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Virus Res. 1996 Dec;46(1-2):19-29.

Assembly of the reovirus outer capsid requires mu 1/sigma 3 interactions which are prevented by misfolded sigma 3 protein in temperature-sensitive mutant tsG453.

Author information

1
Department of Medical Microbiology and Infectious Diseases, University of Manitoba, Winnipeg, Canada.

Abstract

A temperature-sensitive reovirus mutant, tsG453, whose defect was mapped to major outer capsid protein sigma 3, makes core particles but fails to assemble the outer capsid around the core at non-permissive temperature. Previous studies that made use of electron cryo-microscopy and image reconstructions showed that mu 1, the other major outer capsid protein, but not sigma 3, interact extensively with the core capsid. Although wild-type sigma 3 and mu 1 interact with each other, immunocoprecipitation studies showed that mutant sigma 3 protein was incapable of interacting with mu 1 at the non-permissive temperature. In addition, restrictively-grown mutant sigma 3 protein could not be precipitated by some sigma 3-specific monoclonal antibodies. These observations suggest that in a wild-type infection, specific sigma 3 and mu 1 interactions result in changes in mu 1 conformation which are required to allow mu 1/sigma 3 complexes to condense onto the core capsid shell during outer capsid assembly, and that sigma 3 in non-permissive tsG453 infections is misfolded such that it cannot interact with mu 1.

PMID:
9029774
DOI:
10.1016/s0168-1702(96)01372-x
[Indexed for MEDLINE]

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