [cited by applicant]
US 20130149337A1 · Cooper et al. · 2013 [cited by applicant]
US 20130287748A1 · June et al. · 2013 [cited by applicant]
US 20140179011A1 · Brousmiche et al. · 2014 [cited by applicant]
US 20140242709A1 · Brousmiche et al. · 2014 [cited by applicant]
US 20140271635A1 · Brodgon et al. · 2014 [cited by applicant]
US 20140294841A1 · Scheinberg et al. · 2014 [cited by applicant]
US 20210255173A1 · Kodama et al. · 2021 [cited by applicant]
US 20220050114A1 · Prentice · 2022 [cited by applicant]
EP 0304663 · 1992 [cited by applicant]
EP 452342 · 1994 [cited by applicant]
EP 2537416 · 2014 [cited by applicant]
JP H01105160 · 1989 [cited by applicant]
JP 2009103718 · 2009 [cited by applicant]
JP 2009142238 · 2009 [cited by applicant]
JP 2013007742 · 2013 [cited by applicant]
JP 2015091953 · 2015 [cited by applicant]
WO WO1990014421 · 1990 [cited by applicant]
WO WO1992008796 · 1992 [cited by applicant]
WO WO1994028143 · 1994 [cited by applicant]
WO WO1996013593 · 1996 [cited by applicant]
WO WO1996018105 · 1996 [cited by applicant]
WO WO1999018129 · 1999 [cited by applicant]
WO WO1999060120 · 1999 [cited by applicant]
WO WO2000014257 · 2000 [cited by applicant]
WO WO2003020763 · 2003 [cited by applicant]
WO WO2003068201 · 2003 [cited by applicant]
WO WO2004033685 · 2004 [cited by applicant]
WO WO2006000830 · 2006 [cited by applicant]
WO WO2008123793 · 2008 [cited by applicant]
WO WO2008128228 · 2008 [cited by applicant]
WO WO2009027041 · 2009 [cited by applicant]
WO WO2009072003 · 2009 [cited by applicant]
WO WO2010033140 · 2010 [cited by applicant]
WO WO2011044186 · 2011 [cited by applicant]
WO WO2011105544 · 2011 [cited by applicant]
WO WO2012129514 · 2012 [cited by applicant]
WO WO2013071154 · 2013 [cited by applicant]
WO WO2013123061 · 2013 [cited by applicant]
WO WO2013126726 · 2013 [cited by applicant]
WO WO2013166321 · 2013 [cited by applicant]
WO WO2014031687 · 2014 [cited by applicant]
WO WO2014055668 · 2014 [cited by applicant]
WO WO2015075139 · 2015 [cited by applicant]
WO WO2015164675 · 2015 [cited by applicant]
WO WO2016030414 · 2016 [cited by applicant]
WO WO2016036705 · 2016 [cited by applicant]
WO WO2018027197 · 2018 [cited by applicant]
WO WO2020056047 · 2020 [cited by applicant]
US 8,252,592 B2, 08/2012, Jensen (withdrawn) [cited by applicant]
Nakano et al., Mol. Cell. Proteomics 10:1-12 (2011). [cited by examiner]
Alonso-Camino et al., “CARbodies: Human Antibodies Against Cell Surface Tumor Antigens Selected From Repertoires Displayed on T Cell Chimeric Antigen Receptors,” Mol Ther Nucleic Acids (2013) 2(5):e93. [cited by applicant]
Anumula et al., “Advances in Fluorescence Derivatization Methods for High-Performance Liquid Chromatographic Analysis of Glycoprotein Carbohydrates,” Anal Biochem (2006) 350(1): 1-23. [cited by applicant]
Barrett et al., “Chimeric antigen receptor therapy for cancer,” Annu Rev Med. (2014);65:333-47. [cited by applicant]
Bateman et al., “Glycan analysis and influenza A virus infection of primary swine respiratory epithelial cells: the importance of NeuAc{alpha}2-6 glycans.” J Biol Chem. Oct. 29, 2010;285(44):34016-34026. [cited by applicant]
Boris-Lawrie et al., “Recent advances in retrovirus vector technology,” Cur. Opin. Genet. Develop. (1993) 3:102-109. [cited by applicant]
Brash et al., “Strontium phosphate transfection of human cells in primary culture: stable expression of the simian virus 40 large-T-antigen gene in primary human bronchial epithelial cells,” Mol. Cell Biol. (1987) 7: 20… [cited by applicant]
Brentjens et al., “CD19-targeted T cells rapidly induce molecular remissions in adults with chemotherapy-refractory acute lymphoblastic leukemia,” Sci Transl Med. (2013) 5(177):177ra38. [cited by applicant]
Burns et al., “Vesicular stomatitis virus G glycoprotein pseudotyped retroviral vectors: concentration to very high titer and efficient gene transfer into mammalian and nonmammalian cells,” Proc. Natl. Acad. Sci. USA (1… [cited by applicant]
Carlens et al., “Ex vivo T lymphocyte expansion for retroviral transduction: influence of serum-free media on variations in cell expansion rates and lymphocyte subset distribution,” Exp Hematol (2000) 28(10): 1137-46. [cited by applicant]
Cavalieri et al., “Human T lymphocytes transduced by lentiviral vectors in the absence of TCR activation maintain an intact immune competence,” Blood (2003) 102(2): 497-505. [cited by applicant]
Cheadle et al., “Chimeric antigen receptors for T-cell based therapy,” Methods Mol Biol. (2012);907:645-66. [cited by applicant]
Chervin et al., “Engineering higher affinity T cell receptors using a T cell display system,” J Immunol Methods, (2008) 339(2): 175-84. [cited by applicant]
Chicaybam et al., “An efficient low cost method for gene transfer to T lymphocytes,” PLoS One (2013) 8(3): e60298. [cited by applicant]
Cho et al. “Human mammalian cell sorting using a highly integrated microfabricated fluorescence-activated cell sorter (uFACS),” Lab Chip (2010) 10:1567-1573. [cited by applicant]
Chothia et al., “The outline structure of the T-cell alpha beta receptor,” EMBO J. (1988) 7(12):3745-3755. [cited by applicant]
Clackson, T. et al. “Making Antibody Fragments Using Phage Display Libraries,” Nature (1991) 352:624-628. [cited by applicant]
Clarke and Davies in: Methods in Molecular Medicine, vol. 58: Metastasis Research Protocols, vol. 2: Cell Behavior In Vitro and In Vivo, Edited by: S. A. Brooks and U. Schumacher © Humana Press Inc., Totowa, NJ (2001) p… [cited by applicant]
Cohen et al., “Recombinant antibodies with MHC-restricted, peptide-specific, T-cell receptor-like specificity: new tools to study antigen presentation and TCR-peptide-MHC interactions,” J Mol Recognit. (2003) 16(5):324-… [cited by applicant]
Comelli et al., “Activation of Murine CD4+ and CD8+ T Lymphocytes Leads to Dramatic Remodeling of N-linked Glycans,” J Immunol (2006) 177(4): 2431-2440. [cited by applicant]
Cooper et al., “T-cell clones can be rendered specific for CD19: toward the selective augmentation of the graft-versus-B-lineage leukemia effect,” Blood (2003) 101:1637-1644. [cited by applicant]
Davila et al., “CD19 CAR-targeted T cells induce long-term remission and B Cell Aplasia in an immunocompetent mouse model of B cell acute lymphoblastic leukemia,” PLoS One (2013) 8(4):e61338. [cited by applicant]
De Felipe, “Skipping the co-expression problem: the new 2A “Chysel” technology,” Genet Vaccines Ther Sep. 13, 2004;2(1):13. [cited by applicant]
De Felipe, “Targeting of proteins derived from self-processing polyproteins containing multiple signal sequences,” Traffic (2004) 5(8):616-626. [cited by applicant]
Earl et al., “CD45 Glycosylation Controls T-cell Life and Death,” Immunol Cell Biol (2008) 86(7): 608-615. [cited by applicant]
Eshghi et al., “Imaging of N-Linked Glycans from Formalin-Fixed Paraffin-Embedded Tissue Sections Using MALDI Mass Spectrometry.” ACS Chemical Biology 2014 9(9):2149-2156. [cited by applicant]
Fedorov et al., “PD-1- and CTLA-4-based inhibitory chimeric antigen receptors (iCARs) divert off-target immunotherapy responses,” Sci Transl Med. (2013) 5(215):215ra172. [cited by applicant]
Gan et al., “Native Mass Spectrometry of Recombinant Proteins From Crude Cell Lysates,” Anal Chem (2017) 89(8): 4398-4404. [cited by applicant]
Gimenez et al., “Quantitative analysis of N-glycans from human alfa-acid-glycoprotein using stable isotope labeling and zwitterionic hydrophilic interaction capillary liquid chromatography electrospray mass spectrometry… [cited by applicant]
Godin et al., “Microfluidics and photonics for Bio-System-on-a-Chip: a review of advancements in technology towards a microfluidic flow cytometry chip,” J Biophotonics (2008) 1(5):355-376. [cited by applicant]
Gotze et al., “Diagnosis of toxoplasmosis using a synthetic glycosylphosphatidylinositol glycan.” Angew Chem Int Ed Engl. (2014) 53(50):13701-13705. [cited by applicant]
Hall et al., “Cell Surface N-glycans Influence the Level of Functional E-cadherin at the Cell-Cell Border,” FEBS Open Bio (2014) 4: 892-897. [cited by applicant]
Hamouda et al., “Rapid Analysis of Cell Surface N-Glycosylation from Living Cells Using Mass Spectrometry,” J Proteome Research (2014) 13(12):6144-6151. [cited by applicant]
Hara et al., “Determination of mono-O-acetylated N-acetylneuraminic Acids in Human and Rat Sera by Fluorometric High-Performance Liquid Chromatography,” Anal Biochem (1989) 179(1): 162-66. [cited by applicant]
Holler et al., “In vitro evolution of a T cell receptor with high affinity for peptide/MHC,” Proc Natl Acad Sci USA, (2000) 97(10):5387-92. [cited by applicant]
Holler et al., “TCRs with high affinity for foreign pMHC show self-reactivity,” Nat Immunol (2003) 4(1):55-62. [cited by applicant]
Huang et al., “DNA transposons for modification of human primary T lymphocytes,” Methods Mol Biol (2009) 506: 115-126. [cited by applicant]
Hudecek et al., “Receptor affinity and extracellular domain modifications affect tumor recognition by ROR1-specific chimeric antigen receptor T cells,” Clin Cancer Res. Jun. 15, 2013;19(12):3153-3164. [cited by applicant]
Isailovic et al., “Delineating diseases by IMS-MS profiling of serum N-linked glycans.” J Proteome Res. (2012) 11(2):576-85. [cited by applicant]
Janeway et al., Immunobiology: The Immune System in Health and Disease, 3rd ED., Current Biology Publications (1997), p. 4:33. [cited by applicant]
Johnston, “Biolistic transformation: microbes to mice,” Nature (1990) 346:776-777. [cited by applicant]
Jores et al., “Resolution of hypervariable regions in T-cell receptor beta chains by a modified Wu-Kabat index of amino acid diversity.,” PNAS (1990) 87(23):9138-9142. [cited by applicant]
Kindt et al., Kuby Immunology 6th ed., W.H. Freeman and Co. (2007) p. 91. [cited by applicant]
Klebanoff et al., “Sorting through subsets: Which T cell populations mediate highly effective adoptive immunotherapy?,” J Immunother. (2012) 35(9): 651-660. [cited by applicant]
Kochenderfer et al., “Treating B-cell cancer with T cells expressing anti-CD19 chimeric antigen receptors,” Nature Reviews Clinical Oncology (2013) 10, 267-276. [cited by applicant]
Koste et al., “T-cell receptor transfer into human T cells with ecotropic retroviral vectors,” Gene Therapy (2014) 21: 533-538. [cited by applicant]
Kotb, “Bacterial pyrogenic exotoxins as superantigens,” Clinical Microbiology Reviews, (1995) 8:411-426. [cited by applicant]
Kurucz et al., “A bacterially expressed single-chain Fv construct from the 2B4 T-cell receptor,” PNAS (1993) 90(9):3830-3834. [cited by applicant]
Lauber et al, “Rapid Preparation of Released N-Glycans for HILIC Analysis Using a Labeling Reagent that Facilitates Sensitive Fluorescence and ESI-MS Detection,” Analytical Chemistry (2015) 87(10):5401-5409. [cited by applicant]
Lauber et al., “Rapid Preparation of Released N-Glycans for HILIC Analysis Using a Novel Flourescence and MS-Active Labeling Reagent,” Application Note from Waters Corporation (Waters.com) downloaded Mar. 28, 2017. [cited by applicant]
Lefranc et al., “IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains,” Dev Comp Immunol (2003) 27(1):55-77. [cited by applicant]
Li et al., “Directed evolution of human T-cell receptors with picomolar affinities by phage display,” Nat Biotechnol. (2005) 23:349-354. [cited by applicant]
Li et al., “Glycosylation and Stabilization of Programmed Death ligand-1 Suppresses T-cell Activity,” Nat Commun (2016) 7: 12632. [cited by applicant]
Ling et al., “B-cell and plasma cell antigens: new and previously defined clusters,” Leucocyte typing 111. (1987) 302-355. [cited by applicant]
Liu et al., “Cell Surface-Specific N-glycan Profiling in Breast Cancer,” PLoS One (2013) 8(8): e72704. [cited by applicant]
Liu et al., “Inclusion of Strep-tag II in design of antigen receptors for T-cell immunotherapy,” Nat Biotechnol (2016) 34(4):430-434. [cited by applicant]
Lupton et al., “Dominant positive and negative selection using a hygromycin phosphotransferase-thymidine kinase fusion gene,” Mol and Cell Biol (1991) 11(6):3374-3378. [cited by applicant]
Manuri et al., “piggyBac transposon/transposase system to generate CD19-specific T cells for the treatment of B-lineage malignancies,” Hum Gene Ther (2010) 21(4): 427-437. [cited by applicant]
Mehta et al., “Intrinsic Hepatocyte Dedifferentiation Is Accompanied by Upregulation of Mesenchymal Markers, Protein Sialylation and Core Alpha 1,6 Linked Fucosylation,” Sci Rep (2016) 6: 27965. [cited by applicant]
Miller et al., “Improved retroviral vectors for gene transfer and expression,” Biotechniques (1989) 7(9):980-982. [cited by applicant]
Miller et al., “Retrovirus packaging cells,” Human Gene Therapy (1990) 1:5-14. [cited by applicant]
Miwa et al., “Bisected, complex N-glycans and galectins in mouse mammary tumor progression and human breast cancer.” Glycobiology (2013) 23(12):1477-1490. [cited by applicant]
Nabi et al., “The Galectin Lattice at a Glance,” J Cell Sci (2015) 128(13): 2213-2219. [cited by applicant]
Nakano et al., “Identification of glycan structure alterations on cell membrane proteins in desoxyepothilone B resistant leukemia cells,” Mol Cell Proteomics. Nov. 2011;10(11):M111.009001. doi: 10.1074/mcp.M111.009001. [cited by applicant]
N-Glycosidase F, recombinant. Information Sheet, Roche Applied Science, Content version Jun. 2005. [cited by applicant]
Norton et al., “Development and Application of a Novel Recombinant Aleuria Aurantia Lectin With Enhanced Core Fucose Binding for Identification of Glycoprotein Biomarkers of Hepatocellular Carcinoma,” Proteomics (2016) … [cited by applicant]
Ohta et al., “Expression of Sialyl Lewis(x) Antigen on Human T Cells,” Cell Immunol (1993) 151(2): 491-497. [cited by applicant]
Ouedraogo et al., “Global Analysis of Circulating Immune Cells by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry,” PLoS One (2010) 5(10):e13691. [cited by applicant]
Park et al., “Treating cancer with genetically engineered T cells,” Trends Biotechnol. (2011) 29(11): 550-557. [cited by applicant]
Plummer et al., “Demonstration of peptide:N-glycosidase F Activity in endo-beta-N-acetylglucosaminidase F Preparations,” J Biol Chem (1984) 259(17): 10700-10704. [cited by applicant]
PNGaseF Protocol Prime, User Manual Dated Oct. 14, 2015, N-Zyme Scientifics. [cited by applicant]
PNGaseF Sheet, QA-Bio, dated Dec. 2, 2014. [cited by applicant]
Portolano et al., “Lack of Promiscuity in Autoantigen-Specific H and L Chain Combinations as Revealed by Human H and L Chain ‘Roulette’,” The Journal of Immunology (1993) 150(3):880-887. [cited by applicant]
Powers et al., “A Matrix Assisted Laser Desorption Ionization Imaging Mass Spectrometry Workflow for Spatial Profiling Analysis of N-linked Glycan Expression in Tissues,” Anal Chem (2013) 85(20): 9799-9806. [cited by applicant]
Powers et al., “Developing an Integrative Glycobiology Workflow for the Developing an Integrative Glycobiology Workflow for the Identification of Disease Markers for Pancreatic Cancer Identification of Disease Markers f… [cited by applicant]
Powers et al., “MALDI Imaging Mass Spectrometry Profiling of N-Glycans in Formalin-Fixed Paraffin Embedded Clinical Tissue Blocks and Tissue Microarrays,” PLOS One (2014) 9(9):E106255. [cited by applicant]
Powers et al., “Two-Dimensional N-Glycan Distribution Mapping of Hepatocellular Carcinoma Tissues by MALDI-Imaging Mass Spectrometry,” Biomolecules (2015) 5(4):2554-2572. [cited by applicant]
PROzyme InstantAB instruction manual, “Rapid N-Glycan Preparation with InstantAB” www.prozyme.com. [cited by applicant]
Redelinghuys et al., “Early murine T-lymphocyte activation is accompanied by a switch from N-Glycolyl- to N-acetyl-neuraminic acid and generation of ligands for siglec-E,” J Biol Chem. (2011) 286(40):34522-32. [cited by applicant]
Riddell et al., “Phase I study of cellular adoptive immunotherapy using genetically modified CD8+ HIV-specific T cells for HIV seropositive patients undergoing allogeneic bone marrow transplant,” Human Gene Therapy (199… [cited by applicant]
Ruhaak et al., “Glycan Labeling Strategies and Their Use in Identification and Quantification,” Anal Bioanal Chem (2010) 397(8): 3457-3481. [cited by applicant]
Sadelain et al., “The basic principles of chimeric antigen receptor design,” Cancer Discov. (2013) 3(4): 388-398. [cited by applicant]
Scarpa et al., “Characterization of recombinant helper retroviruses from Moloney based vectors in ecotropic and amphotropic packaging cell lines,” Virology (1991) 180:849-852. [cited by applicant]
Schlueter et al., “Specificity and Binding Properties of a Single-chain T Cell Receptor,” J. Mol. Biol. (1996) 256: 859. [cited by applicant]
Schuler et al. “Syfpeithi, Database for Searching and T-Cell Epitope Prediction. in Immunoinformatics,” Methods in Molecular Biology, (2007) vol. 409(1): 75-93, 2007. [cited by applicant]
Sharma et al., “Efficient sleeping beauty DNA transposition from DNA minicircles,” Molec Ther Nucl Acids (2013) 2:e74. [cited by applicant]
Singh et al., “ProPred: prediction of HLA-DR binding,” Bioinformatics (2001) 17(12):1236-1237. [cited by applicant]
Soo Hoo et al. Characterization of a single-chain T-cell receptor expressed in [cited by applicant]
Steinke et al., “The alpha gal story: Lessons learned from connecting the dots.” J Allergy Clin Immunol. Mar. 2015; 135(3): 589-597. [cited by applicant]
Tamada et al., “Redirecting Gene-Modified T Cells Toward Various Cancer Types Using Tagged Antibodies,” Clin Cancer Res (2012) 18(23): 6436-6445. [cited by applicant]
Tarentino et al., “Molecular Cloning and Amino Acid Sequence of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine Amidase From Flavobacterium Meningosepticum,” J Biol Chem (1990) 265(12): 6961-6966. [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. (2012) 119(1):72-82. [cited by applicant]
Townsend, R. R. Carbohydrate Analysis High Performance Liquid Chromatography and Capillary Electrophoresis., Ed. Z. El Rassi, pp. 181-209, 1995. [cited by applicant]
Turtle et al., “Engineered T cells for anti-cancer therapy,” Curr. Opin. Immunol. (2012) 24(5): 633-639. [cited by applicant]
Urbanska et al., “A Universal Strategy for Adoptive Immunotherapy of Cancer Through Use of a Novel T-cell Antigen Receptor,” Cancer Res (2012) 72(7): 1844-52. [cited by applicant]
Van Tendeloo et al., “High-level transgene expression in primary human T lymphocytes and adult bone marrow CD34+ cells via electroporation-mediated gene delivery,” Gene Therapy (2000) 7(16): 1431-1437. [cited by applicant]
Verhoeyen et al., “Lentiviral vector gene transfer into human T cells,” Methods Mol Biol. (2009) 506: 97-114. [cited by applicant]
Wang et al., “Glycan-based diagnostic devices: current progress, challenges and perspectives.” Chem Commun (Camb). (2015) 51(94): 16750-16762. [cited by applicant]
Wang et al., “Phenotypic and Functional Attributes of Lentivirus Modified CD19-specific Human CD8+ Central Memory T Cells Manufactured at Clinical Scale,” J Immunother. (2012) 35(9):689-701. [cited by applicant]
Wu et al., “Adoptive T-cell therapy using autologous tumor-infiltrating lymphocytes for metastatic melanoma: current status and future outlook,” Cancer (2012) 18(2): 160-175. [cited by applicant]
Wulfing et al., “Correctly Folded T-cell Receptor Fragments in the Periplasm of [cited by applicant]
Yang et al., “Quantitative glycome analysis of N-glycan patterns in bladder cancer vs normal bladder cells using an integrated strategy.” J Proteome Res. (2015) 14(2): 639-653. [cited by applicant]
Zhang et al., “Discovery of specific metastasis-related N-glycan alterations in epithelial ovarian cancer based on quantitative glycomics.” PLoS One. (2014) 9(2): e87978. [cited by applicant]
Everest-Dass et al., “N-glycan MALDI Imaging Mass Spectrometry on Formalin-Fixed Paraffin-Embedded Tissue Enables the Delineation of Ovarian Cancer Tissues”, Molecular & Cellular Proteomics (Sep. 2016), vol. 15, Issue 9… [cited by applicant]
Nunomura et al., “Cell Surface Labeling and Mass Spectrometry Reveal Diversity of Cell Surface Markers and Signaling Molecules Expressed in Undifferentiated Mouse Embryonic Stem Cells,” Molecular & Cellular Proteomics (… [cited by applicant]