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rdf:type |
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lifeskim:mentions |
umls-concept:C0019602,
umls-concept:C0043125,
umls-concept:C0178812,
umls-concept:C0220825,
umls-concept:C0237401,
umls-concept:C1512571,
umls-concept:C1550548,
umls-concept:C1555714,
umls-concept:C1611645,
umls-concept:C1705654,
umls-concept:C1707719,
umls-concept:C1709915
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pubmed:issue |
23
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pubmed:dateCreated |
2009-11-5
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pubmed:abstractText |
Histidine residues have been hypothesized to function as sensors of environmental pH that can trigger the activity of viral fusion proteins. We investigated a requirement for histidine residues in the envelope (E) protein of West Nile virus during pH-dependent entry into cells. Each histidine was individually replaced with a nonionizable amino acid and tested functionally. In each instance, mutants capable of orchestrating pH-dependent infection were identified. These results do not support a requirement for any single histidine as a pH-sensing "switch," and they suggest that additional features of the E protein are involved in triggering pH-dependent steps in the flavivirus life cycle.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-10725196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-11463384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-11893341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-12571240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-12829825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-14963486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-15564465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-15608696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16287688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16325883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16415006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16597822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16943291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16963734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-16987985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-17027497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-17301152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-17728239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-17936324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18005691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18208382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18464894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18596815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18776902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18801552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-18936253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-19096510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-19244325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-19386704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-2167941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-3944582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-4031825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-6086817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19776132-8480420
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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 |
Dec
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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 |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12631-5
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pubmed:dateRevised |
2010-9-28
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pubmed:meshHeading |
pubmed-meshheading:19776132-Amino Acid Substitution,
pubmed-meshheading:19776132-Cell Line,
pubmed-meshheading:19776132-Genes, Reporter,
pubmed-meshheading:19776132-Green Fluorescent Proteins,
pubmed-meshheading:19776132-Histidine,
pubmed-meshheading:19776132-Humans,
pubmed-meshheading:19776132-Hydrogen-Ion Concentration,
pubmed-meshheading:19776132-Models, Molecular,
pubmed-meshheading:19776132-Mutagenesis, Site-Directed,
pubmed-meshheading:19776132-Protein Structure, Tertiary,
pubmed-meshheading:19776132-Viral Envelope Proteins,
pubmed-meshheading:19776132-Virus Internalization,
pubmed-meshheading:19776132-West Nile virus
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pubmed:year |
2009
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pubmed:articleTitle |
Protonation of individual histidine residues is not required for the pH-dependent entry of west nile virus: evaluation of the "histidine switch" hypothesis.
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pubmed:affiliation |
Viral Pathogenesis Section, Laboratory of Viral Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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