Similarity between the group B and A streptococcal C5a peptidase genes

Cleary, P P; Handley, J.; Suvorov, Alexander; Podbielski, Andreas; Ferrieri, Patricia

doi:10.1128/iai.60.10.4239-4244.1992

Cited by 49 publications

(23 citation statements)

References 17 publications

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“…It has been noted previously that the scpB and scpA genes of beta-haemolytic streptococci are highly homologous (Cleary et al, 1992;Chmouryguina et al, 1996). Comparison of the nucleotide sequences of this gene, the lmb gene and other known genes in S. agalactiae and S. pyogenes displays an unusually high degree of similarity for these two genes (see Table 2).…”

Section: Discussionmentioning

confidence: 71%

“…This enzyme is anchored at the streptococcal cell wall and impairs the leukocyte recruitment to sites of infection through the cleavage of the chemotactic complement component C5a. Horizontal transfer of this gene among beta-haemolytic streptococci has been suggested, as the nucleotide sequence is highly conserved in these bacteria (Cleary et al, 1992;Chmouryguina et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

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Horizontal gene transfer and host specificity of beta‐haemolytic streptococci: the role of a putative composite transposon containing scpB and lmb

Franken

Haase

Brandt

et al. 2001

Molecular Microbiology

105

118

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Beta‐haemolytic streptococci are important human and animal pathogens: their genetic traits that are associated with the ability to infect human hosts remain, however, unclear. The surface protein, Lmb, mediates the adherence of Streptococcus agalactiae to human laminin. For further analysis of the corresponding gene, the adjacent genomic regions were sequenced. Lmb is localized on a putative composite transposon of 16 kb and is flanked by two copies of a novel insertion sequence element (ISSag2). It harbours the genes scpB and lmb, which are 98% identical with the respective genes of Streptococcus pyogenes. Analysis of the distribution of these genes and ISSag2 among 131 streptococcal strains revealed that all of the human isolates, but only 20% (12 of 61) of the animal isolates, contained scpB and lmb or their homologues. To investigate if the putative transposon can be mobilized, an erythromycin resistance marker was incorporated into the lmb gene of S. agalactiae. Screening for mutant strains with a regained susceptibility for erythromycin identified strains with a deletion of scpB, lmb, and one copy of ISSag2. We hypothesize that a horizontal gene transfer caused the exchange of scpB and lmb and that the ability of S. pyogenes, S. agalactiae and group C and G streptococcal strains to colonize or infect human hosts is dependent on their presence.

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Section: Discussionmentioning

confidence: 71%

Section: Introductionmentioning

confidence: 99%

Horizontal gene transfer and host specificity of beta‐haemolytic streptococci: the role of a putative composite transposon containing scpB and lmb

Franken

Haase

Brandt

et al. 2001

Molecular Microbiology

105

118

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“…The fact that all serotypes of GAS tested to date (8,10) and human isolates of group B (18,11) and G (12) streptococci produce a C5a peptidase or carry the scpA gene is reason to believe that specific cleavage of C5a chemotaxin contributes to the virulence of these streptococci. Earlier experiments in our laboratory with Tn916 and nitrosoguanidine mutagenesis did not conclusively establish that the peptidase is required for full virulence (25).…”

Section: Discussionmentioning

confidence: 99%

“…C5a is cleaved between the His-67 and Lys-68 residues of C5a, a region of the chemotaxin which binds to receptors located on the surface of polymorphonuclear leukocytes (PMNLs) (13,35). A similar peptidase was also shown to be expressed by human isolates of group B (11,18), C (unpublished data), and G (12) streptococci.…”

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confidence: 90%

C5a peptidase alters clearance and trafficking of group A streptococci by infected mice

et al. 1996

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Group A streptococcal C5a peptidase (SCPA) specifically cleaves the human serum chemotaxin C5a at the polymorphonuclear leukocyte (PMNL) binding site. This study tested the proposal that SCPA contributes to virulence by retarding the influx of inflammatory cells and clearance of streptococci during the first few hours after infection. To investigate the specific contribution of SCPA to the virulence of group A streptococci, scpA insertion and deletion mutants were created by directed plasmid insertion into scpA and gene replacement. The precise locations of insertion and deletion mutations were confirmed by PCR and DNA sequence analysis. The impact of mutation on virulence was investigated with a mouse air sac model of inflammation. Experiments evaluated clearance of streptococci from the air sac within 4 h after infection. SCPA ؊ streptococci were cleared more efficiently than wild-type bacteria. Localization of streptococci in lymph nodes and spleens of infected mice revealed a significant difference between mutant and wild-type streptococci. PMNLs and other granulocytes that infiltrated the air sac were quantitated by single-color flow cytometry. The total cellular infiltrate was greater and PMNLs dominated the granulocytic infiltrates of air sacs inoculated with SCPA ؊ mutant bacteria. The data obtained are consistent with the possibility that SCPA ؊ streptococci are initially cleared from the site of infection primarily by PMNLs. Moreover, mutant and wild-type streptococci followed different paths of dissemination. SCPA ؊ bacteria were transported to lymph nodes, whereas wild-type streptococci avoided transport to the lymph nodes and rapidly spread to the spleen.

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“…The C5a peptidase has been investigated as a vaccine candidate due to its widespread conservation throughout GAS (385). Genes nearly identical to scpA have also been found in both group B and G streptococci, although the expression of scpA in the group G streptococci appears to be restricted to the specific strains that are capable of infecting humans (119,123,124).…”

Section: Streptococcus Pyogenes (Group a Streptococci)mentioning

confidence: 99%

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Navarre

Schneewind

1999

Microbiol Mol Biol Rev

1,186

601

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SUMMARY The cell wall envelope of gram-positive bacteria is a macromolecular, exoskeletal organelle that is assembled and turned over at designated sites. The cell wall also functions as a surface organelle that allows gram-positive pathogens to interact with their environment, in particular the tissues of the infected host. All of these functions require that surface proteins and enzymes be properly targeted to the cell wall envelope. Two basic mechanisms, cell wall sorting and targeting, have been identified. Cell well sorting is the covalent attachment of surface proteins to the peptidoglycan via a C-terminal sorting signal that contains a consensus LPXTG sequence. More than 100 proteins that possess cell wall-sorting signals, including the M proteins of Streptococcus pyogenes, protein A of Staphylococcus aureus, and several internalins of Listeria monocytogenes, have been identified. Cell wall targeting involves the noncovalent attachment of proteins to the cell surface via specialized binding domains. Several of these wall-binding domains appear to interact with secondary wall polymers that are associated with the peptidoglycan, for example teichoic acids and polysaccharides. Proteins that are targeted to the cell surface include muralytic enzymes such as autolysins, lysostaphin, and phage lytic enzymes. Other examples for targeted proteins are the surface S-layer proteins of bacilli and clostridia, as well as virulence factors required for the pathogenesis of L. monocytogenes (internalin B) and Streptococcus pneumoniae (PspA) infections. In this review we describe the mechanisms for both sorting and targeting of proteins to the envelope of gram-positive bacteria and review the functions of known surface proteins.

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Similarity between the group B and A streptococcal C5a peptidase genes

Cited by 49 publications

References 17 publications

Horizontal gene transfer and host specificity of beta‐haemolytic streptococci: the role of a putative composite transposon containing scpB and lmb

Horizontal gene transfer and host specificity of beta‐haemolytic streptococci: the role of a putative composite transposon containing scpB and lmb

C5a peptidase alters clearance and trafficking of group A streptococci by infected mice

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

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