Serine proteinase inhibitors from nematodes and the arms race between host and pathogen

Xingxing Zang, Rick M. Maizels

Research output: Contribution to journalReview article

111 Scopus citations

Abstract

Serine proteinase inhibitors are encoded by a large gene family of long evolutionary standing. Recent discoveries of parasite proteins that inhibit human serine proteinases, together with the complete genomic sequence from Caenorhabditis elegans, have provided a set of new serine proteinase inhibitors from more primitive metazoan animals such as nematodes. The structural features (e.g. reactive centre residues), gene organization (including intron arrangements) and inhibitory function and targets (e.g. inflammatory and coagulation pathway proteinase) all contribute important new insights into proteinase inhibitor evolution. Some parasite products have evolved that block enzymes in the mammalian host, but the human host responds with a significant immune response to the parasite inhibitors. Thus, infection produces a finely balanced conflict between host and pathogen at the molecular level, and this might have accelerated the evolution of these proteins in parasitic species as well as their hosts.

Original languageEnglish (US)
Pages (from-to)191-197
Number of pages7
JournalTrends in Biochemical Sciences
Volume26
Issue number3
DOIs
StatePublished - Mar 1 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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