Molecular mimicry between the rabies virus glycoprotein and human immunodeficiency virus-1 GP120: Cross-reacting antibodies induced by rabies vaccination

被引:19
作者
Bracci, L [1 ]
Ballas, SK [1 ]
Spreafico, A [1 ]
Neri, P [1 ]
机构
[1] THOMAS JEFFERSON UNIV HOSP,DEPT MED,CARDEZA FDN HAEMATOL RES,PHILADELPHIA,PA 19107
关键词
D O I
10.1182/blood.V90.9.3623
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The 160-170 sequence of human immunodeficiency virus (HIV)-1 gp120 mimics a nicotinic receptor-binding motif of rabies virus glycoprotein and snake neurotoxins This sequence has been proposed to be involved in the binding of HIV-1 gp120 to the acetylcholine binding sites of nicotinic receptors, BY using biomolecular interaction analysis (BIA) technology we have found that HIV-1 gp120 can bind to detergent-extracted nicotinic receptor from fetal calf muscle, The binding is inhibited by nicotine and by a synthetic peptide reproducing the gp120 160-170 sequence, The molecular mimicry between gp120 and rabies virus glycoprotein is confirmed by cross-reacting antibodies. We have found that vaccination against rabies can induce the production of anti-HIV-1 gp120 antibodies in humans. The cross-reacting antibodies are directed to the gp120 sequence involved in the mimicry with the rabies virus glycoprotein The cross-reactivity between the rabies virus and HIV-1 has important implications in transfusion medicine. Moreover, the presence of cross-reacting antibodies between the nicotinic receptor binding site of rabies virus glycoprotein and a fragment of HIV-1 gp120 strengthens the hypothesis about the possible role of nicotinic receptors as potential receptors for HIV-1 in the central nervous system. (C) 1997 by The American Society of Hematology.
引用
收藏
页码:3623 / 3628
页数:6
相关论文
共 24 条
[1]   NICOTINIC RECEPTOR FUNCTION IN THE MAMMALIAN CENTRAL-NERVOUS-SYSTEM [J].
ALBUQUERQUE, EX ;
PEREIRA, EFR ;
CASTRO, NG ;
ALKONDON, M ;
REINHARDT, S ;
SCHRODER, H ;
MAELICKE, A .
DIVERSITY OF INTERACTING RECEPTORS, 1995, 757 :48-72
[2]  
BRACCI L, 1995, ARCH PATHOL LAB MED, V119, P391
[3]   ANTIPEPTIDE MONOCLONAL-ANTIBODIES INHIBIT THE BINDING OF RABIES VIRUS GLYCOPROTEIN AND ALPHA-BUNGAROTOXIN TO THE NICOTINIC ACETYLCHOLINE-RECEPTOR [J].
BRACCI, L ;
ANTONI, G ;
CUSI, MG ;
LOZZI, L ;
NICCOLAI, N ;
PETRENI, S ;
RUSTICI, M ;
SANTUCCI, A ;
SOLDANI, P ;
VALENSIN, PE ;
NERI, P .
MOLECULAR IMMUNOLOGY, 1988, 25 (09) :881-888
[4]   BINDING OF HIV-1 GP120 TO THE NICOTINIC RECEPTOR [J].
BRACCI, L ;
LOZZI, L ;
RUSTICI, M ;
NERI, P .
FEBS LETTERS, 1992, 311 (02) :115-118
[5]   CURRENT VIEW ON THE STRUCTURE-FUNCTION RELATIONSHIP OF POSTSYNAPTIC NEUROTOXINS FROM SNAKE-VENOMS [J].
ENDO, T ;
TAMIYA, N .
PHARMACOLOGY & THERAPEUTICS, 1987, 34 (03) :403-+
[6]  
Fagerstam L G, 1990, J Mol Recognit, V3, P208, DOI 10.1002/jmr.300030507
[7]  
GOTRI C, 1984, NEUROLOGY, V34, P374
[8]   Hippocampal synaptic transmission enhanced by low concentrations of nicotine [J].
Gray, R ;
Rajan, AS ;
Radcliffe, KA ;
Yakehiro, M ;
Dani, JA .
NATURE, 1996, 383 (6602) :713-716
[9]   IMMOBILIZATION OF PROTEINS TO A CARBOXYMETHYLDEXTRAN-MODIFIED GOLD SURFACE FOR BIOSPECIFIC INTERACTION ANALYSIS IN SURFACE-PLASMON RESONANCE SENSORS [J].
JOHNSSON, B ;
LOFAS, S ;
LINDQUIST, G .
ANALYTICAL BIOCHEMISTRY, 1991, 198 (02) :268-277
[10]   STRUCTURE-FUNCTION-RELATIONSHIPS OF CURAREMIMETIC NEUROTOXIN LOOP-2 AND OF A STRUCTURALLY SIMILAR SEGMENT OF RABIES VIRUS GLYCOPROTEIN IN THEIR INTERACTION WITH THE NICOTINIC ACETYLCHOLINE-RECEPTOR [J].
LENTZ, TL .
BIOCHEMISTRY, 1991, 30 (45) :10949-10957