Journal of General Virology, Vol 79, 2673-2677, Copyright © 1998 by Society for General Microbiology

ARTICLES

A new cysteine in rotavirus VP4 participates in the formation of an alternate disulfide bond

MA Cuadras, E Mendez, CF Arias and S Lopez
Departamento de Genetica y Fisiologia Molecular, Instituto de Biotecnologia, Universidad Nacional Autonoma de Mexico, Cuernavaca, Morelos.

Most animal rotaviruses bind to a cell surface molecule that contains sialic acid (SA). We have recently isolated variants from simian rotavirus RRV which show an SA-independent phenotype. The VP4 protein of these variants was shown to have three amino acid changes with respect to the wt protein, one of them being Tyr-267 --> Cys. In this work, we have investigated whether the new cysteine could interfere with the disulfide bond (Cys-318/Cys-380) present in the VP5* subunit of the wt protein. Cysteine residues 318 and 380 were mutagenized in gpr8 and RRV VP4 genes, and the wt and mutant genes were transcribed and translated in vitro. The protein products were analysed by electrophoresis under reducing and non-reducing conditions. This approach showed that, in the VP4 protein synthesized in vitro, Cys-267 is capable of forming an alternate disulfide bond with Cys-318. This alternate bond also seems to occur in the VP4 protein present in the variant gpr8 virus particles.

This article has been cited by other articles:

				S. Zárate, R. Espinosa, P. Romero, E. Méndez, C. F. Arias, and S. López The VP5 Domain of VP4 Can Mediate Attachment of Rotaviruses to Cells J. Virol., January 1, 2000; 74(2): 593 - 599. [Abstract] [Full Text]