IP Library › Granted Patent US 12,384,819
Granted Patent B2
US 12,384,819 · App. 18/435,026 · Granted Aug 12, 2025

Modified cytomegalovirus proteins and stabilized complexes

Inventors: Enrico Malito (Rockville, MD); Matthew James Bottomley (Rockville, MD); Andrea Carfi (Cambridge, MA); Sumana Chandramouli (Rockville, MD); Kate Luisi (Rockville, MD)
Assignee: GLAXOSMITHKLINE BIOLOGICALS SA
C07K14/045A61K39/245A61K38/00
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Quick Facts
Patent No.
US 12,384,819
App. No.
18/435,026
Granted
Aug 12, 2025
Kind
B2
Abstract

Described are mutant human cytomegalovirus (HCMV) pentamer complex polypeptides, methods of making them, and their use in HCMV protein complexes and compositions. In particular, the use of the modified HCMV polypeptides to stabilize HCMV complexes or unmask a pentamer epitope is described.

Claims (14)

1. A Human Cytomegalovirus (HCMV) polypeptide comprising a mutant glycoprotein L (gL), wherein the mutant gL comprises a substitution mutation at one or more of the amino acid residues H177, G224, G140, G145, D146, G218, L119, C233 and P272, relative to the sequence set forth in SEQ ID NO: 7, or at a corresponding position in other HCMV gL polypeptides, wherein the residues are substituted with an amino acid selected from the group consisting of tryptophan (W), phenylalanine (F), tyrosine (Y), and leucine (L).

2. The HCMV polypeptide of claim 1 further comprising one or more hydrophobic mutations.

3. A Human Cytomegalovirus (HCMV) polypeptide comprising a mutant glycoprotein L (gL), wherein the mutant gL comprises:

(i) a substitution mutation at one or more of the amino acid residues H267, H236, H245, and G161 relative to the sequence set forth in SEQ ID NO: 7, or at a corresponding position in other HCMV gL polypeptides, wherein the residues are substituted with an amino acid selected from the group consisting of tryptophan (W), phenylalanine (F), methionine (M), cysteine (C), alanine (A), leucine (L), isoleucine (I), valine (V) and proline (P),

and (ii) a substitution mutation at amino acid residue C233 relative to the sequence set forth in SEQ ID NO: 7, or at a corresponding position in other HCMV gL polypeptides, wherein the amino acid residue is substituted with an amino acid selected from the group consisting of tryptophan (W), phenylalanine (F), methionine (M), alanine (A), leucine (L), isoleucine (I), valine (V) and proline (P).

4. A Human Cytomegalovirus (HCMV) polypeptide comprising a mutant glycoprotein L (gL), wherein the mutant gL comprises a substitution mutation at one or more of the amino acid residues G161, D163, G224, G218, R166, G140, R160, and A150, relative to the sequence set forth in SEQ ID NO: 7, or at a corresponding position in other HCMV gL polypeptides, wherein the residues are substituted with a cysteine (C).

5. A nucleic acid encoding the HCMV polypeptide of claim 1 .

6. An expression vector comprising the nucleic acid of claim 5 .

7. An isolated host cell comprising the nucleic acid of claim 5 .

8. An immunogenic composition comprising the polypeptide of claim 1 .

9. The immunogenic composition of claim 8 , further comprising a non-antigen component.

10. The immunogenic composition of claim 9 , wherein the non-antigen component is an immunologically effective amount of an adjuvant.

11. A method of inducing an immune response against Human Cytomegalovirus (HCMV), comprising administering to a subject an immunologically effective amount of the immunogenic composition of claim 8 .

12. A method of inhibiting Human Cytomegalovirus (HCMV) entry into a cell comprising contacting the cell with the polypeptide of claim 1 .

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 7, 2024
From: MALITO, ENRICO; BOTTOMLEY, MATTHEW JAMES; CARFI, ANDREA; CHANDRAMOULI, SUMANA
To: GLAXOSMITHKLINE BIOLOGICALS SA
Reel/Frame 066402/0673 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 7, 2024
From: LUISI, KATE
To: GLAXOSMITHKLINE BIOLOGICALS SA
Reel/Frame 066402/0822 →
Continuity (4)
Continuation 17223207 · Apr 6, 2021
Continuation PCTIB2019058777 · Oct 15, 2019
Provisional Application 62746804 · Oct 17, 2018
Related Publication 20240383949A1 · Nov 21, 2024
References Cited (22)
US 9683022B2 · Carfi et al. · 2017 [cited by applicant]
US 10064935B2 · Ciaramella et al. · 2018 [cited by applicant]
US 10111945B2 · Orlinger et al. · 2018 [cited by applicant]
JP 2003509013A · 2003 [cited by applicant]
WO 0100648A1 · 2000 [cited by applicant]
WO 2015181142A1 · 2015 [cited by applicant]
WO 2016116904A1 · 2016 [cited by applicant]
WO 2018182983A1 · 2018 [cited by applicant]
Ciferri C, Chandramouli S, Donnarumma D, Nikitin PA, Cianfrocco MA, Gerrein R, Feire AL, Barnett SW, et. al. Structural and biochemical studies of HCMV gH/gL/gO and Pentamer reveal mutually exclusive cell entry complexe… [cited by examiner]
Ohman MS, Albright ER, Gelbmann CB, Kalejta RF. The Pentamer glycoprotein complex inhibits viral Immediate Early transcription during Human Cytomegalovirus infections. Proc Natl Acad Sci U S A. Sep. 24, 2024;121(39):e24… [cited by examiner]
Hofmann I, Wen Y, Ciferri C, Schulze A, Fühner V, Leong M, Gerber A, Gerrein R, Nandi A, Lilja AE, Carfi A, Laux H. Expression of the human cytomegalovirus pentamer complex for vaccine use in a CHO system. Biotechnol Bi… [cited by examiner]
Schultz EP, Lanchy JM, Ellerbeck EE, Ryckman BJ. Scanning Mutagenesis of Human Cytomegalovirus Glycoprotein gH/gL. J Virol. Dec. 9, 2015;90(5):2294-305. (Year: 2015). [cited by examiner]
Schultz EP, Yu Q, Stegmann C, Day LZ, Lanchy JM, Ryckman BJ. Mutagenesis of Human Cytomegalovirus Glycoprotein L Disproportionately Disrupts gH/gL/gO over gH/gL/pUL128-131. J Virol. Aug. 10, 2021;95(17):e0061221. doi: 1… [cited by examiner]
Hollingsworth SA, Dror RO. Molecular Dynamics Simulation for All. Neuron. Sep. 19, 2018;99(6):1129-1143. (Year: 2018). [cited by examiner]
Kuhlman B, Bradley P. Advances in protein structure prediction and design. Nat Rev Mol Cell Biol. Nov. 2019;20(11):681-697. Epub Aug. 15, 2019. (Year: 2019). [cited by examiner]
Saharkhiz S, Mostafavi M, Birashk A, Karimian S, Khalilollah S, Jaferian S, Yazdani Y, Alipourfard I, Huh YS, Farani MR, Akhavan-Sigari R. The State-of-the-Art Overview to Application of Deep Learning in Accurate Protei… [cited by examiner]
Office Action in corresponding Japanese Patent Application No. 2021-521000, mailed Oct. 3, 2023 (2 pages). [cited by applicant]
International Search Report and Written Report for corresponding International Application No. PCT/IB2019/058777, mailed Dec. 10, 2019 (11 pages). [cited by applicant]
Chandramouli S, Malito E, Nguyen T, Luisi K, Donnarumma D, Xing Y, Norais N, Yu D, Carfi A. Structural basis for potent antibody-mediated neutralization of human cytomegalovirus. Sci Immunol. Jun. 30, 2017;2(12):eaan145… [cited by applicant]
Davey, et al., “Prediction of Stable Globular Proteins Using Negative Design with Non-native Backbone Ensembles,” Structure, 23(11): 2011-2021 (2015). [cited by applicant]
Saito, et al., “Cavity-Filling Mutations Enhance Protein Stability by Lowering the Free Energy of Native,” J. Phys. Chem. Part B., 104(15): 3705-3711 (2000). [cited by applicant]
Sung, et al., “Update on the current status of cytomegalovirus vaccines”, Expert Review of Vaccines, 9(11):1303-1314 (2010). [cited by applicant]