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Induction of a Protein-Targeted Catalytic Response in Autoimmune Prone Mice:  Antibody-Mediated Cleavage of HIV-1 Glycoprotein GP120

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Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, RAS, 16/10, Miklukho-Maklaya str., Moscow 117871, Russia, Engelhardt Institute of Molecular Biology, RAS, 32, Vavilova str., Moscow 117984, Russia, Department of Chemistry, Lomonosov Moscow State University, Moscow 119899, Russia, Puschino Branch of the Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, RAS, Puschino 142290, Russia, CNRS UMR 6022, Compiègne Technological University, BP 20529, 60206 Compiègne Cedex, France, Ciphergen Biosystems, Inc., 6611 Dumbarton Circle, Fremont, California 94555, and Laboratory of Immunopathology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 5640 Fishers Lane, Rockville, Maryland 20852
Cite this: Biochemistry 2006, 45, 1, 324–330
Publication Date (Web):December 9, 2005
https://doi.org/10.1021/bi050675k
Copyright © 2006 American Chemical Society

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    Abstract

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    We have induced a polyclonal IgG that degrades the HIV-1 surface antigen, glycoprotein gp120, by taking advantage of the susceptibility of SJL mice to a peptide-induced autoimmune disorder, experimental autoimmune encephalomyelitis (EAE). Specific pathogen-free SJL mice were immunized with structural fragments of gp120, fused in-frame with encephalitogenic peptide MBP85-101. It has resulted in a pronounced disease-associated immune response against antigens. A dramatic increase of gp120 degradation level by purified polyclonal IgG from immunized versus nonimmunized mice has been demonstrated by a newly developed fluorescence-based assay. This activity was inhibited by anti-mouse immunoglobulin antibodies as well as by Ser- and His-reactive covalent inhibitors. A dominant proteolysis site in recombinant gp120 incubated with purified polyclonal IgG from immunized mice was shown by SDS−PAGE. The SELDI-based mass spectrometry revealed that these antibodies exhibited significant specificity toward the Pro484−Leu485 peptide bond. The sequence surrounding this site is present in nearly half of the HIV-I variants. This novel strategy can be generalized for creating a catalytic vaccine against viral pathogens.

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     This work was done in the frames of BTEP(NIH) Grant 37 for H.C.M. and A.G.G. The work was supported in part by grants from the European Union INCO-COPERNICUS program (IC15 CT96-0909) for A.F. and A.G.G., the ASGL Research Laboratories, the Scientific Russian Schools Program 1800.2003.4 for A.G.G., and the Russian Foundation of Basic Research (Grant 99-04-49163-à) for N.A.P. This work was supported in part by the Intramural Research Program of the NIH, National Institute of Allergy and Infectious Diseases.

     Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry.

    §

     Engelhardt Institute of Molecular Biology.

     Lomonosov Moscow State University.

     Puschino Branch of the Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry.

    #

     Compiègne Technological University.

     Ciphergen Biosystems, Inc.

     Deceased.

     National Institutes of Health.

    *

     To whom correspondence should be addressed at the Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry. Tel:  +7(095) 429-8269. Fax:  +7(095) 330-7329. E-mail:  [email protected].

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    Figure 1, scheme of gp120 and sites of cleavage; Figure 2, distribution of immune response to gp120 in immunized SJL mice; Figure 3, T-lymphocytes phenotype changes during immunization; Figure 4, tissue stains of immunized mice. This material is available free of charge via the Internet at http://pubs.acs.org.

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    6. Emi Hifumi, Shingo Matsumoto, Hiroki Nakashima, Shogo Itonaga, Mitsue Arakawa, Yoshiki Katayama, Ryuichi Kato, Taizo Uda. A novel method of preparing the monoform structure of catalytic antibody light chain. The FASEB Journal 2016, 30 (2) , 895-908. https://doi.org/10.1096/fj.15-276394
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    8. S M Deyev, E N Lebedenko, L E Petrovskaya, D A Dolgikh, A G Gabibov, M P Kirpichnikov. Man-made antibodies and immunoconjugates with desired properties: function optimization using structural engineering. Russian Chemical Reviews 2015, 84 (1) , 1-26. https://doi.org/10.1070/RCR4459
    9. Suiyi Tan, Lin Li, Lu Lu, Chungen Pan, Hong Lu, Yelena Oksov, Xiaojuan Tang, Shibo Jiang, Shuwen Liu. Peptides derived from HIV‐1 gp120 co‐receptor binding domain form amyloid fibrils and enhance HIV‐1 infection. FEBS Letters 2014, 588 (9) , 1515-1522. https://doi.org/10.1016/j.febslet.2014.03.016
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    14. I. V. Smirnov, I. I. Vorobiev, A. Friboulet, B. Avalle, D. Thomas, V. D. Knorre, A. G. Gabibov, N. A. Ponomarenko. The antiidiotypic approach to obtaining a proteolytic antibody. Doklady Biochemistry and Biophysics 2008, 420 (1) , 105-107. https://doi.org/10.1134/S1607672908030022
    15. Ashok K. Singh, Yin Jiang, Shveta Gupta. Effects of chronic alcohol drinking on receptor-binding, internalization, and degradation of human immunodeficiency virus 1 envelope protein gp120 in hepatocytes. Alcohol 2007, 41 (8) , 591-606. https://doi.org/10.1016/j.alcohol.2007.08.003

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