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The structure of the poliovirus 135S cell entry intermediate at 10-Angstrom resolution reveals the location of an externalized polypeptide that binds to membranes

Abstract:

Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational change to the 135S cell entry intermediate. This transition involves shifts of the capsid protein β barrels, accompanied by the externalization of VP4 and the N terminus of VP1. Both polypeptides associate with membranes and are postulated to facilitate entry by forming a translocation pore for the vir...

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Publication status:
Published

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Publisher copy:
10.1128/JVI.79.12.7745.7755

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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Journal:
JOURNAL OF VIROLOGY
Volume:
79
Issue:
12
Pages:
7745-7755
Publication date:
2005-06-05
DOI:
ISSN:
0022-538X
URN:
uuid:0fbbaa1d-c886-4b2d-ae3f-47903a6d88f5
Source identifiers:
39492
Local pid:
pubs:39492
Language:
English

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