Author
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LIN, SHUO LIANG - WYETH, PEARL RIVER, NJ |
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Tian, Peng |
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Submitted to: Virus Genes
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 2/27/2003 Publication Date: 4/20/2003 Citation: Lin, S., Tian, P. 2003 Detailed computational anaylsis of a comprehensive set of group a rotavirus nsp4 proteins. Virus Genes. v.26(3) p. 271-282 Interpretive Summary: Rotavirus infection causes diarrhea to human, animals and birds. The NSP4 protein of Group A rotavirus has been recognized as a viral enterotoxin. Our analysis of 176 NSP4 proteins in Groups A, B and C rotaviruses confirms that the recently published avian NSP4 sequences belong to a new genotype, besides the four known NSP4 genotypes of Group A mammalian rotaviruses. Significant differences are found in the physicochemical properties between the avian and mammalian NSP4 proteins. In particular, lack of a highly probable coiled-coil region in the avian sequences implies a diversion of the NSP4 quaternary structure from the latter, although the secondary and tertiary structures may remain close. Fourteen amino acids are found absolutely conserved in the Group A NSP4 sequences, regardless of genotype. Of the conserved residues, two are glycosylation sites, one is in the middle of the transmembrane segment, seven span the VP4 binding domain, and five are clustered in the middle of the toxic peptide region, indicating the functional importance of the conservation. Technical Abstract: Rotavirus infection causes diarrhea to human, animals and birds. The NSP4 protein of Group A rotavirus has been recognized as a viral enterotoxin. Our analysis of 176 NSP4 proteins in Groups A, B and C rotaviruses confirms that the recently published avian NSP4 sequences belong to a new genotype, besides the four known NSP4 genotypes of Group A mammalian rotaviruses. Significant differences are found in the physicochemical properties between the avian and mammalian NSP4 proteins. In particular, lack of a highly probable coiled-coil region in the avian sequences implies a diversion of the NSP4 quaternary structure from the latter, although the secondary and tertiary structures may remain close. Fourteen amino acids are found absolutely conserved in the Group A NSP4 sequences, regardless of genotype. Of the conserved residues, two are glycosylation sites, one is in the middle of the transmembrane segment, seven span the VP4 binding domain, and five are clustered in the middle of the toxic peptide region, indicating the functional importance of the conservation. |
