Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
| Autor: | Paul Spearman, Stefan Höning, Manuel Favre, Michael Boge, Melissa Batonick, Markus Thali |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
viruses
media_common.quotation_subject Assembly Adaptor Protein Complex 2 Down-Regulation Gene Products gag Adaptor gag Gene Products Human Immunodeficiency Virus Clathrin Virus 03 medical and health sciences Valine Virology Humans Tyrosine Internalization 030304 developmental biology media_common Gag Infectivity chemistry.chemical_classification 0303 health sciences biology Virus Assembly 030302 biochemistry & molecular biology AP-2 3. Good health Cell biology chemistry Viral replication Release HIV-1 biology.protein Glycoprotein HeLa Cells |
| Zdroj: | Virology. 342:190-200 |
| ISSN: | 0042-6822 |
| Popis: | The envelope glycoprotein (Env) of HIV-1 interacts with the clathrin-associated adaptor complex AP-2 during the late phase of the viral replication cycle. Upon its synthesis, Env, therefore, is retrieved from the cellular surface unless internalization is inhibited by viral Gag. Here we demonstrate that not only Env, but also HIV-1 Gag, specifically binds to AP-2. Gag–AP-2 association was found to depend on tyrosine residue 132 and valine residue 135 at the matrix–capsid junction in the Gag polyprotein. Results of a morphological analysis of viral egress from cells expressing dominant-negative AP-2 suggest an involvement of AP-2 in confining HIV-1 exit to distinct microdomains. Further, particle release from AP-2-mutant cells was enhanced compared to release from wild-type cells but the infectivity of virus released from these cells was moderately reduced. Together these data attribute a role to the AP-2 complex in the regulation of HIV-1 assembly/release. |
| Databáze: | OpenAIRE |
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