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Biochemistry (Moscow)

, Volume 76, Issue 12, pp 1300–1311 | Cite as

Diversity of integrase-hydrolyzing IgGs and IgMs from sera of HIV-infected patients

  • S. V. Baranova
  • V. N. Buneva
  • M. A. Kharitonova
  • L. P. Sizyakina
  • O. D. Zakharova
  • G. A. NevinskyEmail author
Article

Abstract

It was previously shown that small fractions of IgGs and IgMs from the sera of AIDS patients specifically hydrolyze only HIV integrase (IN) but not many other tested proteins. Here we present evidence showing that these IgGs and IgMs are extreme catalytically heterogeneous. Affinity chromatography on IN-Sepharose using elution of IgGs (or IgMs) with different concentration of NaCl and acidic buffer separated catalytic antibodies (ABs) into many AB subfractions demonstrating different values of K m for IN and k cat. Nonfractionated IgGs and IgMs possess serine-, thiol-, acidiclike, and metal-dependent proteolytic activity. Metal-dependent activity of abzymes increases in the presence of ions of different metals. In contrast to canonical proteases having one pH optimum, initial nonfractionated IgGs and IgMs demonstrate several optima at pH from 3 to 10. The data obtained show that IN-hydrolyzing polyclonal IgG and IgM of HIV-infected patients are cocktails of anti-IN ABs with different structure of the active centers possessing various affinity to IN, pH optima, and relative rates of the specific substrate hydrolysis.

Key words

human immunodeficiency virus abzymes HIV infection HIV-integrase 

Abbreviations

AB

antibodies

ABappl, ABNaCl, and ABacid

fractions of antibodies eluted from IN-Sepharose on application, with NaCl gradient concentration, and with acidic buffer, respectively

AIDS

acquired immunodeficiency syndrome

HIV

human immunodeficiency virus

IN

HIV-integrase

HSA

human serum albumin

MBP

myelin basic protein

pIgG, pIgM, and pIgA

polyclonal IgG, IgM, and IgA

SLE

systemic lupus erythematosus

VIP

vasoactive intestinal peptide

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Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • S. V. Baranova
    • 1
  • V. N. Buneva
    • 1
    • 2
  • M. A. Kharitonova
    • 3
  • L. P. Sizyakina
    • 3
  • O. D. Zakharova
    • 1
  • G. A. Nevinsky
    • 1
    • 2
    Email author
  1. 1.Institute of Chemical Biology and Fundamental MedicineSiberian Division of the Russian Academy of SciencesNovosibirskRussia
  2. 2.Novosibirsk State UniversityNovosibirskRussia
  3. 3.Institute of Clinical ImmunologyRostov-on-Don State Medical UniversityRostov-on-DonRussia

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