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Bacterial surface protein L binds and inactivates neutrophil proteins S100A8/A9.

Åkerström, Bo LU and Björck, Lars LU (2009) In Journal of immunology (Baltimore, Md. : 1950) 183(7). p.4583-4592
Abstract
Finegoldia magna is an anaerobic bacterial species that is part of the normal human flora on all nonsterile body surfaces, but it is also a significant opportunistic pathogen causing a wide range of infections. Some isolates of F. magna that are more frequently associated with clinical infection express protein L, a surface protein containing multiple homologous domains (B1-B5) that bind Igs through interactions with Ig L chains. The present study shows that the N-terminal A domain of protein L binds S100A8/A9, antibacterial proteins present in large amounts in the cytoplasm of neutrophils, but also extracellularly in tissues during inflammation. As a result, protein L-expressing F. magna are protected against killing by S100A8/A9. Igs and... (More)
Finegoldia magna is an anaerobic bacterial species that is part of the normal human flora on all nonsterile body surfaces, but it is also a significant opportunistic pathogen causing a wide range of infections. Some isolates of F. magna that are more frequently associated with clinical infection express protein L, a surface protein containing multiple homologous domains (B1-B5) that bind Igs through interactions with Ig L chains. The present study shows that the N-terminal A domain of protein L binds S100A8/A9, antibacterial proteins present in large amounts in the cytoplasm of neutrophils, but also extracellularly in tissues during inflammation. As a result, protein L-expressing F. magna are protected against killing by S100A8/A9. Igs and S100A8/A9 were found to interact independently with protein L, demonstrating that this bacterial surface protein is capable of manipulating both adaptive and innate immune defense mechanisms. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of immunology (Baltimore, Md. : 1950)
volume
183
issue
7
pages
4583 - 4592
publisher
American Association of Immunologists
external identifiers
  • wos:000270522500053
  • pmid:19752232
  • scopus:70449709581
ISSN
1550-6606
DOI
10.4049/jimmunol.0901487
language
English
LU publication?
yes
id
58433722-1405-46b9-89bf-e837c7978ee8 (old id 1483527)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19752232?dopt=Abstract
date added to LUP
2009-10-07 10:47:14
date last changed
2017-01-01 07:44:21
@article{58433722-1405-46b9-89bf-e837c7978ee8,
  abstract     = {Finegoldia magna is an anaerobic bacterial species that is part of the normal human flora on all nonsterile body surfaces, but it is also a significant opportunistic pathogen causing a wide range of infections. Some isolates of F. magna that are more frequently associated with clinical infection express protein L, a surface protein containing multiple homologous domains (B1-B5) that bind Igs through interactions with Ig L chains. The present study shows that the N-terminal A domain of protein L binds S100A8/A9, antibacterial proteins present in large amounts in the cytoplasm of neutrophils, but also extracellularly in tissues during inflammation. As a result, protein L-expressing F. magna are protected against killing by S100A8/A9. Igs and S100A8/A9 were found to interact independently with protein L, demonstrating that this bacterial surface protein is capable of manipulating both adaptive and innate immune defense mechanisms.},
  author       = {Åkerström, Bo and Björck, Lars},
  issn         = {1550-6606},
  language     = {eng},
  number       = {7},
  pages        = {4583--4592},
  publisher    = {American Association of Immunologists},
  series       = {Journal of immunology (Baltimore, Md. : 1950)},
  title        = {Bacterial surface protein L binds and inactivates neutrophil proteins S100A8/A9.},
  url          = {http://dx.doi.org/10.4049/jimmunol.0901487},
  volume       = {183},
  year         = {2009},
}