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).