Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases.
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.
Schorr
J
J
Max-Planck-Institute for Medical Research, Heidelberg, Germany.
Kellner
R
R
Fackler
O
O
Freund
J
J
Konvalinka
J
J
Kienzle
N
N
Kräusslich
H G
HG
Mueller-Lantzsch
N
N
Kalbitzer
H R
HR
D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D001665:Binding Sites; D015693:Gene Products, nef / Q000378:metabolism*; D016333:HIV Protease / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism*; D015498:HIV-2 / Q000378:metabolism*; D006801:Humans; D009227:Myristic Acids / Q000378:metabolism; D013379:Substrate Specificity; D054311:nef Gene Products, Human Immunodeficiency Virus
D015693:Gene Products, nef; D009227:Myristic Acids; D054311:nef Gene Products, Human Immunodeficiency Virus; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C065184:p16 protease, Human immunodeficiency virus 2