Evidence map›Paper›PMID 10816485›Full record

ArticleInfection and immunity2000

Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and beta1,4-glucosyltransferase: identification of LOS glycoforms containing lactosamine repeats.

M J Filiatrault, B W Gibson, B Schilling, S Sun, R S Munson, A A Campagnari

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.6field-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

24 citing papers in PubMed, 56 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

6 authors at 4 institutions in 2 countries.

M J FiliatraultDepartment of Microbiology, University at Buffalo, Buffalo, New York 14214, USA.
B W Gibson
B Schilling
S Sun
R S Munson
A A Campagnari
Children’s Institute · USUniversity of California, San Francisco · USCzech Academy of Sciences, Institute of Microbiology · CZUniversity at Buffalo, State University of New York · US

Funding

Structure and Function of Haemophilus ducreyi LOSR01AI031254 · NIAID · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI GIBSON, BRADFORD WAYNE · 1994 to 2007
$2.0M
GENETICS AND BIOLOGY OF THE LOS HAEMOPHILUS DUCREYIR01AI038444 · NIAID · RESEARCH INST NATIONWIDE CHILDREN'S HOSP · PI MUNSON, ROBERT S. · 1997 to 2001
$486k
STRUCTURE OF H DUCREYI LOS--ROLE IN ADHERENCE/INVASIONR01AI030006 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI CAMPAGNARI, ANTHONY A · 1991 to 2000
$174k
NIAID NIH HHS R01 AI031254NIAID NIH HHS R01 AI30006NIAID NIH HHS R01 AI31254NIAID NIH HHS R01 AI38444
6 · The paper itself

Abstract

To begin to understand the role of the lipooligosaccharide (LOS) molecule in chancroid infections, we constructed mutants defective in expression of glycosyltransferase genes. Pyocin lysis and immunoscreening was used to identify a LOS mutant of Haemophilus ducreyi 35000. This mutant, HD35000R, produced a LOS molecule that lacked the monoclonal antibody 3F11 epitope and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Structural studies indicated that the principal LOS glycoform contains lipid A, Kdo, and two of the three core heptose residues. HD35000R was transformed with a plasmid library of H. ducreyi 35000 DNA, and a clone producing the wild-type LOS was identified. Sequence analysis of the plasmid insert revealed one open reading frame (ORF) that encodes a protein with homology to the WaaQ (heptosyltransferase III) of Escherichia coli. A second ORF had homology to the LgtF (glucosyltransferase) of Neisseria meningitidis. Individual isogenic mutants lacking expression of the putative H. ducreyi heptosyltransferase III, the putative glucosyltransferase, and both glycosyltransferases were constructed and characterized. Each mutant was complemented with the representative wild-type genes in trans to restore expression of parental LOS and confirm the function of each enzyme. Matrix-assisted laser desorption ionization mass spectrometry and SDS-PAGE analysis identified several unique LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region of the main LOS branch synthesized by the heptosyltransferase III mutant. These novel H. ducreyi mutants provide important tools for studying the regulation of LOS assembly and biosynthesis.

Indexed as

Bacterial ProteinsEscherichia coli ProteinsAmino SugarsCarbohydrate SequenceChancroidGenetic Complementation TestGlucosyltransferasesGlycosyltransferasesHaemophilus ducreyiHumansLipopolysaccharidesMolecular Sequence DataMutationPyocinsSelection, GeneticSequence AnalysisAmino SugarsBacterial ProteinsEscherichia coli ProteinsGlucosyltransferasesGlycosyltransferaseslactosaminelgtF protein, Neisseria meningitidislipid-linked oligosaccharidesLipopolysaccharidesPyocinsWaaQ protein, E coli

Identifiers

PMID10816485
PMCPMC97600
OpenAlexW2129556455

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Registered trials

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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.