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Identification of a streptococcal octapeptide motif involved in acute rheumatic fever

Dinkla, Katrin; Nitsche-Schmitz, D. Patric; Barroso, Vanessa; Reissmann, Silvana; Linge, Helena LU ; Frick, Inga-Maria LU ; Rohde, Manfred and Chhatwal, Gursharan S. (2007) In Journal of Biological Chemistry 282(26). p.18686-18693
Abstract
Acute rheumatic fever is a serious autoimmune sequela of pharyngitis caused by certain group A streptococci. One mechanism applied by streptococcal strains capable of causing acute rheumatic fever is formation of an autoantigenic complex with human collagen IV. In some geographic regions with a high incidence of acute rheumatic fever pharyngeal carriage of group C and group G streptococci prevails. Examination of such strains revealed the presence of M-like surface proteins that bind human collagen. Using a peptide array and recombinant proteins with targeted amino acid substitutions, we could demonstrate that formation of collagen complexes during streptococcal infections depends on an octapeptide motif, which is present in collagen... (More)
Acute rheumatic fever is a serious autoimmune sequela of pharyngitis caused by certain group A streptococci. One mechanism applied by streptococcal strains capable of causing acute rheumatic fever is formation of an autoantigenic complex with human collagen IV. In some geographic regions with a high incidence of acute rheumatic fever pharyngeal carriage of group C and group G streptococci prevails. Examination of such strains revealed the presence of M-like surface proteins that bind human collagen. Using a peptide array and recombinant proteins with targeted amino acid substitutions, we could demonstrate that formation of collagen complexes during streptococcal infections depends on an octapeptide motif, which is present in collagen binding M and M-like proteins of different beta-hemolytic streptococcal species. Mice immunized with streptococcal proteins that contain the collagen binding octapeptide motif developed high serum titers of anti-collagen antibodies. In sera of rheumatic fever patients such a collagen autoimmune response was accompanied by specific reactivity against the collagen-binding proteins, linking the observed effect to clinical cases. Taken together, the data demonstrate that the identified octapeptide motif through its action on collagen plays a crucial role in the pathogenesis of rheumatic fever. Eradication of streptococci that express proteins with the collagen binding motif appears advisable for controlling rheumatic fever. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
282
issue
26
pages
18686 - 18693
publisher
ASBMB
external identifiers
  • wos:000247475300006
  • scopus:34547127900
ISSN
1083-351X
DOI
10.1074/jbc.M701047200
language
English
LU publication?
yes
id
c96f9f94-1b4e-4969-bd5f-5ca9476ef76f (old id 648831)
date added to LUP
2007-12-07 12:26:35
date last changed
2017-07-23 03:47:09
@article{c96f9f94-1b4e-4969-bd5f-5ca9476ef76f,
  abstract     = {Acute rheumatic fever is a serious autoimmune sequela of pharyngitis caused by certain group A streptococci. One mechanism applied by streptococcal strains capable of causing acute rheumatic fever is formation of an autoantigenic complex with human collagen IV. In some geographic regions with a high incidence of acute rheumatic fever pharyngeal carriage of group C and group G streptococci prevails. Examination of such strains revealed the presence of M-like surface proteins that bind human collagen. Using a peptide array and recombinant proteins with targeted amino acid substitutions, we could demonstrate that formation of collagen complexes during streptococcal infections depends on an octapeptide motif, which is present in collagen binding M and M-like proteins of different beta-hemolytic streptococcal species. Mice immunized with streptococcal proteins that contain the collagen binding octapeptide motif developed high serum titers of anti-collagen antibodies. In sera of rheumatic fever patients such a collagen autoimmune response was accompanied by specific reactivity against the collagen-binding proteins, linking the observed effect to clinical cases. Taken together, the data demonstrate that the identified octapeptide motif through its action on collagen plays a crucial role in the pathogenesis of rheumatic fever. Eradication of streptococci that express proteins with the collagen binding motif appears advisable for controlling rheumatic fever.},
  author       = {Dinkla, Katrin and Nitsche-Schmitz, D. Patric and Barroso, Vanessa and Reissmann, Silvana and Linge, Helena and Frick, Inga-Maria and Rohde, Manfred and Chhatwal, Gursharan S.},
  issn         = {1083-351X},
  language     = {eng},
  number       = {26},
  pages        = {18686--18693},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Identification of a streptococcal octapeptide motif involved in acute rheumatic fever},
  url          = {http://dx.doi.org/10.1074/jbc.M701047200},
  volume       = {282},
  year         = {2007},
}