Evidence map›Paper›PMID 15838019›Full record

ArticleJournal of bacteriology2005

Characterization of a cluster of three glycosyltransferase enzymes essential for Moraxella catarrhalis lipooligosaccharide assembly.

Katie J Edwards, Simon Allen, Bradford W Gibson, Anthony A Campagnari

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. A global perspective on the genomics ofMicrobial genomics · 2025
    Article
  2. Panel 4: Report of the Microbiology Panel.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2017
    Review
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  16. Two Glycosyltransferase Genes ofFrontiers in cellular and infection microbiology
    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

4 authors at 3 institutions in 1 country.

Katie J EdwardsDepartment of Microbiology, State University of New York at Buffalo, NY 14214, USA.
Simon Allen
Bradford W Gibson
Anthony A Campagnari
Buck Institute for Research on Aging · USUniversity at Buffalo, State University of New York · USUniversity of California, San Francisco · US

Funding

Genetics /Biology of M. catarrhalis LOS in Otitis MediaR01DC005837 · NIDCD · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI CAMPAGNARI, ANTHONY A · 2002 to 2013
$3.6M
Recurrent otitis media and COPD: immunity and vaccinesP01AI046422 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI MURPHY, TIMOTHY F · 2001 to 2004
$2.4M
TRAINING IN MICROBIAL PATHOGENESIST32AI007614 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI READ, LAURIE K. · 1999 to 2015
$2.1M
Structure and Function of Haemophilus ducreyi LOSR01AI031254 · NIAID · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI GIBSON, BRADFORD WAYNE · 1994 to 2007
$2.0M
NIAID NIH HHS AI07614NIAID NIH HHS AI31254NIAID NIH HHS AI46422NIAID NIH HHS P01 AI046422NIAID NIH HHS R01 AI031254NIAID NIH HHS T32 AI007614NIDCD NIH HHS DC005837NIDCD NIH HHS R01 DC005837
6 · The paper itself

Abstract

Moraxella catarrhalis isolates express lipooligosaccharide (LOS) molecules on their surface, which share epitopes similar to that of the Neisseria and Haemophilus species. These common LOS epitopes have been implicated in various steps of pathogenesis for the different organisms. In this study, a cluster of three LOS glycosyltransferase genes (lgt) were identified in M. catarrhalis 7169, a strain that produces a serotype B LOS. Mutants in these glycosyltransferase genes were constructed, and the resulting LOS phenotypes were consistent with varying degrees of truncation compared to wild-type LOS. The LOS structures of each lgt mutant were no longer detected by a monoclonal antibody (MAb 4G5) specific to a highly conserved terminal epitope nor by a monoclonal antibody (MAb 3F7) specific to the serotype B LOS side chain. Mass spectrometry of the LOS glycoforms assembled by two of these lgt mutants indicated that lgt1 encodes an alpha(1-2) glucosyltransferase and the lgt2 encodes a beta(1-4) galactosyltransferase. However, these structural studies could not delineate the function for lgt3. Therefore, M. catarrhalis lgt3 was introduced into a defined beta(1-4) glucosyltransferase Haemophilus ducreyi 35000glu- mutant in trans, and monoclonal antibody analysis confirmed that Lgt3 complemented the LOS defect. These data suggest that lgt3 encodes a glucosyltransferase involved in the addition of a beta(1-4)-linked glucose to the inner core. Furthermore, we conclude that this enzymatic step is essential for the assembly of the complete LOS glycoform expressed by M. catarrhalis 7169.

Indexed as

Multigene FamilyAntibodies, BacterialAntibodies, MonoclonalCarbohydrate SequenceCloning, MolecularDNA, BacterialEpitopesGalactosyltransferasesGenes, BacterialGenetic Complementation TestGlucosyltransferasesGlycosyltransferasesHaemophilus ducreyiLipopolysaccharidesMass SpectrometryMolecular Sequence DataAntibodies, BacterialAntibodies, MonoclonalDNA, BacterialEpitopesGalactosyltransferasesGlucosyltransferasesGlycosyltransferaseslipid-linked oligosaccharidesLipopolysaccharides

Identifiers

PMID15838019
PMCPMC1082826
OpenAlexW2161337257

What OpenQuestion holds

Textmetadata
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.