Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q
(2007) In Journal of Biological Chemistry 282(24). p.17530-17536- Abstract
- Recent epidemiological data on diseases caused by beta-hemolytic streptococci belonging to Lancefield group C and G ( GCS, GGS) underline that they are an emerging threat to human health. Among various virulence factors expressed by GCS and GGS isolates from human infections, M and M-like proteins are considered important because of their anti-phagocytic activity. In addition, protein G has been implicated in the accumulation of IgG on the bacterial surface through non-immune binding. The function of this interaction, however, is still unknown. Using isogenic mutants lacking protein G or the M-like protein FOG ( group G streptococci), respectively, we could show that FOG contributes substantially to IgG binding. A detailed characterization... (More)
- Recent epidemiological data on diseases caused by beta-hemolytic streptococci belonging to Lancefield group C and G ( GCS, GGS) underline that they are an emerging threat to human health. Among various virulence factors expressed by GCS and GGS isolates from human infections, M and M-like proteins are considered important because of their anti-phagocytic activity. In addition, protein G has been implicated in the accumulation of IgG on the bacterial surface through non-immune binding. The function of this interaction, however, is still unknown. Using isogenic mutants lacking protein G or the M-like protein FOG ( group G streptococci), respectively, we could show that FOG contributes substantially to IgG binding. A detailed characterization of the interaction between IgG and FOG revealed its ability to bind the Fc region of human IgG and its binding to the subclasses IgG1, IgG2, and IgG4. FOG was also found to bind IgG of several animal species. Surface plasmon resonance measurements indicate a high affinity to human IgG with a dissociation constant of 2.4 pM. The binding site was localized in a central motif of FOG. It has long been speculated about anti-opsonic functions of streptococcal Fc-binding proteins. The presented data for the first time provide evidence and, furthermore, indicate functional differences between protein G and FOG. By obstructing the interaction between IgG and C1q, protein G prevented recognition by the classical pathway of the complement system. In contrast, IgG that was bound to FOG remained capable of binding C1q, an effect that may have important consequences in the pathogenesis of GGS infections. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/650886
- author
- Nitsche-Schmitz, D. Patric ; Linge, Helena LU ; Sastalla, Inka ; Reissmann, Silvana ; Frick, Inga-Maria LU and Chhatwal, Gursharan S.
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 282
- issue
- 24
- pages
- 17530 - 17536
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000247084500023
- scopus:34547113538
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M702612200
- language
- English
- LU publication?
- yes
- id
- 4cd0ffa9-2be0-4bc7-9967-51bc167d78be (old id 650886)
- date added to LUP
- 2016-04-01 11:44:10
- date last changed
- 2022-04-05 04:17:16
@article{4cd0ffa9-2be0-4bc7-9967-51bc167d78be, abstract = {{Recent epidemiological data on diseases caused by beta-hemolytic streptococci belonging to Lancefield group C and G ( GCS, GGS) underline that they are an emerging threat to human health. Among various virulence factors expressed by GCS and GGS isolates from human infections, M and M-like proteins are considered important because of their anti-phagocytic activity. In addition, protein G has been implicated in the accumulation of IgG on the bacterial surface through non-immune binding. The function of this interaction, however, is still unknown. Using isogenic mutants lacking protein G or the M-like protein FOG ( group G streptococci), respectively, we could show that FOG contributes substantially to IgG binding. A detailed characterization of the interaction between IgG and FOG revealed its ability to bind the Fc region of human IgG and its binding to the subclasses IgG1, IgG2, and IgG4. FOG was also found to bind IgG of several animal species. Surface plasmon resonance measurements indicate a high affinity to human IgG with a dissociation constant of 2.4 pM. The binding site was localized in a central motif of FOG. It has long been speculated about anti-opsonic functions of streptococcal Fc-binding proteins. The presented data for the first time provide evidence and, furthermore, indicate functional differences between protein G and FOG. By obstructing the interaction between IgG and C1q, protein G prevented recognition by the classical pathway of the complement system. In contrast, IgG that was bound to FOG remained capable of binding C1q, an effect that may have important consequences in the pathogenesis of GGS infections.}}, author = {{Nitsche-Schmitz, D. Patric and Linge, Helena and Sastalla, Inka and Reissmann, Silvana and Frick, Inga-Maria and Chhatwal, Gursharan S.}}, issn = {{1083-351X}}, language = {{eng}}, number = {{24}}, pages = {{17530--17536}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q}}, url = {{http://dx.doi.org/10.1074/jbc.M702612200}}, doi = {{10.1074/jbc.M702612200}}, volume = {{282}}, year = {{2007}}, }