Specific in vitro cleavage of Mason-Pfizer monkey virus capsid protein: evidence for a potential role of retroviral protease in early stages of infection
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, P.H.S.
Grantová podpora
RR 12878
NCRR NIH HHS - United States
RR 13948
NCRR NIH HHS - United States
PubMed
12781718
DOI
10.1016/s0042-6822(03)00128-4
PII: S0042682203001284
Knihovny.cz E-zdroje
- MeSH
- COS buňky MeSH
- endopeptidasy metabolismus MeSH
- genové produkty gag metabolismus MeSH
- HIV-1 metabolismus MeSH
- HIV-proteasa metabolismus MeSH
- Masonův-Pfizerův opičí virus metabolismus fyziologie MeSH
- nukleokapsida chemie metabolismus MeSH
- replikace viru * MeSH
- sekvence aminokyselin MeSH
- virové plášťové proteiny chemie metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Názvy látek
- endopeptidasy MeSH
- genové produkty gag MeSH
- HIV-proteasa MeSH
- virové plášťové proteiny MeSH
Processing of Gag polyproteins by viral protease (PR) leads to reorganization of immature retroviral particles and formation of a ribonucleoprotein core. In some retroviruses, such as HIV and RSV, cleavage of a spacer peptide separating capsid and nucleocapsid proteins is essential for the core formation. We show here that no similar spacer peptide is present in the capsid-nucleocapsid (CA-NC) region of Mason-Pfizer monkey virus (M-PMV) and that the CA protein is cleaved in vitro by the PR within the major homology region (MHR) and the NC protein in several sites at the N-terminus. The CA cleavage product was also identified shortly after penetration of M-PMV into COS cells, suggesting that the protease-catalyzed cleavage is involved in core disintegration.
Citace poskytuje Crossref.org
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