Document Detail


Structural basis of rotavirus strain preference toward N-acetyl- or N-glycolylneuraminic acid-containing receptors.
MedLine Citation:
PMID:  23035213     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The rotavirus spike protein domain VP8* is essential for recognition of cell surface carbohydrate receptors, notably those incorporating N-acylneuraminic acids (members of the sialic acid family). N-Acetylneuraminic acids occur naturally in both animals and humans, whereas N-glycolylneuraminic acids are acquired only through dietary uptake in normal human tissues. The preference of animal rotaviruses for these natural N-acylneuraminic acids has not been comprehensively established, and detailed structural information regarding the interactions of different rotaviruses with N-glycolylneuraminic acids is lacking. In this study, distinct specificities of VP8* for N-acetyl- and N-glycolylneuraminic acids were revealed using biophysical techniques. VP8* protein from the porcine rotavirus CRW-8 and the bovine rotavirus Nebraska calf diarrhea virus (NCDV) showed a preference for N-glycolyl- over N-acetylneuraminic acids, in contrast to results obtained with rhesus rotavirus (RRV). Crystallographic structures of VP8* from CRW-8 and RRV with bound methyl-N-glycolylneuraminide revealed the atomic details of their interactions. We examined the influence of amino acid type at position 157, which is proximal to the ligand's N-acetyl or N-glycolyl moiety and can mutate upon cell culture adaptation. A structure-based hypothesis derived from these results could account for rotavirus discrimination between the N-acylneuraminic acid forms. Infectivity blockade experiments demonstrated that the determined carbohydrate specificities of these VP8* domains directly correlate with those of the corresponding infectious virus. This includes an association between CRW-8 adaption to cell culture, decreased competition by N-glycolylneuraminic acid for CRW-8 infectivity, and a Pro157-to-Ser157 mutation in VP8* that reduces binding affinity for N-glycolylneuraminic acid.
Authors:
Xing Yu; Vi T Dang; Fiona E Fleming; Mark von Itzstein; Barbara S Coulson; Helen Blanchard
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-10-03
Journal Detail:
Title:  Journal of virology     Volume:  86     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-20     Completed Date:  2013-01-28     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13456-66     Citation Subset:  IM    
Affiliation:
Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
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MeSH Terms
Descriptor/Qualifier:
Base Sequence
Calorimetry
Crystallography, X-Ray
DNA Primers
Flow Cytometry
Models, Molecular
Neuraminic Acids / chemistry,  metabolism*
Nuclear Magnetic Resonance, Biomolecular
Receptors, Virus / metabolism*
Rotavirus / physiology*
Sialic Acids / chemistry,  metabolism*
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Neuraminic Acids; 0/Receptors, Virus; 0/Sialic Acids; 1113-83-3/N-glycolylneuraminic acid
Comments/Corrections

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