Identification of active variants of PARF in human pathogenic group C and group G streptococci leads to an amended description of its consensus motif

Barroso, Vanessa; Rohde, Manfred; Davies, Mark R.; Gillen, Christine M.; Nitsche-Schmitz, D. Patric; Dinkla, Katrin; Chhatwal, Gursharan S.

doi:10.1016/j.ijmm.2009.04.004

Cited by 11 publications

(31 citation statements)

References 19 publications

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“…equisimilis (20,42,48). This includes the M-protein gene, which is of central importance in the pathogenesis of S. pyogenes infections and used for epidemiologic typing (emm typing) of this species (3,6,19). S. dysgalactiae subsp.…”

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confidence: 99%

Delineation of Streptococcus dysgalactiae, Its Subspecies, and Its Clinical and Phylogenetic Relationship to Streptococcus pyogenes

Jensen

Kilian

2012

J Clin Microbiol

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The taxonomic status and structure of Streptococcus dysgalactiae have been the object of much confusion. Bacteria belonging to this species are usually referred to as Lancefield group C or group G streptococci in clinical settings in spite of the fact that these terms lack precision and prevent recognition of the exact clinical relevance of these bacteria. The purpose of this study was to develop an improved basis for delineation and identification of the individual species of the pyogenic group of streptococci in the clinical microbiology laboratory, with a special focus on S. dysgalactiae. We critically reexamined the genetic relationships of the species S. dysgalactiae, Streptococcus pyogenes, Streptococcus canis, and Streptococcus equi, which may share Lancefield group antigens, by phylogenetic reconstruction based on multilocus sequence analysis (MLSA) and 16S rRNA gene sequences and by emm typing combined with phenotypic characterization. Analysis of concatenated sequences of seven genes previously used for examination of viridans streptococci distinguished robust and coherent clusters. S. dysgalactiae consists of two separate clusters consistent with the two recognized subspecies dysgalactiae and equisimilis. Both taxa share alleles with S. pyogenes in several housekeeping genes, which invalidates identification based on single-locus sequencing. S. dysgalactiae, S. canis, and S. pyogenes constitute a closely related branch within the genus Streptococcus indicative of recent descent from a common ancestor, while S. equi is highly divergent from other species of the pyogenic group streptococci. The results provide an improved basis for identification of clinically important pyogenic group streptococci and explain the overlapping spectrum of infections caused by the species associated with humans.

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confidence: 99%

Delineation of Streptococcus dysgalactiae, Its Subspecies, and Its Clinical and Phylogenetic Relationship to Streptococcus pyogenes

Jensen

Kilian

2012

J Clin Microbiol

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“…The additional isolate was typed as stCQ343. None of isolates from Vellore was included in previous studies on collagen-binding M proteins [24], [25], [28], [29]. The S. pyogenes M31 strains included in binding experiments were not isolated in Vellore, but a courtesy of D. R. Johnson from the University of Minnesota Medical School.…”

Section: Methodsmentioning

confidence: 99%

“…This suggests collagen-binding M proteins as triggers of this disease [25], [28]. Their interaction with collagen is mediated by a (A/T/E) X YL XX LN amino acid sequence located in the N-terminal hypervariable region of the M protein and referred to as PARF ( p eptide a ssociated with r heumatic f ever) [28], [29]. Notably, the PARF motif is part of the M protein type 3 (M3), a protein that was used in a vaccination trial in which some of the vaccinees developed ARF or similar symptoms [23].…”

Section: Introductionmentioning

confidence: 99%

Region Specific and Worldwide Distribution of Collagen-Binding M Proteins with PARF Motifs among Human Pathogenic Streptococcal Isolates

et al. 2012

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Some of the variety of Streptococcus pyogenes and Streptococcus dysgalactiae ssp. equisimilis (SDSE) M proteins act as collagen-binding adhesins that facilitate acute infection. Moreover, their potential to trigger collagen autoimmunity has been implicated in the pathogenesis of acute rheumatic fever and attributed to a collagen-binding motif called PARF (peptide associated with rheumatic fever). For the first time we determine the rate of clinical isolates with collagen-binding M proteins that use a PARF motif (A/T/E)XYLXX(L/F)N in a defined geographic region, Vellore in South India. In this region both, incidence of streptococcal infections and prevalence of acute rheumatic fever are high. M proteins with PARF motif conferred collagen-binding activity to 3.9% of 153 S. pyogenes and 10.6% of 255 SDSE clinical isolates from Vellore. The PARF motif occurred in three S. pyogenes and 22 SDSE M protein types. In one of the S. pyogenes and five of the SDSE M proteins that contained the motif, collagen-binding was impaired, due to influences of other parts of the M protein molecule. The accumulated data on the collagen binding activity of certain M protein types allowed a reanalysis of published worldwide emm-typing data with the aim to estimate the rates of isolates that bind collagen via PARF. The results indicate that M proteins, which bind collagen via a PARF motif, are epidemiologically relevant in human infections, not only in Vellore. It is imperative to include the most relevant collagen-binding M types in vaccines. But when designing M protein based vaccines it should be considered that collagen binding motifs within the vaccine antigen remain potential risk factors.

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“…Alternatively, M proteins trigger autoimmune response by a mechanism that requires binding of collagen (Barroso et al, 2009;Dinkla et al, 2007;Dinkla et al, 2003). The rheumatogenic M protein of type 3 (Stollerman, 1969) that caused ARF and ARF-like symptoms in vaccinees (Massell et al, 1969), binds collagens to the streptococcal surface and causes their aggregation (Dinkla et al, 2003).…”

Section: Octapeptide Parf and Its Role In Arfmentioning

confidence: 99%

“…It depends on an (A/T/E)XYLXX(L/F)N octapeptide motif that is located in the N-terminal type-specific part of the M protein (Fig. 1) (Barroso et al, 2009;Dinkla et al, 2007;Reißmann et al, 2012) and contributes to acute infections by facilitating streptococcal colonization of the ECM (Dinkla et al, 2003;Nitsche et al, 2006). When injected into mice, M3 protein and other collagen-binding M proteins that carry the (A/T/E)XYLXX(L/F)N motif trigger production of anti-collagen IV antibodies.…”

Section: Octapeptide Parf and Its Role In Arfmentioning

confidence: 99%

Host–Pathogen Interactions in Streptococcal Immune Sequelae

Nitsche-Schmitz

Chhatwal

2012

Host-Pathogen Interactions in Streptococcal Diseases

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Identification of active variants of PARF in human pathogenic group C and group G streptococci leads to an amended description of its consensus motif

Cited by 11 publications

References 19 publications

Delineation of Streptococcus dysgalactiae, Its Subspecies, and Its Clinical and Phylogenetic Relationship to Streptococcus pyogenes

Delineation of Streptococcus dysgalactiae, Its Subspecies, and Its Clinical and Phylogenetic Relationship to Streptococcus pyogenes

Region Specific and Worldwide Distribution of Collagen-Binding M Proteins with PARF Motifs among Human Pathogenic Streptococcal Isolates

Host–Pathogen Interactions in Streptococcal Immune Sequelae

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