ArticleInfection and immunity2007
Identification of a novel two-partner secretion locus in Moraxella catarrhalis.
Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Otitis media: recent advances in otitis media vaccine development and model systems.Frontiers in microbiology · 2024Review
- The characterization ofMicrobial genomics · 2022Article
- 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
- Review
- Article
- Identification of a Contact-Dependent Growth Inhibition (CDI) System That Reduces Biofilm Formation and Host Cell Adhesion ofFrontiers in microbiology · 2019Article
- A Moraxella catarrhalis vaccine to protect against otitis media and exacerbations of COPD: An update on current progress and challenges.Human vaccines & immunotherapeutics · 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
- Comparative Genomic Analyses of the Moraxella catarrhalis Serosensitive and Seroresistant Lineages Demonstrate Their Independent Evolution.Genome biology and evolution · 2016Article
- Vaccine targets against Moraxella catarrhalis.Expert opinion on therapeutic targets · 2016Review
- A Moraxella catarrhalis two-component signal transduction system necessary for growth in liquid media affects production of two lysozyme inhibitors.Infection and immunity · 2015Article
- Identification of an outer membrane lipoprotein involved in nasopharyngeal colonization by Moraxella catarrhalis in an animal model.Infection and immunity · 2014Article
- Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2.BMC microbiology · 2013Article
- Panel 5: Microbiology and immunology panel.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2013Review
- Panel 6: Vaccines.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2013Review
- Article
- Use of the chinchilla model for nasopharyngeal colonization to study gene expression by Moraxella catarrhalis.Infection and immunity · 2012Article
- The Acinetobacter baumannii biofilm-associated protein plays a role in adherence to human epithelial cells.Infection and immunity · 2012Article
- The Moraxella catarrhalis nitric oxide reductase is essential for nitric oxide detoxification.Journal of bacteriology · 2011Article
- Comparative analysis and supragenome modeling of twelve Moraxella catarrhalis clinical isolates.BMC genomics · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Although Moraxella catarrhalis continues to be a significant cause of disease in both children and adults, the steps involved in pathogenesis remain poorly understood. We have identified three open reading frames in the M. catarrhalis genome that encode homologues of the two-partner secretion system (TPS). The sequenced M. catarrhalis hemagglutinin-like locus of strain 7169 has a unique gene organization composed in the order of mchA1, mchB, and mchA2, where mchA1 is divergent. MchA1 and MchA2 are 74% identical at the amino acid level and diverge only in the C-terminal regions. The TPS motif identified in the common N-terminal regions of MchA1 and MchA2 was found to be homologous to the filamentous hemagglutinin of Bordetella pertussis, and MchB has homology to other TpsB transporters. The presence of MchA1 and MchA2 in outer membrane protein preparations and concentrated culture supernatants (CCSs) of strain 7169 was confirmed by immunoblotting using specific antisera. Nanoscale liquid chromatography-tandem mass spectrometry peptide sequencing of the antibody-reactive bands from the CCSs was performed and demonstrated that 13 different peptides mapped to identical regions of MchA1 and MchA2. Quantitative adherence assays revealed a decrease of binding to primary normal human bronchial epithelial cells by the mch mutants 7169mchB and 7169mchA1A2B compared to that by the wild-type strain. These studies show that MchA1, MchA2, and MchB are components of a novel TPS identified in M. catarrhalis and suggest that these proteins may be involved in colonization.
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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.