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SufA--a novel subtilisin-like serine proteinase of Finegoldia magna.

Karlsson, Christofer; Andersson, Marie-Louise; Collin, Mattias; Schmidtchen, Artur; Björck, Lars and Frick, Inga-Maria LU (2007) In Microbiology 153(Pt 12). p.4208-4218
Abstract
Finegoldia magna is an anaerobic Gram-positive bacterium and commensal, which is also associated with clinically important conditions such as skin and soft tissue infections. This study describes a novel subtilisin-like extracellular serine proteinase of F. magna, denoted SufA (subtilase of Finegoldia magna), which is believed to be the first subtilase described among Gram-positive anaerobic cocci. SufA is associated with the bacterial cell surface, but is also released in substantial amounts during bacterial growth. Papain was used to release SufA from the surface of F. magna and the enzyme was purified by ion-exchange chromatography and gel filtration. A protein band on SDS-PAGE corresponding to the dominating proteolytic activity on... (More)
Finegoldia magna is an anaerobic Gram-positive bacterium and commensal, which is also associated with clinically important conditions such as skin and soft tissue infections. This study describes a novel subtilisin-like extracellular serine proteinase of F. magna, denoted SufA (subtilase of Finegoldia magna), which is believed to be the first subtilase described among Gram-positive anaerobic cocci. SufA is associated with the bacterial cell surface, but is also released in substantial amounts during bacterial growth. Papain was used to release SufA from the surface of F. magna and the enzyme was purified by ion-exchange chromatography and gel filtration. A protein band on SDS-PAGE corresponding to the dominating proteolytic activity on gelatin zymography was analysed by MS/MS. Based on the peptide sequences obtained, the sufA gene was sequenced. The gene comprises 3466 bp corresponding to a preprotein of 127 kDa. Like other members of the subtilase family, SufA contains the catalytic triad of aspartic acid, histidine and serine with surrounding conserved residues. A SufA homologue was identified in 33 of 34 investigated isolates of F. magna, as revealed by PCR and immunoprinting. The enzyme forms dimers, which are more proteolytically active than the monomeric protein. SufA was found to efficiently cleave and inactivate the antibacterial peptide LL-37 and the CXC chemokine MIG/CXCL9, indicating that the enzyme promotes F. magna survival and colonization. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Microbiology
volume
153
issue
Pt 12
pages
4208 - 4218
publisher
MAIK Nauka/Interperiodica
external identifiers
  • pmid:18048934
  • wos:000251931600028
  • scopus:37449017669
ISSN
1465-2080
DOI
10.1099/mic.0.2007/010322-0
language
English
LU publication?
yes
id
3f94919d-75e1-4f46-8734-785b3188d1a3 (old id 1035778)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18048934?dopt=Abstract
date added to LUP
2008-08-15 11:01:55
date last changed
2017-04-16 04:21:31
@article{3f94919d-75e1-4f46-8734-785b3188d1a3,
  abstract     = {Finegoldia magna is an anaerobic Gram-positive bacterium and commensal, which is also associated with clinically important conditions such as skin and soft tissue infections. This study describes a novel subtilisin-like extracellular serine proteinase of F. magna, denoted SufA (subtilase of Finegoldia magna), which is believed to be the first subtilase described among Gram-positive anaerobic cocci. SufA is associated with the bacterial cell surface, but is also released in substantial amounts during bacterial growth. Papain was used to release SufA from the surface of F. magna and the enzyme was purified by ion-exchange chromatography and gel filtration. A protein band on SDS-PAGE corresponding to the dominating proteolytic activity on gelatin zymography was analysed by MS/MS. Based on the peptide sequences obtained, the sufA gene was sequenced. The gene comprises 3466 bp corresponding to a preprotein of 127 kDa. Like other members of the subtilase family, SufA contains the catalytic triad of aspartic acid, histidine and serine with surrounding conserved residues. A SufA homologue was identified in 33 of 34 investigated isolates of F. magna, as revealed by PCR and immunoprinting. The enzyme forms dimers, which are more proteolytically active than the monomeric protein. SufA was found to efficiently cleave and inactivate the antibacterial peptide LL-37 and the CXC chemokine MIG/CXCL9, indicating that the enzyme promotes F. magna survival and colonization.},
  author       = {Karlsson, Christofer and Andersson, Marie-Louise and Collin, Mattias and Schmidtchen, Artur and Björck, Lars and Frick, Inga-Maria},
  issn         = {1465-2080},
  language     = {eng},
  number       = {Pt 12},
  pages        = {4208--4218},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Microbiology},
  title        = {SufA--a novel subtilisin-like serine proteinase of Finegoldia magna.},
  url          = {http://dx.doi.org/10.1099/mic.0.2007/010322-0},
  volume       = {153},
  year         = {2007},
}