Complement evasion strategies of pathogens-Acquisition of inhibitors and beyond.
(2009) In Molecular Immunology 46. p.2808-2817- Abstract
- Activation of the complement system and resulting opsonisation with C3b are key events of the innate immune defense against infections. However, a wide variety of bacterial pathogens subvert complement attack by binding host complement inhibitors such as C4b-binding protein, factor H and vitronectin, which results in diminished opsonophagocytosis and killing of bacteria by lysis. Another widely used strategy is production of proteases, which can effectively degrade crucial complement components. Furthermore, bacterial pathogens such as Moraxella catarrhalis and Staphylococcus aureus capture and incapacitate the key complement component C3. The current review describes examples of these three strategies. Targeting binding sites for... (More)
- Activation of the complement system and resulting opsonisation with C3b are key events of the innate immune defense against infections. However, a wide variety of bacterial pathogens subvert complement attack by binding host complement inhibitors such as C4b-binding protein, factor H and vitronectin, which results in diminished opsonophagocytosis and killing of bacteria by lysis. Another widely used strategy is production of proteases, which can effectively degrade crucial complement components. Furthermore, bacterial pathogens such as Moraxella catarrhalis and Staphylococcus aureus capture and incapacitate the key complement component C3. The current review describes examples of these three strategies. Targeting binding sites for complement inhibitors on bacterial surfaces and complement-degrading proteases with vaccine-induced antibodies may be used to enhance a common vaccine design strategy that depends on the generation of complement-dependent bactericidal and opsonophagocytic antibody activities. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1411918
- author
- Blom, Anna LU ; Hallström, Teresia LU and Riesbeck, Kristian LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Immunology
- volume
- 46
- pages
- 2808 - 2817
- publisher
- Pergamon Press Ltd.
- external identifiers
-
- wos:000269554500010
- pmid:19477524
- scopus:68249086824
- ISSN
- 1872-9142
- DOI
- 10.1016/j.molimm.2009.04.025
- language
- English
- LU publication?
- yes
- id
- c69ad74c-3085-4c07-ba59-8d106e3b0162 (old id 1411918)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/19477524?dopt=Abstract
- date added to LUP
- 2016-04-04 09:25:46
- date last changed
- 2022-04-08 02:58:45
@article{c69ad74c-3085-4c07-ba59-8d106e3b0162, abstract = {{Activation of the complement system and resulting opsonisation with C3b are key events of the innate immune defense against infections. However, a wide variety of bacterial pathogens subvert complement attack by binding host complement inhibitors such as C4b-binding protein, factor H and vitronectin, which results in diminished opsonophagocytosis and killing of bacteria by lysis. Another widely used strategy is production of proteases, which can effectively degrade crucial complement components. Furthermore, bacterial pathogens such as Moraxella catarrhalis and Staphylococcus aureus capture and incapacitate the key complement component C3. The current review describes examples of these three strategies. Targeting binding sites for complement inhibitors on bacterial surfaces and complement-degrading proteases with vaccine-induced antibodies may be used to enhance a common vaccine design strategy that depends on the generation of complement-dependent bactericidal and opsonophagocytic antibody activities.}}, author = {{Blom, Anna and Hallström, Teresia and Riesbeck, Kristian}}, issn = {{1872-9142}}, language = {{eng}}, pages = {{2808--2817}}, publisher = {{Pergamon Press Ltd.}}, series = {{Molecular Immunology}}, title = {{Complement evasion strategies of pathogens-Acquisition of inhibitors and beyond.}}, url = {{http://dx.doi.org/10.1016/j.molimm.2009.04.025}}, doi = {{10.1016/j.molimm.2009.04.025}}, volume = {{46}}, year = {{2009}}, }