The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41

Squeglia, Flavia; Bachert, Beth A.; Simone, Alfonso De; Łukomski, Sławomir; Berisio, Rita

doi:10.1074/jbc.m113.523597

Cited by 27 publications

(27 citation statements)

References 74 publications

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“…The tertiary structure of this domain from strain scl2.3 has been reported 30 and the present strain scl2.28 has a very similar sequence and the same sequence length to that for scl2.3. 30 The structure shows that one Tyr, at position 52 in scl2.3, is buried in an internal a-helical, three-coil bundle and would not be accessible for crosslink formation. The other Tyr, at position 45, is located at the junction of a partially unstructured turn and link sequence and the second outer a-helical coil, contributing to hydrophobic interactions, so is also unlikely to be in a conformation to enable involvement in crosslink formation.…”

Section: Discussionmentioning

confidence: 97%

“…When the V‐domain was present it is possible that there was some involvement of the two Tyr residues from this domain. The tertiary structure of this domain from strain scl2.3 has been reported and the present strain scl2.28 has a very similar sequence and the same sequence length to that for scl2.3 . The structure shows that one Tyr, at position 52 in scl2.3, is buried in an internal α‐helical, three‐coil bundle and would not be accessible for crosslink formation.…”

Section: Discussionmentioning

confidence: 99%

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Formation of multimers of bacterial collagens through introduction of specific sites for oxidative crosslinking

Stoichevska

Peng

et al. 2016

J Biomedical Materials Res

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A range of non-animal collagens has been described, derived from bacterial species, which form stable triple-helical structures without the need for secondary modification to include hydroxyproline in the sequence. The non-animal collagens studied to date are typically smaller than animal interstitial collagens, around one quarter the length and do not pack into large fibrillar aggregates like those that are formed by the major animal interstitial collagens. A consequence of this for biomedical products is that fabricated items, such as collagen sponges, are not as mechanically and dimensionally stable as those of animal collagens. In the present study, we examined the production of larger, polymeric forms of non-animal collagens through introduction of tyrosine and cysteine residues that can form selective crosslinks through oxidation. These modifications allow the formation of larger aggregates of the non-animal collagens. When Tyr residues were incorporated, gels were obtained. And with Cys soluble aggregates were formed. These materials can be formed into sponges that are more stable than those formed without these modifications. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 104A: 2369-2376, 2016.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Formation of multimers of bacterial collagens through introduction of specific sites for oxidative crosslinking

Stoichevska

Peng

et al. 2016

J Biomedical Materials Res

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“…Recently, the crystal structure of the V domain of Scl2 from M3‐type S. pyogenes was reported (Squeglia et al ., 2013; 2014). It folds into a six‐helical bundle, with three pairs of antiparallel alpha helices, each connected by a variable loop region.…”

Section: Classification Of Scl Proteinsmentioning

confidence: 99%

Collagen‐like proteins of pathogenic streptococci

Łukomski

Bachert

Squeglia

et al. 2017

Molecular Microbiology

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SummaryThe collagen domain, which is defined by the presence of the Gly-X-Y triplet repeats, is amongst the most versatile and widespread known structures found in proteins from organisms representing all three domains of life. The streptococcal collagen-like (Scl) proteins are widely present in pathogenic streptococci, including Streptococcus pyogenes, S. agalactiae, S. pneumoniae, and S. equi. Experiments and bioinformatic analyses support the hypothesis that all Scl proteins are homotrimeric and cell wallanchored. These proteins contain the rod-shaped collagenous domain proximal to cell surface, as well as a variety of outermost non-collagenous domains that generally lack predicted functions but can be grouped into one of six clusters based on sequence similarity. The well-characterized Scl1 proteins of S. pyogenes show a dichotomous switch in ligand binding between human tissue and blood environments. In tissue, Scl1 adhesin specifically recognizes the wound microenvironment, promotes adhesion and biofilm formation, decreases bacterial killing by neutrophil extracellular traps, and modulates S. pyogenes virulence. In blood, ligands include components of complement and coagulationfibrinolytic systems, as well as plasma lipoproteins. In all, the Scl proteins signify a large family of structurally related surface proteins, which contribute to the ability of streptococci to colonize and cause diseases in humans and animals.

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“…In S. pyogenes , the N-terminal globular domains (V domains) of the Scl1 and Scl2 proteins are of variable lengths and amino acid sequences in different strains, although all V domains share a high content of α-helical secondary structure (Han et al 2006b; Yu et al 2010). Recently, the crystal structure of Scl2.3 globular domain has been reported as a compact trimeric six-helix bundle (Squeglia et al 2014) which is unique among any known trimerization domains of collagen. The V domains of S. pyogenes have been shown to promote the refolding of the triple-helix domain.…”

Section: Characterization and Manipulation Of Trimerization Domainmentioning

confidence: 99%

Bacterial collagen-like proteins that form triple-helical structures

Ramshaw

et al. 2014

Journal of Structural Biology

121

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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The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41

Cited by 27 publications

References 74 publications

Formation of multimers of bacterial collagens through introduction of specific sites for oxidative crosslinking

Formation of multimers of bacterial collagens through introduction of specific sites for oxidative crosslinking

Collagen‐like proteins of pathogenic streptococci

Bacterial collagen-like proteins that form triple-helical structures

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