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rdf:type |
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lifeskim:mentions |
umls-concept:C0015127,
umls-concept:C0019691,
umls-concept:C0019704,
umls-concept:C0021024,
umls-concept:C0026882,
umls-concept:C0031437,
umls-concept:C0205147,
umls-concept:C0205171,
umls-concept:C0205419,
umls-concept:C0525038,
umls-concept:C1314792,
umls-concept:C1720529,
umls-concept:C1948059
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pubmed:issue |
1
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pubmed:dateCreated |
1996-1-25
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pubmed:abstractText |
The second major cysteine loop of human immunodeficiency virus type 1 envelope glycoprotein gp120 contains 5 to 11 consensus N-linked glycosylation sites, which is disproportionately higher than the number of such sites found in other regions of gp120. Amino acid substitutions introduced at three of six N-linked glycosylation sites in this region of an infectious molecular clone, HXB2, resulted in severe impairment of virus infectivity. Isolation and genetic characterization of a revertant of this mutant revealed an isoleucine-for-valine substitution at position 84 in constant region 1 and an isoleucine-for-methionine substitution at position 434 in constant region 4. Further mutational analysis indicated that either isoleucine substitution was sufficient to confer the revertant phenotype. These findings demonstrate that V1/V2 not only functionally interacts with C4, as previously reported, but also interacts with C1. The observation that compensatory changes do not involve regeneration of N-linked glycosylation sites in the second major cysteine loop suggests that replication of human immunodeficiency virus type 1 in vitro is independent of the presence of a disproportionate number of N-linked glycosylation sites within this loop.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1100841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1279195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1281869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1347797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1438212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1527847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1548783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1549584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1703212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1920632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-1986308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2355006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2410792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2433466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2547987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2842694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2983217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2991896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2992084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-2997922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-3104797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-3257102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-3881765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-6095449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-6505693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7515975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7679751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7684463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7687303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7687306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7690418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7734192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7856100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7933065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-7983752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-8139010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-8139032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-8350416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-8497073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-8497077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523579-8502996
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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 |
Jan
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
607-11
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8523579-Amino Acid Sequence,
pubmed-meshheading:8523579-Animals,
pubmed-meshheading:8523579-Base Sequence,
pubmed-meshheading:8523579-Binding Sites,
pubmed-meshheading:8523579-Cell Line,
pubmed-meshheading:8523579-Cloning, Molecular,
pubmed-meshheading:8523579-DNA Primers,
pubmed-meshheading:8523579-Genetic Variation,
pubmed-meshheading:8523579-Glycosylation,
pubmed-meshheading:8523579-HIV Envelope Protein gp120,
pubmed-meshheading:8523579-HIV-1,
pubmed-meshheading:8523579-Humans,
pubmed-meshheading:8523579-Molecular Sequence Data,
pubmed-meshheading:8523579-Mutagenesis, Site-Directed,
pubmed-meshheading:8523579-Mutation,
pubmed-meshheading:8523579-Phenotype
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pubmed:year |
1996
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pubmed:articleTitle |
Single amino acid substitution in constant region 1 or 4 of gp120 causes the phenotype of a human immunodeficiency virus type 1 variant with mutations in hypervariable regions 1 and 2 to revert.
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pubmed:affiliation |
Department of Cancer Biology, Harvard School of Public Health, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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