Evidence map›Paper›PMID 19168738›Full record

ArticleInfection and immunity2009

Identification of novel glycosyltransferases required for assembly of the Pasteurella multocida A:1 lipopolysaccharide and their involvement in virulence.

John D Boyce, Marina Harper, Frank St Michael, Marietta John, Annie Aubry, Henrietta Parnas, Susan M Logan, Ian W Wilkie, Mark Ford, Andrew D Cox and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 46 citations in OpenAlex.

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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

11 authors at 5 institutions in 2 countries.

John D BoyceAustralian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, VIC 3800, Australia.
Marina Harper
Frank St Michael
Marietta John
Annie Aubry
Henrietta Parnas
Susan M Logan
Ian W Wilkie
Mark Ford
Andrew D Cox
Ben Adler
Institute for Biological Sciences · CAMonash University · AUAustralian Research Council · AUCommonwealth Scientific and Industrial Research Organisation · AUUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously determined the structure of the Pasteurella multocida Heddleston type 1 lipopolysaccharide (LPS) molecule and characterized some of the transferases essential for LPS biosynthesis. We also showed that P. multocida strains expressing truncated LPS display reduced virulence. Here, we have identified all of the remaining glycosyltransferases required for synthesis of the oligosaccharide extension of the P. multocida Heddleston type 1 LPS, including a novel alpha-1,6 glucosyltransferase, a beta-1,4 glucosyltransferase, a putative bifunctional galactosyltransferase, and two heptosyltransferases. In addition, we identified a novel oligosaccharide extension expressed only in a heptosyltransferase (hptE) mutant background. All of the analyzed mutants expressing LPS with a truncated main oligosaccharide extension displayed reduced virulence, but those expressing LPS with an intact heptose side chain were able to persist for long periods in muscle tissue. The hptC mutant, which expressed LPS with the shortest oligosaccharide extension and no heptose side chain, was unable to persist on the muscle or cause any disease. Furthermore, all of the mutants displayed increased sensitivity to the chicken antimicrobial peptide fowlicidin 1, with mutants expressing highly truncated LPS being the most sensitive.

Indexed as

GlycosyltransferasesAnimalsAntimicrobial Cationic PeptidesBacterial ProteinsChickensGalactosyltransferasesGlucosyltransferasesLipopolysaccharidesMicrobial Sensitivity TestsMutationPasteurella InfectionsPasteurella multocidaPoultry DiseasesVirulence1,3-alpha-D-glucan synthaseAntimicrobial Cationic PeptidesBacterial ProteinsGalactosyltransferasesGlucosyltransferasesGlycosyltransferasesheptosyltransferaseLipopolysaccharides

Identifiers

PMID19168738
PMCPMC2663145
OpenAlexW2159878588

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.