ArticleJournal of bacteriology2007
A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 60 citations in OpenAlex.
- Review
- Article
- HrpA anchors meningococci to the dynein motor and affects the balance between apoptosis and pyroptosis.Journal of biomedical science · 2022Article
- Review
- The Host-Pathogen Interactions and Epicellular Lifestyle ofFrontiers in cellular and infection microbiology · 2022Review
- Immunization with HMW1 and HMW2 adhesins protects against colonization by heterologous strains of nontypeableProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Contact-Dependent Growth Inhibition in Bacteria: Do Not Get Too Close!International journal of molecular sciences · 2020Review
- Single Domain Antibodies Targeting Receptor Binding Pockets of NadA Restrain Adhesion ofFrontiers in molecular biosciences · 2020Article
- Molecular interactions between Neisseria meningitidis and its human host.Cellular microbiology · 2019Review
- Identification of a Contact-Dependent Growth Inhibition (CDI) System That Reduces Biofilm Formation and Host Cell Adhesion ofFrontiers in microbiology · 2019Article
- Type V Secretion Systems: An Overview of Passenger Domain Functions.Frontiers in microbiology · 2019Review
- The influence of two-partner secretion systems on the virulence of Acinetobacter baumannii.Virulence · 2017Article
- Transcriptomic buffering of cryptic genetic variation contributes to meningococcal virulence.BMC genomics · 2017Article
- Can't you hear me knocking: contact-dependent competition and cooperation in bacteria.Emerging topics in life sciences · 2017Article
- Comparative Genome Sequencing Reveals Within-Host Genetic Changes in Neisseria meningitidis during Invasive Disease.PloS one · 2017Article
- 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
- Meningococcal Two-Partner Secretion Systems and Their Association with Outcome in Patients with Meningitis.Infection and immunity · 2016Article
- Fitness Cost of Rifampin Resistance in Neisseria meningitidis: In Vitro Study of Mechanisms Associated with rpoB H553Y Mutation.Antimicrobial agents and chemotherapy · 2015Article
- CdiA promotes receptor-independent intercellular adhesion.Molecular microbiology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neisseria meningitidis is a frequent commensal of the human nasopharynx causing severe invasive infections in rare cases. A functional two-partner secretion (TPS) system in N. meningitidis, composed of the secreted effector protein HrpA and its cognate transporter HrpB, is identified and characterized in this study. Although all meningococcal strains harbor at least one TPS system, the hrpA genes display significant C-terminal sequence variation. Meningococcal genes encoding the TPS effector proteins and their transporters are closely associated and transcribed into a single mRNA. HrpA proteins are translocated across the meningococcal outer membrane by their cognate transporters HrpB and mainly released into the environment. During this process, HrpA is proteolytically processed to a mature 180-kDa form. In contrast to other known TPS systems, immature HrpA proteins are stable in the absence of HrpB and accumulate within the bacterial cell. A small percentage of mature HrpA remains associated with the bacteria and contributes to the interaction of meningococci with epithelial cells.
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Registered trials
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.