Article
A new cysteine in rotavirus VP4 participates in the formation of an alternate disulfide bond.
The Journal of general virology - 1 Nov 1998
Cuadras M A, Méndez E, Arias C F, López S
Abstract excerpt
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...
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