Amino Acid Substitution Positions on the VP7 and NSP4 Molecules of Rotavirus Circulating in China

Rotavirus is the leading cause of severe diarrhea among infants and young children, and its outer capsid structural protein, VP7, stimulates the production of distinct neutralizing antibodies in the host and also determines the serotype of the virus strain. NSP4, the rotavirus nonstructural protein, plays a role in viral assembly and is becoming an attractive candidate for vaccine development. By using the Maximum likelihood method with codon-substitution models, amino acid substitutions on the VP7 and NSP4 protein-coding sequences of G1~G3 serotype rotavirus circulating in China are analyzed, and no amino acid site under positive selection in VP7 is found, but three amino acid sites under positive selection in NSP4 are detected. Since these sites are located in different functional sequence segments, we may draw a conclusion that these sites are crucial to related virus biological function, and should be paid much attention in developing vaccine.

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