Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV‐1) Nef protein by HIV‐1 protease

FEBS Letters

Kohleisen, B.¹  Schön, A.¹  Gaedigk-Nitschko, K.¹  Erfle, V.¹  Wachinger, G.¹ 

[1] GSF-Forschungszentrum für Umwelt and Gesundheit, Institut für Molekulare Virologie, Neuherberg, Ingolstaedter Landstr. 1, 85764 Oberschleissheim, Germany

关键词: Nef protein;    HIV-1 protease;    Proteolytic cleavage;   

DOI  :  10.1016/0014-5793(94)01370-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown