Cleavage of vimentin by different retroviral proteases
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.
Grant support
R31W00050
PHS HHS - United States
PubMed
10845700
DOI
10.1006/abbi.2000.1776
PII: S0003986100917764
Knihovny.cz E-resources
- MeSH
- Aspartic Acid Endopeptidases metabolism MeSH
- Sodium Chloride metabolism MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Endopeptidases metabolism MeSH
- HIV Protease MeSH
- Hydrogen-Ion Concentration MeSH
- Mason-Pfizer monkey virus enzymology MeSH
- Mutation MeSH
- Mice MeSH
- Retroviridae enzymology MeSH
- Substrate Specificity MeSH
- Binding Sites genetics MeSH
- Vimentin chemistry metabolism MeSH
- Leukemia Virus, Bovine enzymology MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Names of Substances
- Aspartic Acid Endopeptidases MeSH
- Sodium Chloride MeSH
- Endopeptidases MeSH
- HIV Protease MeSH
- p16 protease, Human immunodeficiency virus 2 MeSH Browser
- protease p15 MeSH Browser
- Vimentin MeSH
Proteases (PRs) of retroviruses cleave viral polyproteins into their mature structural proteins and replication enzymes. Besides this essential role in the replication cycle of retroviruses, PRs also cleave a variety of host cell proteins. We have analyzed the in vitro cleavage of mouse vimentin by proteases of human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2), bovine leukemia virus (BLV), Mason-Pfizer monkey virus (M-PMV), myeloblastosis-associated virus (MAV), and two active-site mutants of MAV PR. Retroviral proteases display significant differences in specificity requirements. Here, we show a comparison of substrate specificities of several retroviral proteases on vimentin as a substrate. Vimentin was cleaved by all the proteases at different sites and with different rates. The results show that the physiologically important cellular protein vimentin can be degraded by different retroviral proteases.
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