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Nectin-like interactions between poliovirus and its receptor trigger conformational changes associated with cell entry.


ABSTRACT:

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Poliovirus infection is initiated by attachment to a receptor on the cell surface called Pvr or CD155. At physiological temperatures, the receptor catalyzes an irreversible expansion of the virus to form an expanded form of the capsid called the 135S particle. This expansion results in the externalization of the myristoylated capsid protein VP4 and the N-terminal extension of the capsid protein VP1, both of which become inserted into the cell membrane. Structures of the expanded forms of poliovirus and of several related viruses have recently been reported. However, until now, it has been unclear how receptor binding triggers viral expansion at physiological temperature. Here, we report poliovirus in complex with an enzymatically partially deglycosylated form of the 3-do

SUBMITTER: Strauss M 

PROVIDER: S-EPMC4442392 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature