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rdf:type |
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lifeskim:mentions |
umls-concept:C0019704,
umls-concept:C0028778,
umls-concept:C0042760,
umls-concept:C0205171,
umls-concept:C0205369,
umls-concept:C0243126,
umls-concept:C0331858,
umls-concept:C0332206,
umls-concept:C0525038,
umls-concept:C1422036,
umls-concept:C1511625,
umls-concept:C1704640,
umls-concept:C1706515
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pubmed:issue |
3
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pubmed:dateCreated |
1995-3-13
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pubmed:abstractText |
Incorporation of envelope glycoproteins into a budding retrovirus is an essential step in the formation of an infectious virus particle. By using site-directed mutagenesis, we identified specific amino acid residues in the matrix domain of the human immunodeficiency virus type 1 (HIV-1) Gag protein that are critical to the incorporation of HIV-1 envelope glycoproteins into virus particles. Pseudotyping analyses were used to demonstrate that two heterologous envelope glycoproteins with short cytoplasmic tails (the envelope of the amphotropic murine leukemia virus and a naturally truncated HIV-2 envelope) are efficiently incorporated into HIV-1 particles bearing the matrix mutations. Furthermore, deletion of the cytoplasmic tail of HIV-1 transmembrane envelope glycoprotein gp41 from 150 to 7 or 47 residues reversed the incorporation block imposed by the matrix mutations. These results suggest the existence of a specific functional interaction between the HIV-1 matrix and the gp41 cytoplasmic tail.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1357190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1501283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1501299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1548759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1583717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1604808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1629961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1652977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1691314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1729720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1845882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-1883539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2072454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2164597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2170021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2305256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2386620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2405382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2421920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2425430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2677400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2677749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2778881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2795718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2823148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2836951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-2849111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-3031510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-3041017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-3257102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-3261862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-6190011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-6304351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-6325711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-7693966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8030287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8035531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8065455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8105392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8107229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8139032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8151785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8207836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8411340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8416370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8474176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7853546-8497044
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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 |
Mar
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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 |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1984-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7853546-Cytoplasm,
pubmed-meshheading:7853546-Gene Products, gag,
pubmed-meshheading:7853546-HIV Envelope Protein gp41,
pubmed-meshheading:7853546-HIV-1,
pubmed-meshheading:7853546-HIV-2,
pubmed-meshheading:7853546-HeLa Cells,
pubmed-meshheading:7853546-Humans,
pubmed-meshheading:7853546-Leukemia Virus, Murine,
pubmed-meshheading:7853546-Morphogenesis,
pubmed-meshheading:7853546-Mutagenesis, Site-Directed,
pubmed-meshheading:7853546-Sequence Deletion,
pubmed-meshheading:7853546-Structure-Activity Relationship,
pubmed-meshheading:7853546-Viral Envelope Proteins,
pubmed-meshheading:7853546-Virion,
pubmed-meshheading:7853546-Virus Replication
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pubmed:year |
1995
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pubmed:articleTitle |
Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix.
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pubmed:affiliation |
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892-0460.
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pubmed:publicationType |
Journal Article
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