Preservation of antimicrobial properties of complement peptide C3a - from invertebrates to humans.

Research output: Contribution to journalArticle

Abstract

The human anaphylatoxin peptide C3a, generated during complement activation, exerts antimicrobial effects. Phylogenetic analysis, sequence analyses, and structural modeling studies paired with antimicrobial assays of peptides from known C3a sequences showed that, in particular in vertebrate C3a, crucial structural determinants governing antimicrobial activity have been conserved during the evolution of C3a. Thus, regions of the ancient C3a from Carcinoscorpius rotundicauda as well as corresponding parts of human C3a exhibited helical structures upon binding to bacterial lipopolysaccharide permeabilized liposomes and were antimicrobial against Gram-negative and Gram-positive bacteria. Human C3a and C4a (but not C5a) were antimicrobial, in concert with the separate evolutionary development of the chemotactic C5a. Thus, the results demonstrate that, notwithstanding a significant sequence variation, functional and structural constraints imposed on C3a during evolution have preserved critical properties governing antimicrobial activity.

Details

Authors
Organisations
External organisations
  • Uppsala University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Dermatology and Venereal Diseases
  • Other Clinical Medicine
  • Infectious Medicine
Original languageEnglish
Pages (from-to)2520-2528
JournalJournal of Biological Chemistry
Volume282
Issue number4
Publication statusPublished - 2007
Publication categoryResearch
Peer-reviewedYes

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