2.50
Hdl Handle:
http://hdl.handle.net/10033/19652
Title:
Identification of a streptococcal octapeptide motif involved in acute rheumatic fever.
Authors:
Dinkla, Katrin; Nitsche-Schmitz, D Patric; Barroso, Vanessa; Reissmann, Silvana; Johansson, Helena M; Frick, Inga-Maria; Rohde, Manfred ( 0000-0003-0522-3580 ) ; Chhatwal, Gursharan S
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.
Affiliation:
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
Citation:
Identification of a streptococcal octapeptide motif involved in acute rheumatic fever. 2007, 282 (26):18686-93 J. Biol. Chem.
Journal:
The Journal of biological chemistry
Issue Date:
29-Jun-2007
URI:
http://hdl.handle.net/10033/19652
DOI:
10.1074/jbc.M701047200
PubMed ID:
17452321
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorDinkla, Katrinen
dc.contributor.authorNitsche-Schmitz, D Patricen
dc.contributor.authorBarroso, Vanessaen
dc.contributor.authorReissmann, Silvanaen
dc.contributor.authorJohansson, Helena Men
dc.contributor.authorFrick, Inga-Mariaen
dc.contributor.authorRohde, Manfreden
dc.contributor.authorChhatwal, Gursharan Sen
dc.date.accessioned2008-03-04T13:25:29Zen
dc.date.available2008-03-04T13:25:29Zen
dc.date.issued2007-06-29en
dc.identifier.citationIdentification of a streptococcal octapeptide motif involved in acute rheumatic fever. 2007, 282 (26):18686-93 J. Biol. Chem.en
dc.identifier.issn0021-9258en
dc.identifier.pmid17452321en
dc.identifier.doi10.1074/jbc.M701047200en
dc.identifier.urihttp://hdl.handle.net/10033/19652en
dc.description.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.en
dc.language.isoenen
dc.subject.meshAcute Diseaseen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAnimalsen
dc.subject.meshAntibodies, Bacterialen
dc.subject.meshAutoantibodiesen
dc.subject.meshAutoimmunityen
dc.subject.meshBacterial Proteinsen
dc.subject.meshBiological Markersen
dc.subject.meshCollagen Type IVen
dc.subject.meshFemaleen
dc.subject.meshHumansen
dc.subject.meshMiceen
dc.subject.meshMice, Inbred C3Hen
dc.subject.meshMicroscopy, Electron, Scanningen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshPeptide Fragmentsen
dc.subject.meshRheumatic Feveren
dc.subject.meshSpecific Pathogen-Free Organismsen
dc.subject.meshStreptococcusen
dc.subject.meshSurface Plasmon Resonanceen
dc.subject.meshVirulenceen
dc.titleIdentification of a streptococcal octapeptide motif involved in acute rheumatic fever.en
dc.typeArticleen
dc.contributor.departmentDepartment of Microbial Pathogenesis, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.en
dc.identifier.journalThe Journal of biological chemistryen

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