Several regions of the repeat domain of the<i>Staphylococcus caprae</i>autolysin, AtlC, are involved in fibronectin binding

Allignet, Jeanine; England, Patrick; Old, Iain G.; Solh, Névine El

doi:10.1111/j.1574-6968.2002.tb11305.x

Cited by 39 publications

(7 citation statements)

References 12 publications

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“…This strongly indicates that multivalent interactions are involved in the binding of Aaa to these plasma and ECM proteins. Such multivalent interactions have also been described for other adhesins, such as the Fn-binding autolysin/adhesin AtlC from S. caprae [19] and FnBPA or FnBPB, where different and partially repeated domains of the proteins are involved in binding to Fg, elastin, and Fn [8].…”

Section: Discussionmentioning

confidence: 67%

“…As the first member of the staphylococcal autolysin/adhesin family, we identified the 148-kDa AtlE from S. epidermidis that mediates attachment to polystyrene, adherence to Vn, and biofilm formation [16]. AtlE homologues, such as Aas from Staphylococcus saprophyticus [18], AtlC from Staphylococcus caprae [19], and Atl from S. aureus [20] bind to Fn. Like AtlE, the 137-kDa Atl mediates attachment to polystyrene and biofilm formation [21].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the Modular Design of the Autolysin/Adhesin Aaa from Staphylococcus Aureus

et al. 2012

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Background Staphylococcus aureus is a frequent cause of serious and life-threatening infections, such as endocarditis, osteomyelitis, pneumonia, and sepsis. Its adherence to various host structures is crucial for the establishment of diseases. Adherence may be mediated by a variety of adhesins, among them the autolysin/adhesins Atl and Aaa. Aaa is composed of three N-terminal repeated sequences homologous to a lysin motif (LysM) that can confer cell wall attachment and a C-terminally located cysteine, histidine-dependent amidohydrolase/peptidase (CHAP) domain having bacteriolytic activity in many proteins. Methodology/Principal Findings Here, we show by surface plasmon resonance that the LysM domain binds to fibrinogen, fibronectin, and vitronectin respresenting a novel adhesive function for this domain. Moreover, we demonstrated that the CHAP domain not only mediates the bacteriolytic activity, but also adherence to fibrinogen, fibronectin, and vitronectin, thus demonstrating for the first time an adhesive function for this domain. Adherence of an S. aureus aaa mutant and the complemented aaa mutant is slightly decreased and increased, respectively, to vitronectin, but not to fibrinogen and fibronectin, which might at least in part result from an increased expression of atl in the aaa mutant. Furthermore, an S. aureus atl mutant that showed enhanced adherence to fibrinogen, fibronectin, and endothelial cells also demonstrated increased aaa expression and production of Aaa. Thus, the redundant functions of Aaa and Atl might at least in part be interchangeable. Lastly, RT-PCR and zymographic analysis revealed that aaa is negatively regulated by the global virulence gene regulators agr and SarA. Conclusions/Significance We identified novel functions for two widely distributed protein domains, LysM and CHAP, i.e. the adherence to the extracellular matrix proteins fibrinogen, fibronectin, and vitronectin. The adhesive properties of Aaa might promote S. aureus colonization of host extracellular matrix and tissue, suggesting a role for Aaa in the pathogenesis of S. aureus infections.

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Section: Discussionmentioning

confidence: 67%

Section: Introductionmentioning

confidence: 99%

Characterization of the Modular Design of the Autolysin/Adhesin Aaa from Staphylococcus Aureus

et al. 2012

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“…This would seem to be the logical alternative mechanism for internalization as the other CoNS also have autolysins ( Albrecht et al, 2012 ). However, existing studies only describe an ability to bind to Fn through autolysin and/or become internalized but do not offer a mechanistic explanation ( Table 1 ) ( Hell et al, 1998 , 2003 ; Allignet et al, 1999 , 2001 , 2002 ; Szabados et al, 2008 ; Pereira et al, 2012 ; Hussain et al, 2015 ). It is also noteworthy that the involvement in the internalization process of the fibrinogen-binding protein Fbl produced in S. lugdunensis , a homolog of S. aureus ClfA, has also been investigated, with negative results ( Szabados et al, 2011 ).…”

Section: Staphylococcus Epidermidis and Other Coagulase-negamentioning

confidence: 99%

Staphylococcal Adhesion and Host Cell Invasion: Fibronectin-Binding and Other Mechanisms

2017

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Opportunistic bacteria from the genus Staphylococcus can cause life-threatening infections such as pneumonia, endocarditis, bone and joint infections, and sepsis. This pathogenicity is closely related to their capacity to bind directly to the extracellular matrix or to host cells. Adhesion is indeed the first step in the formation of biofilm or the invasion of host cells, which protect the bacteria from the host immune system and facilitate chronic infection. Adhesion relies on the expression of a repertoire of surface proteins called adhesins, notably microbial surface components recognizing adhesive matrix molecules. In this short review, we discuss the main pathway (FnBP-Fn-α5β1 integrin), as well as alternatives, through which Staphylococcus aureus adheres to and then invades non-professional phagocytic cells. We then examine the corresponding mechanisms for coagulase negative staphylococci. There is currently a little understanding of the molecular mechanisms that lead to internalization. Filling this gap in the literature would therefore be an important step toward limiting the duration of staphylococci infections in clinical practice.

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“…They included the fructose bisphosphate aldolase and two glyceraldehyde 3-phosphate dehydrogenases. Of note, the N-acetylmuramoyl-L-alanine amidase mentioned above is also known as a moonlighting protein [33]. …”

Section: Resultsmentioning

confidence: 99%

Contribution of sortase SrtA2 to Lactobacillus casei BL23 inhibition of Staphylococcus aureus internalization into bovine mammary epithelial cells

et al. 2017

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Probiotics have been considered as a promising strategy to prevent various diseases in both humans and animals. This approach has gained interest in recent years as a potential means to control bovine mastitis. In a previous study, we found that several L. casei strains, including BL23, were able to inhibit the internalization of S. aureus, a major etiologic agent of mastitis, into bovine mammary epithelial cells (bMEC). This antagonism required a direct contact between L. casei and bMEC or S. aureus, suggesting the inhibition relied on interactions between L. casei cell surface components and bMEC. In this study, we have investigated the impact of some candidates which likely influence bacteria host cell interactions. We have shown that L. casei BL23 fbpA retained its inhibitory potential, indicating that L. casei BL23 antagonism did not rely (solely) on competition between S. aureus and L. casei fibronectin-binding proteins for adhesion to bMEC. We have then investigated the impact of four sortase mutants, srtA1, srtA2, srtC1 and srtC2, and a double mutant (srtA1-srtA2) on L. casei BL23 inhibitory potential. Sortases are responsible for the anchoring on the bacterial cell wall of LPXTG-proteins, which reportedly play an important role in bacteria-host cell interaction. All the srt mutants tested presented a reduced inhibition capacity, the most pronounced effect being observed with the srtA2 mutant. A lower internalization capacity of L. casei srtA2 into bMEC was also observed. This was associated with several changes at the surface of L. casei BL23 srtA2 compared to the wild type (wt) strain, including altered abundance of some LPXTG- and moonlighting proteins, and modifications of cell wall structure. These results strongly support the role of sortase A2 in L. casei BL23 inhibition against S. aureus internalization. Deciphering the contribution of the cell surface components altered in srtA2 strain in the inhibition will require further investigation.

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Several regions of the repeat domain of theStaphylococcus capraeautolysin, AtlC, are involved in fibronectin binding

Cited by 39 publications

References 12 publications

Characterization of the Modular Design of the Autolysin/Adhesin Aaa from Staphylococcus Aureus

Characterization of the Modular Design of the Autolysin/Adhesin Aaa from Staphylococcus Aureus

Staphylococcal Adhesion and Host Cell Invasion: Fibronectin-Binding and Other Mechanisms

Contribution of sortase SrtA2 to Lactobacillus casei BL23 inhibition of Staphylococcus aureus internalization into bovine mammary epithelial cells

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