Inhibition of human immunodeficiency virus infection by the lectin jacalin and by a derived peptide showing a sequence similarity with gp120

European Journal of Immunology - Tập 23 Số 1 - Trang 179-185 - 1993
Jean Favero1, Pierre Corbeau2,3, Michel Nicolas1, Monsef Benkirane3, Gilles Travé1, James F. P. Dixon4, Pièrre Aucouturier5, Surayia Rasheed4, Jōhn W. Parker4, Jean‐Pierre Liautard1, Christian Devaux3, Jacques Dornand1
1INSERM U65 Université Montpellier II
2Centre de Tri des molécules anti-HIV, Institut de Biologie, Montpellier
3Sciences et Techniques du Languedoc, Montpellier, CRBM, CNRS-INSERM U249
4Laboratoire d'Immunologic, Hǒpital Lapeyronie, Montpellier, Department of Pathology, University of Southern California
5School of Medicine, Los Angeles, and Laboratoire d'Immunologie et Immunopathologie, URA CNRS 1172, Poitiers

Tóm tắt

AbstractJacalin is a plant lectin known to specifically induce the proliferation of CD4+ T lymphocytes in human. We demonstrate here that jacalin completely blocks human immunodeficiency virus type 1 (HIV‐1) in vitro infection of lymphoid cells. Jacalin does not bind the viral envelope glycoprotein gp120. Besides other T cell surface molecules, it interacts with CD4, the high‐affinity receptor to HIV. Binding of jacalin to CD4 does not prevent gp120‐CD4 interaction and does not inhibit virus binding and syncytia formation. The anti‐HIV effect of the native lectin can be reproduced by its separated a‐subunits. More importantly, we have defined in the a‐chain of jacalin a 14‐amino acid sequence which shows high similarities with a peptide of the second conserved domain of gpl20. A synthetic peptide corresponding to this similar stretch also exerts a potent anti‐HIV effect. This peptide is not mitogenic for peripheral blood mononuclear cells and does not inhibit anti‐CD3‐induced lymphocyte proliferation. These results make jacalin a chain‐derived peptide a potentially valuable therapeutic agent for acquired immunodeficiency syndrome.

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Tài liệu tham khảo

10.1038/312763a0

10.1038/312767a0

Mc Dougal J. S., 1985, J. Immunol., 135, 3151, 10.4049/jimmunol.135.5.3151

10.1016/0092-8674(86)90590-8

10.1126/science.3001934

10.1016/0092-8674(87)90524-1

Merkcnschlager M., 1990, J. Immunol., 145, 2839, 10.4049/jimmunol.145.9.2839

Merkenschlager M., 1990, J Immunol., 145, 3181, 10.4049/jimmunol.145.10.3181

10.1126/science.2431482

10.1073/pnas.84.19.6924

10.1073/pnas.85.9.3198

10.1073/pnas.85.6.1932

10.1073/pnas.85.12.4478

10.1126/science.3500514

10.1038/331076a0

10.1038/331078a0

10.1038/331082a0

10.1038/331084a0

10.1073/pnas.88.17.7802

Moore J. P., 1992, J. Virol., 66, 235, 10.1128/jvi.66.1.235-243.1992

10.1016/0042-6822(92)90441-Q

10.1002/jcla.1860030409

10.1016/0003-9861(89)90542-0

10.1016/0014-5793(91)80518-8

10.1111/j.1365-2249.1990.tb03304.x

10.1097/00002030-198910000-00008

10.1016/0014-4827(89)90284-X

Rieber E. P., 1989, Leukocyte typing IV, 229

10.1038/227680a0

10.1042/bj1940351

10.1016/0006-291X(84)90696-X

10.1016/0005-2736(91)90332-3

10.1016/0161-5890(87)90025-3

Corbeau P., 1990, J. Virol., 64, 1459, 10.1128/jvi.64.4.1459-1464.1990

10.1016/0161-5890(88)90092-2

10.1084/jem.164.6.2101

10.1084/jem.169.1.185

10.1097/00002030-198910000-00003

10.1097/00002030-198912000-00003

10.1073/pnas.87.17.6574

Hasunuma T., 1992, J. Immunol., 148, 1841, 10.4049/jimmunol.148.6.1841

10.1016/S0021-9258(19)67689-1

10.1084/jem.172.4.1233

10.1016/0167-5699(92)90154-Y

10.1073/pnas.88.24.11320

10.1126/science.2830667

Willey R. L., 1989, J. Virol., 63, 3595, 10.1128/jvi.63.9.3595-3600.1989

10.1038/335445a0

10.1038/333278a0

Mohagheghpour N., 1991, J. Biol. Chem., 266, 7233, 10.1016/S0021-9258(20)89635-5

10.1097/00002030-199112000-00007

10.1093/intimm/4.2.295

10.1093/intimm/4.2.233

10.1016/0923-2494(91)90017-D