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

Pasupuleti, Mukesh LU ; Walse, Bjorn; Nordahl, Emma LU ; Mörgelin, Matthias LU ; Malmsten, Martin and Schmidtchen, Artur LU (2007) In Journal of Biological Chemistry 282(4). p.2520-2528
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... (More)
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. (Less)
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author
organization
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Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
282
issue
4
pages
2520 - 2528
publisher
ASBMB
external identifiers
  • wos:000243593200044
  • scopus:34047259526
ISSN
1083-351X
DOI
10.1074/jbc.M607848200
language
English
LU publication?
yes
id
9d06ba00-5f88-4746-895e-2c5bbf9fe49b (old id 164289)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17132627&dopt=Abstract
date added to LUP
2007-07-12 14:11:19
date last changed
2017-09-03 03:43:59
@article{9d06ba00-5f88-4746-895e-2c5bbf9fe49b,
  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.},
  author       = {Pasupuleti, Mukesh and Walse, Bjorn and Nordahl, Emma and Mörgelin, Matthias and Malmsten, Martin and Schmidtchen, Artur},
  issn         = {1083-351X},
  language     = {eng},
  number       = {4},
  pages        = {2520--2528},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Preservation of antimicrobial properties of complement peptide C3a - from invertebrates to humans.},
  url          = {http://dx.doi.org/10.1074/jbc.M607848200},
  volume       = {282},
  year         = {2007},
}