+Search query
-Structure paper
Title | Antibody-induced uncoating of human rhinovirus B14. |
---|---|
Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 114, Issue 30, Page 8017-8022, Year 2017 |
Publish date | Jul 25, 2017 |
![]() | Yangchao Dong / Yue Liu / Wen Jiang / Thomas J Smith / Zhikai Xu / Michael G Rossmann / ![]() ![]() |
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) ...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. |
![]() | ![]() ![]() ![]() |
Methods | EM (single particle) |
Resolution | 2.26 - 3.01 Å |
Structure data | EMDB-8754, PDB-5w3e: EMDB-8761, PDB-5w3l: |
Chemicals | ![]() ChemComp-HOH: |
Source |
|
![]() | VIRUS/IMMUNE SYSTEM / ![]() ![]() |