Streptococcus pneumoniae evades complement attack and opsonophagocytosis by expressing the pspC locus-encoded Hic protein that binds to short consensus repeats 8-11 of factor H
(2002) In Journal of Immunology 168(4). p.1886-1894- Abstract
- Streptococcus pneumoniae is an important cause of upper and lower respiratory tract infections, meningitis, peritonitis, bacterial arthritis, and sepsis. Here we have studied a novel immune evasion mechanism of serotype 3 pneumococci, which are particularly resistant to phagocytosis. On their surfaces the bacteria express the factor H-binding inhibitor of complement (Hie), a protein of the pneumococcal surface protein C family. Using radioligand binding, microtiter plate assays, surface plasmon resonance analysis, and recombinant constructs of factor H, we located the binding site of Hie to short consensus repeats (SCRs) 8-11 in the middle part of factor H. This represents a novel microbial interaction region on factor H. The only other... (More)
- Streptococcus pneumoniae is an important cause of upper and lower respiratory tract infections, meningitis, peritonitis, bacterial arthritis, and sepsis. Here we have studied a novel immune evasion mechanism of serotype 3 pneumococci, which are particularly resistant to phagocytosis. On their surfaces the bacteria express the factor H-binding inhibitor of complement (Hie), a protein of the pneumococcal surface protein C family. Using radioligand binding, microtiter plate assays, surface plasmon resonance analysis, and recombinant constructs of factor H, we located the binding site of Hie to short consensus repeats (SCRs) 8-11 in the middle part of factor H. This represents a novel microbial interaction region on factor H. The only other ligand known so far for SCRs 8-11 of factor H is C-reactive protein (CRP), an acute phase protein that binds to the pneumococcal C-polysaccharide. The binding sites of Hie and CRP within the SCR8-11 region were different, however, because CRP did not inhibit the binding of Hie and required calcium for binding. Binding of factor H to Hic-expressing pneumococci promoted factor I-mediated cleavage of C3b and restricted phagocytosis of pneumococci. Thus, virulent pneumococci avoid complement attack and opsonophagocytosis by recruiting functionally active factor H with the Hie surface protein. Hie binds to a previously unrecognized microbial interaction site in the middle part of factor H. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/343407
- author
- Jarva, Hanna LU ; Janulczyk, Robert LU ; Hellwage, Jens ; Zipfel, Peter F ; Björck, Lars LU and Meri, Seppo
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Immunology
- volume
- 168
- issue
- 4
- pages
- 1886 - 1894
- publisher
- American Association of Immunologists
- external identifiers
-
- wos:000173771000050
- pmid:11823523
- scopus:0037083508
- ISSN
- 1550-6606
- language
- English
- LU publication?
- yes
- id
- 10bfe934-46fd-4ce3-8980-72379c805bb2 (old id 343407)
- date added to LUP
- 2016-04-01 16:22:45
- date last changed
- 2022-02-20 05:39:16
@article{10bfe934-46fd-4ce3-8980-72379c805bb2,
abstract = {{Streptococcus pneumoniae is an important cause of upper and lower respiratory tract infections, meningitis, peritonitis, bacterial arthritis, and sepsis. Here we have studied a novel immune evasion mechanism of serotype 3 pneumococci, which are particularly resistant to phagocytosis. On their surfaces the bacteria express the factor H-binding inhibitor of complement (Hie), a protein of the pneumococcal surface protein C family. Using radioligand binding, microtiter plate assays, surface plasmon resonance analysis, and recombinant constructs of factor H, we located the binding site of Hie to short consensus repeats (SCRs) 8-11 in the middle part of factor H. This represents a novel microbial interaction region on factor H. The only other ligand known so far for SCRs 8-11 of factor H is C-reactive protein (CRP), an acute phase protein that binds to the pneumococcal C-polysaccharide. The binding sites of Hie and CRP within the SCR8-11 region were different, however, because CRP did not inhibit the binding of Hie and required calcium for binding. Binding of factor H to Hic-expressing pneumococci promoted factor I-mediated cleavage of C3b and restricted phagocytosis of pneumococci. Thus, virulent pneumococci avoid complement attack and opsonophagocytosis by recruiting functionally active factor H with the Hie surface protein. Hie binds to a previously unrecognized microbial interaction site in the middle part of factor H.}},
author = {{Jarva, Hanna and Janulczyk, Robert and Hellwage, Jens and Zipfel, Peter F and Björck, Lars and Meri, Seppo}},
issn = {{1550-6606}},
language = {{eng}},
number = {{4}},
pages = {{1886--1894}},
publisher = {{American Association of Immunologists}},
series = {{Journal of Immunology}},
title = {{Streptococcus pneumoniae evades complement attack and opsonophagocytosis by expressing the pspC locus-encoded Hic protein that binds to short consensus repeats 8-11 of factor H}},
volume = {{168}},
year = {{2002}},
}