MétaCan
← all works

Aeromonas hydrophila Flagella Glycosylation: Involvement of a Lipid Carrier

2014· article· en· 13 citations· W1977248433 on OpenAlex· 10.1371/journal.pone.0089630

Why is this work in the frame?

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

Canadian affiliationAn author listed a Canadian institution. This is the only route the usual frame has.
Canadian funderA Canadian agency funded it. The work may carry no Canadian affiliation at all.

Post-publication record

Nature
Retraction
Reason
Concerns/Issues about Image;Duplication of/in Image;Euphemisms for Duplication;Investigation by Journal/Publisher;Original Data and/or Images not Provided and/or not Available;Unreliable Results and/or Conclusions;
Date
5/9/2025 0:00
Flagged by OpenAlex?
Yes

Source: Retraction Watch, joined by DOI. OpenAlex records retraction as is_retracted, a boolean over a state space with at least four values, so it cannot express an expression of concern, a correction or a reinstatement — it reports them as false, which reads as “fine”.

Abstract

Polar flagellin proteins from Aeromonas hydrophila strain AH-3 (serotype O34) were found to be O-glycosylated with a heterogeneous glycan. Mutants unable to produce WecP or Gne enzymes showed altered motility, and the study of their polar flagellin glycosylation showed that the patterns of glycosylation differed from that observed with wild type polar flagellin. This suggested the involvement of a lipid carrier in glycosylation. A gene coding for an enzyme linking sugar to a lipid carrier was identified in strain AH-3 (WecX) and subsequent mutation abolished completely motility, flagella production by EM, and flagellin glycosylation. This is the first report of a lipid carrier involved in flagella O-glycosylation. A molecular model has been proposed. The results obtained suggested that the N-acetylhexosamines are N-acetylgalactosamines and that the heptasaccharide is completely independent of the O34-antigen lipopolysaccharide. Furthermore, by comparing the mutants with differing degrees of polar flagellin glycosylation, we established their importance in A. hydrophila flagella formation and motility.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

The record

Venue
PLoS ONE
Topic
Bacteriophages and microbial interactions
Field
Environmental Science
Canadian institutions
National Research Council Canada
Funders
National Research Council CanadaUniversitat de BarcelonaGeneralitat de Catalunya
Keywords
FlagellinGlycosylationFlagellumGlycanMutantAeromonas hydrophilaBiochemistryBiologyChemistryMicrobiologyGeneGlycoproteinGeneticsBacteria
Has abstract in OpenAlex
yes