ArticleJournal of bacteriology2006
The streptococcal Blr and Slr proteins define a family of surface proteins with leucine-rich repeats: camouflaging by other surface structures.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- The Slr protein of Streptococcus pyogenes is selectively expressed in vivo and is a target for protective antibodies.EMBO molecular medicine · 2026Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Inactivation of theVirulence · 2020Article
- An original infection model identifies host lipoprotein import as a route for blood-brain barrier crossing.Nature communications · 2020Article
- Article
- The type II histidine triad protein HtpsC is a novel adhesion with the involvement of Streptococcus suis virulence.Virulence · 2015Article
- Role of Pht proteins in attachment of Streptococcus pneumoniae to respiratory epithelial cells.Infection and immunity · 2014Article
- Insight into the evolution of the histidine triad protein (HTP) family in Streptococcus.PloS one · 2013Article
- New insights into histidine triad proteins: solution structure of a Streptococcus pneumoniae PhtD domain and zinc transfer to AdcAII.PloS one · 2013Article
- Virulence gene pool detected in bovine group C Streptococcus dysgalactiae subsp. dysgalactiae isolates by use of a group A S. pyogenes virulence microarray.Journal of clinical microbiology · 2011Article
- Article
- The C-terminal tail of Yersinia pseudotuberculosis YopM is critical for interacting with RSK1 and for virulence.Infection and immunity · 2010Article
- Functional dissection of Streptococcus pyogenes M5 protein: the hypervariable region is essential for virulence.PloS one · 2009Article
- Streptococcus pneumoniae surface protein PcpA elicits protection against lung infection and fatal sepsis.Infection and immunity · 2008Article
- Enterococcal leucine-rich repeat-containing protein involved in virulence and host inflammatory response.Infection and immunity · 2007Article
- Listeria monocytogenes surface proteins: from genome predictions to function.Microbiology and molecular biology reviews : MMBR · 2007Review
- C-terminal WxL domain mediates cell wall binding in Enterococcus faecalis and other gram-positive bacteria.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regions with tandemly arranged leucine-rich repeats (LRRs) have been found in many prokaryotic and eukaryotic proteins, in which they provide a remarkably versatile framework for the formation of ligand-binding sites. Bacterial LRR proteins include the recently described Slr protein of Streptococcus pyogenes, which is related to internalin A of Listeria monocytogenes. Here, we show that strains of the human pathogen Streptococcus agalactiae express a protein, designated Blr, which together with Slr defines a family of internalin A-related streptococcal LRR proteins. Analysis with specific antibodies demonstrated that Blr is largely inaccessible on S. agalactiae grown in vitro, but surface exposure was increased approximately 100-fold on mutants lacking polysaccharide capsule. In S. pyogenes, surface exposure of Slr was not affected in a mutant lacking hyaluronic acid capsule but was increased >20-fold in mutants lacking M protein or protein F. Thus, both Blr and Slr are efficiently camouflaged by other surface structures on bacteria grown in vitro. When Blr and Slr exposed on the bacterial surface were compared, they exhibited only little immunological cross-reactivity, in spite of extensive residue identity, suggesting that their surface-exposed parts have been under evolutionary pressure to diverge functionally and/or antigenically. These data identify a family of immunologically diverse streptococcal LRR proteins that show unexpected complexity in their interactions with other bacterial surface components.
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