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Review
. 2005 Mar;26(4):485-503.
doi: 10.1007/s00281-004-0191-1. Epub 2005 Jan 5.

Antibodies as defensive enzymes

Sudhir Paul  1 , Yasuhiro Nishiyama, Stephanie Planque, Sangeeta Karle, Hiroaki Taguchi, Carl Hanson, Marc E Weksler
Affiliations
Review

Antibodies as defensive enzymes

Sudhir Paul et al. Springer Semin Immunopathol. 2005 Mar.

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 beta-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.

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