Expression of the Arp protein, a member of the M protein family, is not sufficient to inhibit phagocytosis of Streptococcus pyogenes

Husmann, L K; Scott, June R.; Lindahl, Gunnar; Stenberg, Lars

doi:10.1128/iai.63.1.345-348.1995

Cited by 79 publications

(32 citation statements)

References 36 publications

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“…Although the growth of the tested strains was lower in hirudin, their relative growth rate was the same in heparin and hirudin. As noted by several authors, there was pronounced interexperimental variation (Husmann et al, 1995;Thern et al, 1998;Kotarsky et al, 2000). Nevertheless, the overall interpretation of the results was clear: in all experiments, strains expressing proteins deleted for the major FH -FHL-1-binding transformed with constructs encoding wild-type M5 or truncated M5 variants was analysed.…”

Section: Role Of the Fh -Fhl-1-binding Regions In Phagocytosis Resistmentioning

confidence: 90%

“…GAS were harvested by centrifugation, washed twice with PBS (0.15 M NaCl, 0.03 M phosphate, pH 7.2) and stored in PBS containing 0.02% sodium azide. M5 protein encoding plasmids pLZ12(spec ) is a shuttle plasmid carrying a spectinomycin resistance marker (Husmann et al, 1995). Cloning of the emm5 gene in pLZ12(spec ) has been described previously .…”

Section: Bacterial Strains and Culture Conditionsmentioning

confidence: 99%

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Group A streptococcal phagocytosis resistance is independent of complement factor H and factor H-like protein 1 binding

Kotarsky

Gustafsson

Svensson

et al. 2002

Molecular Microbiology

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SummaryFactor H (FH) and factor H-like protein 1 (FHL-1) regulate complement activation through the alternative pathway. Several extracellular bacterial pathogens, prime targets for the complement system, bind FH and FHL-1, thereby acquiring a potential mechanism for minimizing complement deposition on their surface. For group A streptococci (GAS), surfacebound antiphagocytic M proteins mediate the interaction. To study the role of the FH -FHL-1 interaction for complement deposition and opsonophagocytosis of GAS, we first constructed a set of truncated M5 protein variants and expressed them on the surface of a homologous M-negative GAS strain. Binding experiments with the resulting strains demonstrated that the major FH -FHL-1 binding is located in a 42-amino-acid region within the N-terminal third of M5. Measurement of bacteria-bound complement factor C3 after incubation in plasma showed that the presence of this region had little impact upon complement deposition through the alternative pathway. Moreover, streptococci expressing M5 proteins lacking the major FH and FHL-1 binding sequence resisted phagocytosis in human blood as efficiently as bacteria expressing the wild-type protein. Consequently, the data suggest that the binding of the regulators of the alternative pathway is of limited importance for GAS phagocytosis resistance.

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Section: Role Of the Fh -Fhl-1-binding Regions In Phagocytosis Resistmentioning

confidence: 90%

Section: Bacterial Strains and Culture Conditionsmentioning

confidence: 99%

Group A streptococcal phagocytosis resistance is independent of complement factor H and factor H-like protein 1 binding

Kotarsky

Gustafsson

Svensson

et al. 2002

Molecular Microbiology

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“…The serotype M1 S. pyogenes strain SF370 was obtained from the ATCC. Plasmids pG + host 9 (Fontaine et al ., 2003), was generously provided by E. Maguin (INRA, Jouy en Josas, France), pCM18 (Hansen et al ., 2001) by C. Robinson (AHT, Newmarket, UK), and pLZ12spec (Husmann et al ., 1995) by G. Lindahl (University of Lund, Sweden). S. pyogenes was grown, without shaking, in THY broth or THY blood‐agar plates (Fontaine et al ., 2003), at 37°C and 5% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

Pili mediate specific adhesion of Streptococcus pyogenes to human tonsil and skin

Smith²,

et al. 2007

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SummaryVery little is known about the biological functions of pili that have recently been found to be expressed by important Gram-positive pathogens such as Corynebacterium diphtheriae, Streptococcus agalacticae, S. pneumoniae and S. pyogenes. Using various ex vivo tissue and cellular models, here we show that pili mediate adhesion of serotype M1 S. pyogenes strain SF370 to both human tonsil epithelium and primary human keratinocytes, which represent the two main sites of infection by this human-specific pathogen. Mutants lacking minor pilus subunits retained the ability to express cell-surface pili, but these were functionally defective. In contrast to above, pili were not required for S. pyogenes adhesion to either immortalized HEp-2 or A549 cells, highlighting an important limitation of these extensively used adhesion/invasion models. Adhering bacteria were internalized very effectively by both HEp-2 and A549 cells, but not by tonsil epithelium or primary keratinocytes. While pili acted as the primary adhesin, the surface M1 protein clearly enhanced adhesion to tonsil, but surprisingly, had the opposite effect on adhesion to keratinocytes. These studies provide clear evidence that S. pyogenes pili display an adhesive specificity for clinically relevant human tissues and are likely to play a critical role in the initial stages of infection.

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“…These primers created SalI and PstI sites at the 3′ end of comR-US and the 5′ end of comR-DS respectively. The aad9 gene was amplified from pLZ12Spec (Husmann et al, 1995) using primers LMW5/LMW6 generating a SalI site at the 5′ and a PstI site at the 3′ ends. Two resulting PCR fragments were fused at SalI sites by in vitro ligation.…”

Section: Construction Of Mutants and Complementation Plasmidsmentioning

confidence: 99%

A novel double‐tryptophan peptide pheromone controls competence in Streptococcus spp. via an Rgg regulator

Mashburn‐Warren¹,

Morrison²,

Federle³

2010

Molecular Microbiology

270

590

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SummaryAll streptococcal genomes encode the alternative sigma factor SigX and 21 SigX-dependent proteins required for genetic transformation, yet no pyogenic streptococci are known to develop competence. Resolving this paradox may depend on understanding the regulation of sigX. We report the identification of a regulatory circuit linked to the sigX genes of mutans, pyogenic, and bovis streptococci that uses a novel small, double-tryptophan-containing sigX-inducing peptide (XIP) pheromone. In all three groups, the XIP gene (comS), and sigX have identical, non-canonical promoters consisting of 9 bp inverted repeats separated from a -10 hexamer by 19 bp. comS is adjacent to a gene encoding a putative transcription factor of the Rgg family and is regulated by its product, which we designate ComR. Deletion of comR or comS in Streptococcus mutans abolished transformability, as did deletion of the oligopeptide permease subunit oppD, suggesting that XIP is imported. Providing S. mutans with synthetic fragments of ComS revealed that seven C-terminal residues, including the WW motif, cause robust induction of both sigX and the competent state. We propose that this circuit is the proximal regulator of sigX in S. mutans, and we infer that it controls competence in a parallel way in all pyogenic and bovis streptococci.

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Expression of the Arp protein, a member of the M protein family, is not sufficient to inhibit phagocytosis of Streptococcus pyogenes

Cited by 79 publications

References 36 publications

Group A streptococcal phagocytosis resistance is independent of complement factor H and factor H-like protein 1 binding

Group A streptococcal phagocytosis resistance is independent of complement factor H and factor H-like protein 1 binding

Pili mediate specific adhesion of Streptococcus pyogenes to human tonsil and skin

A novel double‐tryptophan peptide pheromone controls competence in Streptococcus spp. via an Rgg regulator

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