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United States Department of Agriculture

Agricultural Research Service

Title: Detailed Computational Anaylsis of a Comprehensive Set of Group a Rotavirus Nsp4 Proteins

Authors
item Lin, Shuo Liang - WYETH, PEARL RIVER, NJ
item Tian, Peng

Submitted to: Virus Genes
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: February 27, 2003
Publication Date: April 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.

Last Modified: 11/20/2014
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