FEBS Letters | |
Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV‐1) Nef protein by HIV‐1 protease | |
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
【 预 览 】
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