Bacterial surface protein L binds and inactivates neutrophil proteins S100A8/A9.
(2009) In Journal of immunology 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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1483527
- author
- Åkerström, Bo LU and Björck, Lars LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of immunology
- 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
- 2016-04-04 09:11:55
- date last changed
- 2022-03-31 01:31:19
@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}},
title = {{Bacterial surface protein L binds and inactivates neutrophil proteins S100A8/A9.}},
url = {{http://dx.doi.org/10.4049/jimmunol.0901487}},
doi = {{10.4049/jimmunol.0901487}},
volume = {{183}},
year = {{2009}},
}