Linked Life Data

11811686

Source:http://linkedlifedata.com/resource/pubmed/id/11811686

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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2002-1-28
pubmed:abstractText
In order to study structural associations, RSV surface glycoproteins were evaluated using heparin agarose affinity chromatography (HAAC). When RSV-infected cell lysate was analyzed by HAAC, all three surface glycoproteins, (F, G and SH), were eluted. Similarly, when separate lysates from Vero cells infected with vaccinia recombinants expressing F (vvF), G (vvG) and SH (vvSH) proteins were subjected to HAAC, only vvF and vvG expressed proteins bound to heparin, whereas vvSH expressed protein did not bind. When lysates from vvF, vvG and vvSH-infected Vero cells were mixed prior to HAAC, only F and G bound heparin. In contrast, following co-infection of Vero cells with vvF, vvG and vvSH, all three proteins were detected subsequent to HAAC. Following HAAC of A2-infected cell lysate and lysate from vvF, vvG and vvSH co-infected Vero cells, two high molecular weight complexes of 175 Kd and 210 Kd, respectively, were identified that reacted with anti-F, anti-G and anti-SH antisera. In addition, anti-SH antiserum was able to co-precipitate RSV F, G and SH. Using HAAC and a NaCl step gradient we demonstrated that a fraction of RSV F, G and SH eluted at higher salt concentrations than either purified F or G protein. Taken together, these data suggest that RSV F, G and SH glycoproteins can form an oligomeric complex within infected cells and this complex has a higher affinity for heparin than either G or F protein alone.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0304-8608
pubmed:author
pubmed:issnType
Print
pubmed:volume
146
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2369-83
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Human respiratory syncytial virus surface glycoproteins F, G and SH form an oligomeric complex.
pubmed:affiliation
Food and Drug Administration, Center for Biologics Evaluation and Research, Laboratory of Pediatrics and Respiratory Viruses, Bethesda, Maryland 20852-1448, USA.
pubmed:publicationType
Journal Article