Interaction between respiratory syncytial virus and glycosaminoglycans, including heparan sulfate.
Identifieur interne : 001E18 ( PubMed/Curation ); précédent : 001E17; suivant : 001E19Interaction between respiratory syncytial virus and glycosaminoglycans, including heparan sulfate.
Auteurs : Louay K. Hallak [États-Unis] ; Steven A. Kwilas ; Mark E. PeeplesSource :
- Methods in molecular biology (Clifton, N.J.) [ 1064-3745 ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Protéines membranaires, Protéoglycanes à sulfate d'héparane, Virus du SRAS.
- Animaux, Cellules CHO, Cricetinae, Cricetulus, Humains.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Heparan Sulfate Proteoglycans, Membrane Proteins.
- metabolism : SARS Virus.
- Animals, CHO Cells, Cricetinae, Cricetulus, Humans.
Abstract
Glycosaminoglycans (GAGs), including heparan sulfate (HS), are expressed on the surface of nearly all cells, linked to transmembrane proteins. These GAGs are sulfated to varying extents, lending a negative charge, and are used by a large number of viruses to initiate infection of immortalized cell lines. Here we describe the rationale and methods for analyzing GAG usage by one such virus, respiratory syncytial virus (RSV). The protocols presented allow the determination of which GAG(s) is employed by the virus, which GAG modification(s) is important, and whether the important GAG is on the cell or on the virus. We also discuss the finding that many viruses are selected for GAG usage during passage in culture and present a method for rapidly determining whether GAG usage is characteristic of a wild virus or is limited to laboratory-adapted virus.
DOI: 10.1007/978-1-59745-393-6_2
PubMed: 17502668
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Hallak</name><affiliation wicri:level="1"><nlm:affiliation>Center for Vaccines and Immunity, Columbus Children's Research Institute, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Vaccines and Immunity, Columbus Children's Research Institute, OH</wicri:regionArea></affiliation></author><author><name sortKey="Kwilas, Steven A" sort="Kwilas, Steven A" uniqKey="Kwilas S" first="Steven A" last="Kwilas">Steven A. Kwilas</name></author><author><name sortKey="Peeples, Mark E" sort="Peeples, Mark E" uniqKey="Peeples M" first="Mark E" last="Peeples">Mark E. Peeples</name></author></analytic><series><title level="j">Methods in molecular biology (Clifton, N.J.)</title><idno type="ISSN">1064-3745</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>CHO Cells</term><term>Cricetinae</term><term>Cricetulus</term><term>Heparan Sulfate Proteoglycans (metabolism)</term><term>Humans</term><term>Membrane Proteins (metabolism)</term><term>SARS Virus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules CHO</term><term>Cricetinae</term><term>Cricetulus</term><term>Humains</term><term>Protéines membranaires (métabolisme)</term><term>Protéoglycanes à sulfate d'héparane (métabolisme)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Heparan Sulfate Proteoglycans</term><term>Membrane Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines membranaires</term><term>Protéoglycanes à sulfate d'héparane</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>CHO Cells</term><term>Cricetinae</term><term>Cricetulus</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules CHO</term><term>Cricetinae</term><term>Cricetulus</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glycosaminoglycans (GAGs), including heparan sulfate (HS), are expressed on the surface of nearly all cells, linked to transmembrane proteins. These GAGs are sulfated to varying extents, lending a negative charge, and are used by a large number of viruses to initiate infection of immortalized cell lines. Here we describe the rationale and methods for analyzing GAG usage by one such virus, respiratory syncytial virus (RSV). The protocols presented allow the determination of which GAG(s) is employed by the virus, which GAG modification(s) is important, and whether the important GAG is on the cell or on the virus. We also discuss the finding that many viruses are selected for GAG usage during passage in culture and present a method for rapidly determining whether GAG usage is characteristic of a wild virus or is limited to laboratory-adapted virus.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17502668</PMID><DateCompleted><Year>2007</Year><Month>06</Month><Day>13</Day></DateCompleted><DateRevised><Year>2007</Year><Month>12</Month><Day>03</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1064-3745</ISSN><JournalIssue CitedMedium="Print"><Volume>379</Volume><PubDate><Year>2007</Year></PubDate></JournalIssue><Title>Methods in molecular biology (Clifton, N.J.)</Title><ISOAbbreviation>Methods Mol. 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