PMID: 8971042Dec 1, 1996Paper

Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases

Journal of Virology
J SchorrH R Kalbitzer

Abstract

Human immunodeficiency virus type 2 (HIV-2) Nef is proteolytically cleaved by the HIV-2-encoded protease. The proteolysis is not influenced by the absence or presence of the N-terminal myristoylation. The main cleavage site is located between residues 39 and 40, suggesting a protease recognition sequence, GGEY-SQFQ. As observed previously for Nef protein from HIV-1, a large, stable core domain with an apparent molecular mass of 30 kDa is produced by the proteolytic activity. Cleavage of Nef from HIV-1 in two domains by its own protease or the protease from HIV-2 is also independent of Nef myristoylation. However, processing of HIV-1 Nef by the HIV-2 protease is less selective than that by the HIV-1 protease: the obtained core fragment is heterogeneous at its N terminus and has an additional cleavage site between amino acids 99 and 100. Preliminary experiments suggest that the full-length Nef of HIV-2 and the core domain are part of the HIV-2 particles, analogous to the situation reported recently for HIV-1.

References

Jan 26, 1995·The New England Journal of Medicine·F KirchhoffR C Desrosiers
Apr 15, 1994·European Journal of Biochemistry·J FreundH R Kalbitzer
Apr 1, 1995·Journal of Biomolecular NMR·J Freund, H R Kalbitzer

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Citations

Jul 1, 2016·Microbiology and Molecular Biology Reviews : MMBR·Guangdi Li, Erik De Clercq
Jul 13, 2000·Protein Science : a Publication of the Protein Society·S AroldC Dumas
Aug 13, 2005·Molecular Therapy : the Journal of the American Society of Gene Therapy·Silvia PerettiMaurizio Federico

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