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. 1996 Dec;70(12):9051-4.
doi: 10.1128/JVI.70.12.9051-9054.1996.

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

J Schorr  1 , R Kellner, O Fackler, J Freund, J Konvalinka, N Kienzle, H G Kräusslich, N Mueller-Lantzsch, H R Kalbitzer
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Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases

J Schorr et al. J Virol. 1996 Dec.

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.

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