| Structural basis of rotavirus strain preference toward N-acetyl- or N-glycolylneuraminic acid-containing receptors. | |
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MedLine Citation:
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PMID: 23035213 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Xing Yu; Vi T Dang; Fiona E Fleming; Mark von Itzstein; Barbara S Coulson; Helen Blanchard |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-10-03 |
Journal Detail:
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Title: Journal of virology Volume: 86 ISSN: 1098-5514 ISO Abbreviation: J. Virol. Publication Date: 2012 Dec |
Date Detail:
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Created Date: 2012-11-20 Completed Date: 2013-01-28 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 0113724 Medline TA: J Virol Country: United States |
Other Details:
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Languages: eng Pagination: 13456-66 Citation Subset: IM |
Affiliation:
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Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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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:
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0/DNA Primers; 0/Neuraminic Acids; 0/Receptors, Virus; 0/Sialic Acids; 1113-83-3/N-glycolylneuraminic acid |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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