Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
نویسندگان
چکیده
منابع مشابه
Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus.
Binding of the human immunodeficiency virus type 1 (HIV-1) Gag protein precursor, Pr55(Gag), to membrane is an indispensable step in virus assembly. Previously, we reported that a matrix (MA) residue 6 substitution (6VR) imposed a virus assembly defect similar to that observed with myristylation-defective mutants, suggesting that the 6VR change impaired membrane binding. Intriguingly, the 6VR m...
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Human immunodeficiency virus type 1 (HIV-1) protease inhibitors comprise an important class of drugs used in HIV treatments. However, mutations of protease genes accelerated by low fidelity of reverse transcriptase yield drug resistant mutants of reduced affinities for the inhibitors. This problem is considered to be a serious barrier against HIV treatment for the foreseeable future. In this st...
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Objective Dot Blot (DB) assay provides highly specific results, but usually not reliable for quantification of antibody production. The need for a more objective DB assay to provide a better definition of the immune status, against HIV antigens, promoted this study to be done to develop a quantitative DB assay. Material and Methods Dot blot (DB) strips for antibodies directed to human immuno...
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The human immunodeficiency virus type 1 matrix (MA) protein is phosphorylated during virion maturation on its C-terminal tyrosine and on several serine residues. Whereas MA tyrosine phosphorylation facilitates viral nuclear import, the significance of MA serine phosphorylation remains unclear. Here, we report that MA serine but not tyrosine phosphorylation is strongly enhanced by Nef. Mutations...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1994
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.68.8.5311-5320.1994