ArticlePloS one2013
SecA localization and SecA-dependent secretion occurs at new division septa in group B Streptococcus.
Article in PloS one, 2013. 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, 23 citations in OpenAlex.
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Article
- Signal peptidase SpsB coordinates staphylococcal cell cycle, surface protein septal trafficking and LTA synthesis.bioRxiv : the preprint server for biology · 2024Article
- Spatial and temporal localization of cell wall associated pili in Enterococcus faecalis.Molecular microbiology · 2023Article
- The Role of Streptococcal Cell-Envelope Proteases in Bacterial Evasion of the Innate Immune System.Journal of innate immunity · 2022Review
- Spatial regulation of protein A in Staphylococcus aureus.Molecular microbiology · 2021Article
- Cellular dynamics of the SecA ATPase at the single molecule level.Scientific reports · 2021Article
- YSIRK-G/S-directed translocation is required forVirulence · 2020Article
- Class A PBPs have a distinct and unique role in the construction of the pneumococcal cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Interactions Screenings Unearth Potential New Divisome Components in theMicroorganisms · 2019Article
- Septal secretion of protein A ineLife · 2018Article
- Review
- Evaluation of small molecule SecA inhibitors against methicillin-resistant Staphylococcus aureus.Bioorganic & medicinal chemistry · 2015Article
- Article
- FbsC, a novel fibrinogen-binding protein, promotes Streptococcus agalactiae-host cell interactions.The Journal of biological chemistry · 2014Article
- Focal targeting by human β-defensin 2 disrupts localized virulence factor assembly sites in Enterococcus faecalis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exported proteins of Streptococcus agalactiae (GBS), which include proteins localized to the bacterial surface or secreted into the extracellular environment, are key players for commensal and pathogenic interactions in the mammalian host. These proteins are transported across the cytoplasmic membrane via the general SecA secretory pathway and those containing the so-called LPXTG sorting motif are covalently attached to the peptidoglycan by sortase A. How SecA, sortase A, and LPXTG proteins are spatially distributed in GBS is not known. In the close relative Streptococcus pyogenes, it was shown that presence of the YSIRKG/S motif (literally YSIRKX3Gx2S) in the signal peptide (SP) constitutes the targeting information for secretion at the septum. Here, using conventional and deconvolution immunofluorescence analyses, we have studied in GBS strain NEM316 the localization of SecA, SrtA, and the secreted protein Bsp whose signal peptide contains a canonical YSIRKG/S motif (YSLRKykfGlaS). Replacing the SP of Bsp with four other SPs containing or not the YSIRKG/S motif did not alter the localized secretion of Bsp at the equatorial ring. Our results indicate that secretion and cell wall-anchoring machineries are localized at the division septum. Cell wall- anchored proteins displayed polar (PilB, Gbs0791), punctuate (CspA) or uniform distribution (Alp2) on the bacterial surface. De novo secretion of Gbs0791 following trypsin treatment indicates that it is secreted at the septum, then redistributed along the lateral sides, and finally accumulated to the poles. We conclude that the ±YSIRK SP rule driving compartimentalized secretion is not true in S. agalactiae.
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