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Protein FOG - a streptococcal inhibitor of neutrophil function.

Linge, Helena LU ; Mörgelin, Matthias LU and Frick, Inga-Maria LU (2004) In Microbiology1994-01-01+01:00 150(Pt 12). p.4211-4221
Abstract
Several strains of group G streptococci (GGS) form aggregates when grown in vitro. Aggregating strains interact with fibrinogen, and this study reports the isolation of a novel self-associating and fibrinogen-binding protein of GGS, denoted protein FOG. Sequencing of the fog gene revealed structural similarity with M proteins of both GGS and group A streptococci (GAS). Analogous to GAS, GGS were found to multiply in human blood. All strains of GGS express protein G, a protein known to interact with the constant region of immunoglobulin G and albumin. Surprisingly, a clinical isolate expressing protein G, but lacking protein FOG, was killed in human whole blood; however, the addition of intact soluble protein FOG restored the ability of the... (More)
Several strains of group G streptococci (GGS) form aggregates when grown in vitro. Aggregating strains interact with fibrinogen, and this study reports the isolation of a novel self-associating and fibrinogen-binding protein of GGS, denoted protein FOG. Sequencing of the fog gene revealed structural similarity with M proteins of both GGS and group A streptococci (GAS). Analogous to GAS, GGS were found to multiply in human blood. All strains of GGS express protein G, a protein known to interact with the constant region of immunoglobulin G and albumin. Surprisingly, a clinical isolate expressing protein G, but lacking protein FOG, was killed in human whole blood; however, the addition of intact soluble protein FOG restored the ability of the bacteria to survive and multiply in human blood. This is believed to be the first report of a soluble M-like protein salvaging an M-negative strain from being killed. The antibactericidal property of protein FOG is dependent on its fibrinogen-binding activity. Thus, in plasma, FOG precipitates fibrinogen, and when added to whole blood, protein FOG triggers the formation of visible aggregates comprising fibrinogen and neutrophils that are disabled in their killing of the bacteria. Moreover, the results emphasize the importance of an intact FOG molecule, as presented on the bacterial surface, for full protective effect. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Microbiology1994-01-01+01:00
volume
150
issue
Pt 12
pages
4211 - 4221
publisher
MAIK Nauka/Interperiodica
external identifiers
  • pmid:15583173
  • wos:000226043000033
  • scopus:11044234357
ISSN
1465-2080
DOI
10.1099/mic.0.27269-0
language
English
LU publication?
yes
id
fcaa6b93-d3e0-4118-89d3-38e0f22cb82f (old id 132131)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15583173&dopt=Abstract
date added to LUP
2007-07-04 16:30:10
date last changed
2017-08-27 04:04:23
@article{fcaa6b93-d3e0-4118-89d3-38e0f22cb82f,
  abstract     = {Several strains of group G streptococci (GGS) form aggregates when grown in vitro. Aggregating strains interact with fibrinogen, and this study reports the isolation of a novel self-associating and fibrinogen-binding protein of GGS, denoted protein FOG. Sequencing of the fog gene revealed structural similarity with M proteins of both GGS and group A streptococci (GAS). Analogous to GAS, GGS were found to multiply in human blood. All strains of GGS express protein G, a protein known to interact with the constant region of immunoglobulin G and albumin. Surprisingly, a clinical isolate expressing protein G, but lacking protein FOG, was killed in human whole blood; however, the addition of intact soluble protein FOG restored the ability of the bacteria to survive and multiply in human blood. This is believed to be the first report of a soluble M-like protein salvaging an M-negative strain from being killed. The antibactericidal property of protein FOG is dependent on its fibrinogen-binding activity. Thus, in plasma, FOG precipitates fibrinogen, and when added to whole blood, protein FOG triggers the formation of visible aggregates comprising fibrinogen and neutrophils that are disabled in their killing of the bacteria. Moreover, the results emphasize the importance of an intact FOG molecule, as presented on the bacterial surface, for full protective effect.},
  author       = {Linge, Helena and Mörgelin, Matthias and Frick, Inga-Maria},
  issn         = {1465-2080},
  language     = {eng},
  number       = {Pt 12},
  pages        = {4211--4221},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Microbiology1994-01-01+01:00},
  title        = {Protein FOG - a streptococcal inhibitor of neutrophil function.},
  url          = {http://dx.doi.org/10.1099/mic.0.27269-0},
  volume       = {150},
  year         = {2004},
}