Gram&amp;mdash;Positive Adhesins

Talay, Susanne R.

doi:10.1159/000081691

Cited by 19 publications

(27 citation statements)

References 110 publications

(138 reference statements)

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“…This demonstrates that the binding of Shr is specific to a subset of ECM components. GAS expresses multiple fibronectin binding proteins on its surface (22,50). To test to the ability of Shr to mediate bacterial binding to fibronectin in the absence of the other GAS fibronectin-binding proteins, we expressed Shr in a heterologous host.…”

Section: Resultsmentioning

confidence: 99%

“…Analysis of variance (ANOVA) followed by the Tukey honest significant difference (HSD) post hoc test was used for multigroup comparisons; a P value of Յ0.05 was considered to be significant. Zebrafish survival data were analyzed by the method of Reed and Muench for the calculation of the LD 50 . KaplanMeier plots of zebrafish survival were used to compare infections by the wildtype, mutant, and complemented GAS strains.…”

Section: Methodsmentioning

confidence: 99%

“…This amphipathic surface molecule has been proposed to counteract the electrostatic repulsion between the bacteria and host surfaces. The subsequent step in adherence involves high-affinity binding to host components and is mediated by a large number of adhesins (6,22,50). These include M proteins from several serotypes, F and F-like proteins, the hyaluronic acid capsule, and the recently described pili (1,28).…”

mentioning

confidence: 99%

“…GAS expresses several surface molecules that bind collagen or laminin (10,14,24,52). However, many more GAS adhesins target the ECM component fibronectin (22,50). At least 11 fibronectinbinding proteins have been identified in GAS thus far, including F1 (SfbI), F2 (PFBP), Fbp54, SOF, and several M proteins.…”

mentioning

confidence: 99%

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Shr Is a Broad-Spectrum Surface Receptor That Contributes to Adherence and Virulence in Group A Streptococcus

Fisher

Huang

et al. 2008

Infect Immun

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Group A streptococcus (GAS) is a common hemolytic pathogen that produces a range of suppurative infections and autoimmune sequelae in humans. Shr is an exported protein in GAS, which binds in vitro to hemoglobin, myoglobin, and the hemoglobin-haptoglobin complex. We previously reported that Shr is found in association with whole GAS cells and in culture supernatant. Here, we demonstrate that cell-associated Shr could not be released from the bacteria by the muralytic enzyme mutanolysin and was instead localized to the membrane. Shr was available, however, on the exterior of GAS, exposed to the extracellular environment. In vitro binding and competition assays demonstrated that in addition to hemoprotein binding, purified Shr specifically interacts with immobilized fibronectin and laminin. The absence of typical fibronectin-binding motifs indicates that a new protein pattern is involved in the binding of Shr to the extracellular matrix. Recombinant Lactococcus lactis cells expressing Shr on the bacterial surface gained the ability to bind to immobilized fibronectin, suggesting that Shr can function as an adhesin. The inactivation of shr resulted in a 40% reduction in the attachment to human epithelial cells in comparison to the parent strain. GAS infection elicited a high titer of Shr antibodies in sera from convalescent mice, demonstrating that Shr is expressed in vivo. The shr mutant was attenuated for virulence in an intramuscular zebrafish model system. In summary, this study identifies Shr as being a new microbial surface component recognizing adhesive matrix molecules in GAS that mediates attachment to epithelial cells and contributes to the infection process.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Shr Is a Broad-Spectrum Surface Receptor That Contributes to Adherence and Virulence in Group A Streptococcus

Fisher

Huang

et al. 2008

Infect Immun

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“…In addition, lipoproteins such as ABC metal permease PsaA (13), a pathogenicity-island encoded protein PsrP (14,15) and pili, expressed by a subclass of pneumococci (16,17) have been suggested to have adhesive functions. Furthermore, a number of pneumococcal proteins interacts with fibronectin or plasminogen, a strategy commonly employed by many invading pathogens to colonize or disseminate within the host (18,19). These include pneumococcal adherence and virulence factor (Pav) A, PavB, plasmin and fibronectin-binding protein (Pfb) A as well as PfbB that have been identified as plasminogen-and fibronectin-binding proteins (20 -24).…”

mentioning

confidence: 99%

Streptococcus pneumoniae Endopeptidase O (PepO) Is a Multifunctional Plasminogen- and Fibronectin-binding Protein, Facilitating Evasion of Innate Immunity and Invasion of Host Cells

Agarwal

Kuchipudi

Fulde

et al. 2013

Journal of Biological Chemistry

110

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Background: Pneumococci have developed multiple strategies to infect the host. Results: PepO is a ubiquitously expressed pneumococcal protein that interacts with host proteins and facilitates host cell invasion and evasion of innate immunity. Conclusion: PepO is a plasminogen-and fibronectin-binding pneumococcal invasin. Significance: Understanding the mechanism of pneumococcal interaction with host aids designing better therapeutical strategies and gaining control over the pathogen.

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Cytopathology of Pathogenic Prokaryotes

Brogden

2009

Ultrastructural Pathology the Comparative Cellular Basis of Disease

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Gram—Positive Adhesins

Cited by 19 publications

References 110 publications

Shr Is a Broad-Spectrum Surface Receptor That Contributes to Adherence and Virulence in Group A Streptococcus

Shr Is a Broad-Spectrum Surface Receptor That Contributes to Adherence and Virulence in Group A Streptococcus

Streptococcus pneumoniae Endopeptidase O (PepO) Is a Multifunctional Plasminogen- and Fibronectin-binding Protein, Facilitating Evasion of Innate Immunity and Invasion of Host Cells

Cytopathology of Pathogenic Prokaryotes

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