Identification of a streptococcal octapeptide motif involved in acute rheumatic fever.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Nitsche-Schmitz, D Patric
Johansson, Helena M
Chhatwal, Gursharan S
MetadataShow full item record
AbstractAcute 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.
CitationIdentification of a streptococcal octapeptide motif involved in acute rheumatic fever. 2007, 282 (26):18686-93 J. Biol. Chem.
AffiliationDepartment of Microbial Pathogenesis, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
The following license files are associated with this item:
- Identification of active variants of PARF in human pathogenic group C and group G streptococci leads to an amended description of its consensus motif.
- Authors: Barroso V, Rohde M, Davies MR, Gillen CM, Nitsche-Schmitz DP, Dinkla K, Chhatwal GS
- Issue date: 2009 Dec
- Rheumatic fever-associated Streptococcus pyogenes isolates aggregate collagen.
- Authors: Dinkla K, Rohde M, Jansen WT, Kaplan EL, Chhatwal GS, Talay SR
- Issue date: 2003 Jun
- Identification of cardiac autoantigens in human heart cDNA libraries using acute rheumatic fever sera.
- Authors: Eichbaum QG, Beatty DW, Parker MI
- Issue date: 1994 Apr
- Mapping a conserved conformational epitope from the M protein of group A streptococci.
- Authors: Relf WA, Cooper J, Brandt ER, Hayman WA, Anders RF, Pruksakorn S, Currie B, Saul A, Good MF
- Issue date: 1996 Jan-Feb
- Identification of T cell autoepitopes that cross-react with the C-terminal segment of the M protein of group A streptococci.
- Authors: Pruksakorn S, Currie B, Brandt E, Phornphutkul C, Hunsakunachai S, Manmontri A, Robinson JH, Kehoe MA, Galbraith A, Good MF
- Issue date: 1994 Aug