Evidence map›Paper›PMID 17608944›Full record

ArticleBMC microbiology2007

Regions important for the adhesin activity of Moraxella catarrhalis Hag.

Brian Bullard, Serena Lipski, Eric R Lafontaine

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. How bacteria hack the matrix and dodge the bullets of immunity.European respiratory review : an official journal of the European Respiratory Society · 2018
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Panel 5: Microbiology and immunology panel.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2013
    Review
  10. Panel 6: Vaccines.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Molecular aspects of Moraxella catarrhalis pathogenesis.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Brian BullardDepartment of Medical Microbiology and Immunology, University of Toledo Health Sciences Campus, Toledo, OH 43614, USA. brian.bullard@osumc.edu
Serena Lipski
Eric R Lafontaine
University of Toledo Medical Center · USUniversity of Georgia · US

Funding

Adherence mechanisms of Moraxella catarrhalisR01AI051477 · NIAID · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI LAFONTAINE, ERIC R · 2003 to 2007
$1.1M
Adherence mechanisms of Moraxella catarrhalisR56AI051477 · NIAID · UNIVERSITY OF GEORGIA · PI LAFONTAINE, ERIC R · 2010 to 2010
$297k
NIAID NIH HHS AI051477NIAID NIH HHS R01 AI051477NIAID NIH HHS R56 AI051477
6 · The paper itself

Abstract

backgroundThe Moraxella catarrhalis Hag protein, an Oca autotransporter adhesin, has previously been shown to be important for adherence of this respiratory tract pathogen to human middle ear and A549 lung cells.

resultsThe present study demonstrates that adherence of M. catarrhalis isogenic hag mutant strains to the human epithelial cell lines Chang (conjunctival) and NCIH292 (lung) is reduced by 50-93%. Furthermore, expressing Hag in a heterologous Escherichia coli background substantially increased the adherence of recombinant bacteria to NCIH292 cells and murine type IV collagen. Hag did not, however, increase the attachment of E. coli to Chang cells. These results indicate that Hag directly mediates adherence to NCIH292 lung cells and collagen, but is not sufficient to confer binding to conjunctival monolayers. Several in-frame deletions were engineered within the hag gene of M. catarrhalis strain O35E and the resulting proteins were tested for their ability to mediate binding to NCIH292 monolayers, middle ear cells, and type IV collagen. These experiments revealed that epithelial cell and collagen binding properties are separable, and that residues 385-705 of this ~2,000 amino acid protein are important for adherence to middle ear and NCIH292 cells. The region of O35E-Hag encompassing aa 706 to 1194 was also found to be required for adherence to collagen. In contrast, beta-roll repeats present in Hag, which are structural features conserved in several Oca adhesins and responsible for the adhesive properties of Yersinia enterocolitica YadA, are not important for Hag-mediated adherence.

conclusionHag is a major adherence factor for human cells derived from various anatomical sites relevant to pathogenesis by M. catarrhalis and its structure-function relationships differ from those of other, closely-related autotransporter proteins.

Indexed as

Adhesins, BacterialBacterial AdhesionBacterial ProteinsCell LineCollagenEscherichia coliHumansMoraxella catarrhalisMutationProtein Structure, TertiarySequence DeletionAdhesins, BacterialBacterial ProteinsCollagenHag-1 protein, Moraxella catarrhalis

Identifiers

PMID17608944
PMCPMC1931440
OpenAlexW2149824897

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.