ArticleFEMS microbiology letters2010
The Scl1 of M41-type group A Streptococcus binds the high-density lipoprotein.
Article in FEMS microbiology letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Surface-exposed loops and an acidic patch in the Scl1 protein of group AThe Journal of biological chemistry · 2018Article
- Collagen-like proteins of pathogenic streptococci.Molecular microbiology · 2017Review
- LDL acts as an opsonin enhancing the phagocytosis of group A Streptococcus by monocyte and whole human blood.Medical microbiology and immunology · 2016Article
- Role for streptococcal collagen-like protein 1 in M1T1 group A Streptococcus resistance to neutrophil extracellular traps.Infection and immunity · 2014Article
- Bacterial collagen-like proteins that form triple-helical structures.Journal of structural biology · 2014Article
- 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.The Journal of biological chemistry · 2014Article
- Crystallization and preliminary X-ray crystallographic analysis of the variable domain of Scl2.3, a streptococcal collagen-like protein from invasive M3-type Streptococcus pyogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- The group A streptococcal collagen-like protein-1, Scl1, mediates biofilm formation by targeting the extra domain A-containing variant of cellular fibronectin expressed in wounded tissue.Molecular microbiology · 2013Article
- Polyproline and triple helix motifs in host-pathogen recognition.Current protein & peptide science · 2012Review
- The streptococcal collagen-like protein-1 (Scl1) is a significant determinant for biofilm formation by group A Streptococcus.BMC microbiology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Streptococcal collagen-like protein 1 (Scl1) is a virulence factor on the surface of group A Streptococcus (GAS). We have reported previously that several Scl1 proteins derived from various M-type GAS strains, including M41, can bind to low-density lipoprotein, but the Scl1 protein derived from the M6-type GAS strain cannot. Here, we demonstrated that recombinant protein, designated C176, derived from Scl1.41 of the GAS M41-type strain also binds both plasma and purified high-density lipoprotein (HDL). Next, we determined that the intact noncollagenous region of C176 was necessary and sufficient for HDL binding. C176-HDL interaction could be eliminated by the presence of low concentrations of the nonionic detergent, Tween 20, indicating the hydrophobic nature of this interaction. We finally showed that whole GAS cells expressing native Scl1.41 protein absorbed HDL from human plasma in the absence of Tween 20, but M6-type GAS cells did not. Altogether, our results add further evidence to the importance of GAS-lipoprotein binding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.