English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Cryo-electron Microscopy Structures of Expanded Poliovirus with VHHs Sample the Conformational Repertoire of the Expanded State

Strauss, M., Schotte, L., Karunatilaka, K. S., Filman, D. J., & Hogle, J. M. (2017). Cryo-electron Microscopy Structures of Expanded Poliovirus with VHHs Sample the Conformational Repertoire of the Expanded State. Journal of Virology, 91(3): e01443-16. doi:10.1128/JVI.01443-16.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-ED7E-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-ED7F-8
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Strauss, Mike1, Author              
Schotte, Lise2, Author
Karunatilaka, Krishanthi S.2, Author
Filman, David J.2, Author
Hogle, James M.2, Author
Affiliations:
1Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              
2external, ou_persistent22              

Content

show
hide
Free keywords: EM STRUCTURE DETERMINATION; DOMAIN ANTIBODY FRAGMENTS; CELL ENTRY; CRYO-EM; ELECTRON-MICROSCOPY; 135S PARTICLES; RESOLUTION; RECEPTOR; INTERMEDIATE; MUTANTSVirology; 80S; VHH; cryo-electron microscopy; expanded virus; poliovirus; single-domain antibodies; three-dimensional structure;
 Abstract: By using cryo-electron microscopy, expanded 80S-like poliovirus virions (poliovirions) were visualized in complexes with four 80S-specific camelid VHHs (Nanobodies). In all four complexes, the VHHs bind to a site on the top surface of the capsid protein VP3, which is hidden in the native virus. Interestingly, although the four VHHs bind to the same site, the structures of the expanded virus differ in detail in each complex, suggesting that each of the Nanobodies has sampled a range of low-energy structures available to the expanded virion. By stabilizing unique structures of expanded virions, VHH binding permitted a more detailed view of the virus structure than was previously possible, leading to a better understanding of the expansion process that is a critical step in infection. It is now clear which polypeptide chains become disordered and which become rearranged. The higher resolution of these structures also revealed well-ordered conformations for the EF loop of VP2, the GH loop of VP3, and the N-terminal extensions of VP1 and VP2, which, in retrospect, were present in lower-resolution structures but not recognized. These structural observations help to explain preexisting mutational data and provide insights into several other stages of the poliovirus life cycle, including the mechanism of receptor-triggered virus expansion. IMPORTANCE When poliovirus infects a cell, it undergoes a change in its structure in order to pass RNA through its protein coat, but this altered state is short-lived and thus poorly understood. The structures of poliovirus bound to single-domain antibodies presented here capture the altered virus in what appear to be intermediate states. A careful analysis of these structures lets us better understand the molecular mechanism of infection and how these changes in the virus lead to productive-infection events.

Details

show
hide
Language(s): eng - English
 Dates: 20172017-02
 Publication Status: Published in print
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000393194600006
DOI: 10.1128/JVI.01443-16
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Virology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: American Society for Microbiology (ASM)
Pages: - Volume / Issue: 91 (3) Sequence Number: e01443-16 Start / End Page: - Identifier: ISSN: 0022-538X
CoNE: https://pure.mpg.de/cone/journals/resource/954925419045