ArticleJournal of bacteriology2013
System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Structural and biophysical characterization of the secreted, β-helical adhesin EtpA of Enterotoxigenic Escherichia coli.PloS one · 2023Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- Article
- The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases.BioMed research international · 2018Review
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Cloning, Expression, and Immunogenicity of Fimbrial-F17A Subunit Vaccine againstBioMed research international · 2017Article
- Meningococcal Two-Partner Secretion Systems and Their Association with Outcome in Patients with Meningitis.Infection and immunity · 2016Article
- Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation.Protein science : a publication of the Protein Society · 2015Article
- Whole-genome comparative analysis of virulence genes unveils similarities and differences between endophytes and other symbiotic bacteria.Frontiers in microbiology · 2015Article
- A new family of secreted toxins in pathogenic Neisseria species.PLoS pathogens · 2015Article
- The polypeptide transport-associated (POTRA) domains of TpsB transporters determine the system specificity of two-partner secretion systems.The Journal of biological chemistry · 2014Article
- The biology of Neisseria adhesins.Biology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The two-partner secretion (TPS) systems of Gram-negative bacteria consist of a large secreted exoprotein (TpsA) and a transporter protein (TpsB) located in the outer membrane. TpsA targets TpsB for transport across the membrane via its ∼30-kDa TPS domain located at its N terminus, and this domain is also the minimal secretory unit. Neisseria meningitidis genomes encode up to five TpsAs and two TpsBs. Sequence alignments of TPS domains suggested that these are organized into three systems, while there are two TpsBs, which raised questions on their system specificity. We show here that the TpsB2 transporter of Neisseria meningitidis is able to secrete all types of TPS domains encoded in N. meningitidis and the related species Neisseria lactamica but not domains of Haemophilus influenzae and Pseudomonas aeruginosa. In contrast, the TpsB1 transporter seemed to be specific for its cognate N. meningitidis system and did not secrete the TPS domains of other meningococcal systems. However, TpsB1 did secrete the TPS2b domain of N. lactamica, which is related to the meningococcal TPS2 domains. Apparently, the secretion depends on specific sequences within the TPS domain rather than the overall TPS domain structure.
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