ArticleThe Journal of biological chemistry2014
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.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Phylogenomic analysis of the collagen-like BclA proteins inApplied and environmental microbiology · 2026Article
- A conserved strategy to attack collagen: The activator domain in bacterial collagenases unwinds triple-helical collagen.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Article
- Role for Cell-Surface Collagen ofACS infectious diseases · 2020Article
- Expression and Purification of Collagen-Like Proteins of Group A Streptococcus.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Adaptation of the group A Streptococcus adhesin Scl1 to bind fibronectin type III repeats within wound-associated extracellular matrix: implications for cancer therapy.Molecular microbiology · 2019Article
- Surface-exposed loops and an acidic patch in the Scl1 protein of group AThe Journal of biological chemistry · 2018Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Collagen-like proteins of pathogenic streptococci.Molecular microbiology · 2017Review
- Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.The Journal of biological chemistry · 2016Article
- Hydroxyproline-containing collagen peptide derived from the skin of the Alaska pollack inhibits HIV-1 infection.Molecular medicine reports · 2016Article
- Unique Footprint in the scl1.3 Locus Affects Adhesion and Biofilm Formation of the Invasive M3-Type Group A Streptococcus.Frontiers in cellular and infection microbiology · 2016Article
- Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4.Viruses · 2015Article
- Bacterial collagen-like proteins that form triple-helical structures.Journal of structural biology · 2014Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
The arsenal of virulence factors deployed by streptococci includes streptococcal collagen-like (Scl) proteins. These proteins, which are characterized by a globular domain and a collagen-like domain, play key roles in host adhesion, host immune defense evasion, and biofilm formation. In this work, we demonstrate that the Scl2.3 protein is expressed on the surface of invasive M3-type strain MGAS315 of Streptococcus pyogenes. We report the crystal structure of Scl2.3 globular domain, the first of any Scl. This structure shows a novel fold among collagen trimerization domains of either bacterial or human origin. Despite there being low sequence identity, we observed that Scl2.3 globular domain structurally resembles the gp41 subunit of the envelope glycoprotein from human immunodeficiency virus type 1, an essential subunit for viral fusion to human T cells. We combined crystallographic data with modeling and molecular dynamics techniques to gather information on the entire lollipop-like Scl2.3 structure. Molecular dynamics data evidence a high flexibility of Scl2.3 with remarkable interdomain motions that are likely instrumental to the protein biological function in mediating adhesive or immune-modulatory functions in host-pathogen interactions. Altogether, our results provide molecular tools for the understanding of Scl-mediated streptococcal pathogenesis and important structural insights for the future design of small molecular inhibitors of streptococcal invasion.
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