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J. Virol., Jan 1997, 59-64, Vol 71, No. 1
J Martinez-Costas, A Grande, R Varela, C Garcia-Martinez and J Benavente
There are a number of discrepancies in the literature regarding the protein
composition of the avian reoviruses. The present study demonstrates that
avian reovirus S1133 contains at least 10 proteins (lambdaA, lambdaB,
lambdaC, muA, muB, muBC, muBN, sigmaA, sigmaB, and sigmaC). Polypeptides
muB, muBC, muBN, sigmaB, and sigmaC are components of the outer capsid
layer of the virus, while lambdaA, lambdaB, muA, and sigmaA are core
polypeptides. Protein lambdaC is a component of both layers, extending from
the inner core to the outer capsid. The minor outer-capsid polypeptide
sigmaC is shown to be the cell attachment protein, since it is the only
viral polypeptide present in extracts of S1133-infected cells that binds
specifically to chicken embryo fibroblasts; furthermore, its binding to
avian cells was competitively inhibited by S1133 reovirions but not by
mammalian reovirions. Our results also show that sigmaC is an oligomeric
protein both in the virion and free in the cytoplasm, and preliminary
results suggest that the multimer is made up of three monomeric units.
Copyright © 1997, American Society for Microbiology
Protein architecture of avian reovirus S1133 and identification of the cell attachment protein
Departamento de Bioquimica y Biologia Molecular, Facultad de Farmacia,University of Santiago, Spain.
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