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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

Jarva, Hanna LU ; Janulczyk, Robert LU ; Hellwage, Jens; Zipfel, Peter F; Björck, Lars LU and Meri, Seppo (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)
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author
organization
publishing date
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
2007-10-24 14:17:35
date last changed
2017-09-17 07:25:05
@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},
}