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M9550141.TXT
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1995-03-04
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Document 0141
DOCN M9550141
TI Cleavage of recombinant and cell derived human immunodeficiency virus 1
(HIV-1) Nef protein by HIV-1 protease.
DT 9505
AU Gaedigk-Nitschko K; Schon A; Wachinger G; Erfle V; Kohleisen B;
GSF-Forschungszentrum fur Umwelt und Gesundheit, Institut fur;
Molekulare Virologie, Oberschleissheim, Germany.
SO FEBS Lett. 1995 Jan 9;357(3):275-8. Unique Identifier : AIDSLINE
MED/95137104
AB Recombinant purified Nef protein of HIV-1, as well as Nef protein
derived from extracts of permanently HIV-1 infected glioblastoma cells
and monocytes, are specifically cleaved by the HIV-1 protease. Nef
cleavage products in cellular extracts treated with protease showed
identical molecular weights as those obtained by digestion of purified
Nef with recombinant HIV-1 protease. Since cellular extracts were
prepared by detergent and mechanical lysis it cannot be excluded that
physiological cytoplasmic conditions were altered. The lack of Nef
cleavage by endogenous HIV-1 protease in infected cells might be due to
low concentrations of viral protease and the presence of Gag precursor
molecules as natural substrate. Using a panel of monoclonal antibodies
two cleavage fragments of 19 kDa and 8 kDa were defined. The cleavage
site was located by microsequencing between amino acid 57 and 58
(AW*LEAQEEEEVGF). The conserved cleavage motif within HIV-1 Nef suggests
a potential biological function of Nef processing.
DE Amino Acid Sequence Antibodies, Monoclonal Gene Products,
gag/METABOLISM Gene Products, nef/*METABOLISM Hydrolysis HIV
Protease/*METABOLISM HIV-1/ENZYMOLOGY/*METABOLISM Molecular Sequence
Data Support, Non-U.S. Gov't Tumor Cells, Cultured JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).