MOLECULAR MIMICRY BETWEEN THE RABIES VIRUS GLYCOPROTEIN AND HUMAN IMMUNODEFICIENCY VIRUS-1 GP120 - CROSS-REACTING ANTIBODIES INDUCED BY RABIES VACCINATION
L. Bracci et al., MOLECULAR MIMICRY BETWEEN THE RABIES VIRUS GLYCOPROTEIN AND HUMAN IMMUNODEFICIENCY VIRUS-1 GP120 - CROSS-REACTING ANTIBODIES INDUCED BY RABIES VACCINATION, Blood, 90(9), 1997, pp. 3623-3628
The 160-170 sequence of human immunodeficiency virus (HIV)-1 gp120 mim
ics a nicotinic receptor-binding motif of rabies virus glycoprotein an
d snake neurotoxins This sequence has been proposed to be involved in
the binding of HIV-1 gp120 to the acetylcholine binding sites of nicot
inic receptors, BY using biomolecular interaction analysis (BIA) techn
ology we have found that HIV-1 gp120 can bind to detergent-extracted n
icotinic receptor from fetal calf muscle, The binding is inhibited by
nicotine and by a synthetic peptide reproducing the gp120 160-170 sequ
ence, The molecular mimicry between gp120 and rabies virus glycoprotei
n is confirmed by cross-reacting antibodies. We have found that vaccin
ation against rabies can induce the production of anti-HIV-1 gp120 ant
ibodies in humans. The cross-reacting antibodies are directed to the g
p120 sequence involved in the mimicry with the rabies virus glycoprote
in The cross-reactivity between the rabies virus and HIV-1 has importa
nt implications in transfusion medicine. Moreover, the presence of cro
ss-reacting antibodies between the nicotinic receptor binding site of
rabies virus glycoprotein and a fragment of HIV-1 gp120 strengthens th
e hypothesis about the possible role of nicotinic receptors as potenti
al receptors for HIV-1 in the central nervous system. (C) 1997 by The
American Society of Hematology.