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rdf:type |
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lifeskim:mentions |
umls-concept:C0006933,
umls-concept:C0205314,
umls-concept:C0370215,
umls-concept:C0679622,
umls-concept:C1160185,
umls-concept:C1412056,
umls-concept:C1514562,
umls-concept:C1521991,
umls-concept:C1564874,
umls-concept:C1880022,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
17
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pubmed:dateCreated |
2008-8-15
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pubmed:databankReference |
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pubmed:abstractText |
A new adeno-associated virus (AAV), referred to as AAV(VR-942), has been isolated as a contaminant of adenovirus strain simian virus 17. The sequence of the rep gene places it in the AAV serotype 2 (AAV2) complementation group, while the capsid is only 88% identical to that of AAV2. High-level AAV(VR-942) transduction activity requires cell surface heparan sulfate proteoglycans, although AAV(VR-942) lacks residues equivalent to the AAV2 R585 and R588 amino acid residues essential for mediating the interaction of AAV2 with the heparan sulfate proteoglycan receptor. Instead, AAV(VR-942) uses a distinct transduction region. This finding shows that distinct domains on different AAV isolates can be responsible for the same activities.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-10725206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-11413329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-11435568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-11752169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-12136130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-12768018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-14512555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-15088385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-15163731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-15163744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-16282478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-16409121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-16641301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-16699032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-16940521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-16943302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-9420229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-9445046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18524816-9882336
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1098-5514
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
82
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8911-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18524816-Amino Acid Sequence,
pubmed-meshheading:18524816-Amino Acids, Basic,
pubmed-meshheading:18524816-Animals,
pubmed-meshheading:18524816-COS Cells,
pubmed-meshheading:18524816-Capsid Proteins,
pubmed-meshheading:18524816-Cercopithecus aethiops,
pubmed-meshheading:18524816-Dependovirus,
pubmed-meshheading:18524816-Evolution, Molecular,
pubmed-meshheading:18524816-Green Fluorescent Proteins,
pubmed-meshheading:18524816-Heparan Sulfate Proteoglycans,
pubmed-meshheading:18524816-Models, Molecular,
pubmed-meshheading:18524816-Molecular Sequence Data,
pubmed-meshheading:18524816-Phylogeny,
pubmed-meshheading:18524816-Protein Structure, Tertiary,
pubmed-meshheading:18524816-Sequence Homology, Amino Acid,
pubmed-meshheading:18524816-Time Factors,
pubmed-meshheading:18524816-Transduction, Genetic
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pubmed:year |
2008
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pubmed:articleTitle |
Molecular characterization of the heparin-dependent transduction domain on the capsid of a novel adeno-associated virus isolate, AAV(VR-942).
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pubmed:affiliation |
Gene Therapy and Therapeutics Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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