5W3E

CryoEM structure of rhinovirus B14 in complex with C5 Fab (33 degrees Celsius, molar ratio 1:3, full particle)

Summary for 5W3E

• Entry DOI: 10.2210/pdb5w3e/pdb
• EMDB information: 8754 8761 8762 8763
• Descriptor: C5 antibody variable heavy domain, C5 antibody variable light domain, viral protein 1, ... (7 entities in total)
• Functional Keywords: virus, antibody, virus-immune system complex, virus/immune system
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 6
• Total formula weight: 117369.02

Authors

Liu, Y.,Dong, Y.,Rossmann, M.G. (deposition date: 2017-06-07, release date: 2017-07-12, Last modification date: 2024-10-16)

Primary citation

Dong, Y.,Liu, Y.,Jiang, W.,Smith, T.J.,Xu, Z.,Rossmann, M.G.
Antibody-induced uncoating of human rhinovirus B14.
Proc. Natl. Acad. Sci. U.S.A., 114:8017-8022, 2017

PubMed Abstract: Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 Å and 3.0 Å resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody-virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

PubMed: 28696310
DOI: 10.1073/pnas.1707369114

Experimental method

ELECTRON MICROSCOPY (2.53 Å)