7KDD

HCMV postfusion gB in complex with SM5-1 Fab

Summary for 7KDD

• Entry DOI: 10.2210/pdb7kdd/pdb
• EMDB information: 22819
• Descriptor: Envelope glycoprotein B, SM5-1 Fab antibody heavy chain, SM5-1 Fab antibody light chain, ... (5 entities in total)
• Functional Keywords: fusogen, postfusion, hcmv, gb, antibody, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 9
• Total formula weight: 463398.34

Authors

Liu, Y.,Heim, P.K.,Che, Y.,Chi, X.,Qiu, X.,Han, S.,Dormitzer, P.R.,Yang, X. (deposition date: 2020-10-08, release date: 2021-03-17, Last modification date: 2024-11-20)

Primary citation

Liu, Y.,Heim, K.P.,Che, Y.,Chi, X.,Qiu, X.,Han, S.,Dormitzer, P.R.,Yang, X.
Prefusion structure of human cytomegalovirus glycoprotein B and structural basis for membrane fusion.
Sci Adv, 7:-, 2021

PubMed Abstract: Human cytomegalovirus (HCMV) causes congenital disease with long-term morbidity. HCMV glycoprotein B (gB) transitions irreversibly from a metastable prefusion to a stable postfusion conformation to fuse the viral envelope with a host cell membrane during entry. We stabilized prefusion gB on the virion with a fusion inhibitor and a chemical cross-linker, extracted and purified it, and then determined its structure to 3.6-Å resolution by electron cryomicroscopy. Our results revealed the structural rearrangements that mediate membrane fusion and details of the interactions among the fusion loops, the membrane-proximal region, transmembrane domain, and bound fusion inhibitor that stabilized gB in the prefusion state. The structure rationalizes known gB antigenic sites. By analogy to successful vaccine antigen engineering approaches for other viral pathogens, the high-resolution prefusion gB structure provides a basis to develop stabilized prefusion gB HCMV vaccine antigens.

PubMed: 33674318
DOI: 10.1126/sciadv.abf3178

Experimental method

ELECTRON MICROSCOPY (3.5 Å)