Springer Seminars in Immunopathology

, Volume 26, Issue 4, pp 485–503

Antibodies as defensive enzymes

Authors

    • Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory MedicineUniversity of Texas-Houston Medical School
  • Yasuhiro Nishiyama
    • Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory MedicineUniversity of Texas-Houston Medical School
  • Stephanie Planque
    • Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory MedicineUniversity of Texas-Houston Medical School
  • Sangeeta Karle
    • Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory MedicineUniversity of Texas-Houston Medical School
  • Hiroaki Taguchi
    • Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory MedicineUniversity of Texas-Houston Medical School
  • Carl Hanson
    • Rickettsial Disease LabCalifornia Department of Health Services
  • Marc E. Weksler
    • Department of MedicineWeill Medical College of Cornell University
Original Article

DOI: 10.1007/s00281-004-0191-1

Cite this article as:
Paul, S., Nishiyama, Y., Planque, S. et al. Springer Semin Immun (2005) 26: 485. doi:10.1007/s00281-004-0191-1

Abstract

Antibodies (Abs) and enzymes are structural and functional relatives. Abs with promiscuous peptidase activity are ubiquitous in healthy humans, evidently derived from germline variable domain immunoglobulin genes encoding the serine protease-like nucleophilic function. Exogenous and endogenous electrophilic antigens can bind the nucleophilic sites covalently, and recent evidence suggests that immunization with such antigens can induce proteolytic antibodies. Previously, Ab catalytic activities have been linked to pathogenic autoimmune reactions, but recent studies indicate that proteolytic Abs may also serve beneficial functions. An example is the rapid and selective cleavage of the HIV-1 coat protein gp120 by IgMs found in uninfected humans. The selectivity of this reaction appears to derive from recognition of gp120 as a superantigen. A second example is the cleavage of amyloid β-peptide by IgM and IgG from aged humans, a phenomenon that may represent a specific proteolytic response to a neurotoxic endogenous peptide implicated in the pathogenesis of Alzheimer’s disease.

Keywords

Abzymes Catalytic antibodies Serine proteases Autoimmune disease HIV infection

Copyright information

© Springer-Verlag 2005