Surface proteins of Finegoldia magna interacting with the human host
Author
Summary, in English
One of the identified proteins, SufA, is a protease belonging to the subtilase family. This protease cleaves and inactivates the antimicrobial peptide LL-37 and the antibacterial chemokine MIG/CXCL9. Furthermore, the protease cleaves fibrinogen and thereby inhibits fibrin network formation. To our knowledge, the first example of directed mutagenesis of F. magna is presented with the disruption of the sufA gene.
The other identified protein is FAF. This is a cell wall attached α-helical protein that forms hair-like projections on the bacterial surface. FAF is self-associating and contributes to bacterial clumping. FAF also mediates adhesion of the bacterium to basement membranes of human skin by interacting with BM-40. A further function of FAF is blocking of the activity of antimicrobial peptides. The genes encoding faf and sufA are present in a majority of investigated isolates indicating that the proteins have important functions.
In conclusion, the findings presented in this thesis may help explain how F. magna colonizes the human host and causes opportunistic infections.
Department/s
Publishing year
2008
Language
English
Publication/Series
Lund University Faculty of Medicine Doctoral Dissertation Series
Volume
2008:134
Full text
Document type
Dissertation
Publisher
Department of Clinical Sciences, Lund University
Topic
- Infectious Medicine
Keywords
- Finegoldia magna
- Gram-positive anaerobic cocci
- surface proteins
- protease
- LL-37
- MIG/CXCL9
- Fibrinogen
- adhesion
- gene disruption
- bacterial aggregation
- basement membranes
Status
Published
ISBN/ISSN/Other
- ISSN: 1652-8220
- ISBN: 978-91-86059-87-3
Defence date
19 December 2008
Defence time
09:15
Defence place
Rune Grubb-salen, Biomedicinskt Centrum, Sölvegatan 18, 22184 Lund
Opponent
- Paul W. O'Toole (Dr)