C-terminal Arginine Cluster is Essential for Receptor Binding of Norovirus Capsid Protein.
From: Division of Infectious Diseases, Cincinnati Children’s Hospital Medical Center, 3333 Burnet Avenue, Cincinnati, OH 45229-3039, USA.
Journal of virology
- Publish Date: Aug 2006
- ISSN: 0022-538X
- Volume: 80
- Issue: 15
- Pages: 7322-31
- Medium: Print
- Language: English
- Citation (JAMA): Tan Ming, Meller Jarek, Jiang Xi, et al. C-terminal Arginine Cluster is Essential for Receptor Binding of Norovirus Capsid Protein.. J. Virol. Aug 2006;80:7322-31
Abstract
Noroviruses are the major viral pathogens of epidemic acute gastroenteritis affecting people worldwide. They have been found to recognize human histo-blood group antigens as receptors. The P domain of norovirus capsid protein was found to be responsible for binding to viral receptors, and the recombinant P protein forms P dimers and P particles in vitro. In this study, we demonstrate that a highly conserved arginine (R) cluster at the C terminus of the P domain is critical for receptor binding and P particle formation of the P proteins. Deletions of the R cluster abolished these functions. Replacement of the R cluster with histidines (another positively charged amino acid) resulted in low efficiency of receptor binding and P particle formation, while replacement with alanines led to loss of both functions completely. The R cluster also contains a highly conserved trypsin digestion site. A treatment of capsid protein or P domain mutants from both genogroup I (Norwalk virus) and genogroup II (VA387) noroviruses with trypsin resulted in a removal of the R cluster and the S domain, leaving a P polypeptide of 31.3 kDa (Norwalk virus) or 34.3 kDa (VA387), similar to the soluble P protein found in vivo. Our findings imply that the proteolytic process could be a necessary step for norovirus replication in the host.
Mesh Headings (Keywords): Animals, Arginine, Capsid Proteins, Dimerization, Humans, Mutation, Norovirus, Peptide Fragments, Protein Binding, Protein Structure, Tertiary, Receptors, Virus, Recombinant Proteins, Saliva, Spectrometry, Mass, Electrospray Ionization, Spodoptera, Virion
Check for Full Text / PubMed Unique Identifier (PMID): 16840313
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