The Scl1 of M41-type group A Streptococcus binds the high-density lipoprotein

Gao, Yumin; Liang, Chunwei; Zhao, Ruidong; Łukomski, Sławomir; Han, Runlin

doi:10.1111/j.1574-6968.2010.02013.x

Cited by 13 publications

(17 citation statements)

References 27 publications

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“…The two S. pyogenes bacterial collagens, Scl1 and Scl2, have sequences indicating they are anchored on the cell surface and have been shown to bind to a variety of host proteins. Depending on the specific serotype, the non-collagenous V-domain of Scl1 may bind to high-density lipoprotein (HDL) (Gao et al 2010), low-density lipoprotein (LDL) (Han et al 2006a), factor H (Caswell et al 2008a), complement factor H-related protein 1 (CFHR1) (Reuter et al 2010), or the extra cellular matrix (ECM) proteins fibronectin and laminin (Caswell et al 2009). Binding to these components helps S. pyogenes escape from complement-regulated phagocytosis and enhances its adherence to the macrophages and ECM.…”

Section: Biological Role Of Bacterial Collagen-like Proteinsmentioning

confidence: 99%

Bacterial collagen-like proteins that form triple-helical structures

Ramshaw

et al. 2014

Journal of Structural Biology

126

133

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A large number of collagen-like proteins have been identified in bacteria during the past ten years, principally from analysis of genome databases. These bacterial collagens share the distinctive Gly-Xaa-Yaa repeating amino acid sequence of animal collagens which underlies their unique triple-helical structure. A number of the bacterial collagens have been expressed in E. coli, and they all adopt a triple-helix conformation. Unlike animal collagens, these bacterial proteins do not contain the post-translationally modified amino acid, hydroxyproline, which is known to stabilize the triple-helix structure and may promote self-assembly. Despite the absence of collagen hydroxylation, the triple-helix structures of the bacterial collagens studied exhibit a high thermal stability of 35–39 °C, close to that seen for mammalian collagens. These bacterial collagens are readily produced in large quantities by recombinant methods, either in the original amino acid sequence or in genetically manipulated sequences. This new family of recombinant, easy to modify collagens could provide a novel system for investigating structural and functional motifs in animal collagens and could also form the basis of new biomedical materials with designed structural properties and functions.

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Section: Biological Role Of Bacterial Collagen-like Proteinsmentioning

confidence: 99%

Bacterial collagen-like proteins that form triple-helical structures

Ramshaw

et al. 2014

Journal of Structural Biology

126

133

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“…3A, top panel). To prevent the possibility of serum proteins binding to Scl-1 (21,22,(25)(26)(27) and affecting phagocytosis, bacteria were not preop-sonized or incubated in the presence of human serum during phagocytosis assays or subsequent in vitro cell-based assays. Control treatment of the neutrophils with cyt D to prevent phagocytosis effectively eliminated the fluorescent signal and validated our assay specificity (Fig.…”

Section: Scl-1 Is Important For Bacterial Persistence In a Mouse Modementioning

confidence: 99%

“…In other, less virulent GAS serotype strains, Scl-1 has been shown to participate in biofilm formation (16,17), attachment to extracellular matrix proteins (18), and attachment to lung epithelial cells (15,19,20) but not pharyngeal cells (14). Studies using recombinant Scl-1 have shown that the protein, via its serotype-hypervariable N terminus, can bind a variety of host proteins, including serum lipoproteins (21,22), integrins (23,24), the complement inhibitors FH and FH-related protein 1 (25,26), and the thrombin-activatable fibrinolysis inhibitor (27). While Scl-1 proteins of different GAS serotypes bind a variety of host proteins, the results suggest a common role for Scl-1 in perturbing the functions of the innate immune system.…”

mentioning

confidence: 99%

Role for Streptococcal Collagen-Like Protein 1 in M1T1 Group A Streptococcus Resistance to Neutrophil Extracellular Traps

et al. 2014

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c Streptococcal collagen-like protein 1 (Scl-1) is one of the most highly expressed proteins in the invasive M1T1 serotype group A Streptococcus (GAS), a globally disseminated clone associated with higher risk of severe invasive infections. Previous studies using recombinant Scl-1 protein suggested a role in cell attachment and binding and inhibition of serum proteins. Here, we studied the contribution of Scl-1 to the virulence of the M1T1 clone in the physiological context of the live bacterium by generating an isogenic strain lacking the scl-1 gene. Upon subcutaneous infection in mice, wild-type bacteria induced larger lesions than the ⌬scl mutant. However, loss of Scl-1 did not alter bacterial adherence to or invasion of skin keratinocytes. We found instead that Scl-1 plays a critical role in GAS resistance to human and murine phagocytic cells, allowing the bacteria to persist at the site of infection. Phenotypic analyses demonstrated that Scl-1 mediates bacterial survival in neutrophil extracellular traps (NETs) and protects GAS from antimicrobial peptides found within the NETs. Additionally, Scl-1 interferes with myeloperoxidase (MPO) release, a prerequisite for NET production, thereby suppressing NET formation. We conclude that Scl-1 is a virulence determinant in the M1T1 GAS clone, allowing GAS to subvert innate immune functions that are critical in clearing bacterial infections.

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“…It has been demonstrated that Scl1 can bind selected human extracellular matrix components [109], cellular integrin receptors [107,118,119], and plasma components [120-122]. Importantly, human collagen receptors such as integrins α2β1 and α11β1 recognize the triple helix CL domain of Scl1, and this event results in cell signaling [107,118,119].…”

Section: Bacterial Collagen Triple Helix As a Bait For Host-pathogen mentioning

confidence: 99%

Polyproline and Triple Helix Motifs in Host-Pathogen Recognition

Berisio¹,

Vitagliano

2012

CPPS

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Secondary structure elements often mediate protein-protein interactions. Despite their low abundance in folded proteins, polyproline II (PPII) and its variant, the triple helix, are frequently involved in protein-protein interactions, likely due to their peculiar propensity to be solvent-exposed. We here review the role of PPII and triple helix in mediating host-pathogen interactions, with a particular emphasis to the structural aspects of these processes. After a brief description of the basic structural features of these elements, examples of host-pathogen interactions involving these motifs are illustrated. Literature data suggest that the role played by PPII motif in these processes is twofold. Indeed, PPII regions may directly mediate interactions between proteins of the host and the pathogen. Alternatively, PPII may act as structural spacers needed for the correct positioning of the elements needed for adhesion and infectivity. Recent investigations have highlighted that collagen triple helix is also a common target for bacterial adhesins. Although structural data on complexes between adhesins and collagen models are rather limited, experimental and theoretical studies have unveiled some interesting clues of the recognition process. Interestingly, very recent data show that not only is the triple helix used by pathogens as a target in the host-pathogen interaction but it may also act as a bait in these processes since bacterial proteins containing triple helix regions have been shown to interact with host proteins. As both PPII and triple helix expose several main chain non-satisfied hydrogen bond acceptors and donors, both elements are highly solvated. The preservation of the solvation state of both PPII and triple helix upon protein-protein interaction is an emerging aspect that will be here thoroughly discussed.

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The Scl1 of M41-type group A Streptococcus binds the high-density lipoprotein

Cited by 13 publications

References 27 publications

Bacterial collagen-like proteins that form triple-helical structures

Bacterial collagen-like proteins that form triple-helical structures

Role for Streptococcal Collagen-Like Protein 1 in M1T1 Group A Streptococcus Resistance to Neutrophil Extracellular Traps

Polyproline and Triple Helix Motifs in Host-Pathogen Recognition

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