Evidence map›Paper›PMID 12540541›Full record

ArticleInfection and immunity2003

The msbB mutant of Neisseria meningitidis strain NMB has a defect in lipooligosaccharide assembly and transport to the outer membrane.

Deborah M B Post, Margaret R Ketterer, Nancy J Phillips, Bradford W Gibson, Michael A Apicella

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Characterization and Genomic Analysis ofAnimals : an open access journal from MDPI · 2025
    Article
  2. Role ofMicroorganisms · 2025
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  3. Lipid a is more than acyl chains.Infection and immunity · 2014
    Article
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  8. Gonococcal cervicitis: a role for biofilm in pathogenesis.The Journal of infectious diseases · 2008
    Article
  9. Article
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  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Deborah M B PostDepartment of Microbiology, University of Iowa, Iowa City 52242, USA.
Margaret R Ketterer
Nancy J Phillips
Bradford W Gibson
Michael A Apicella
University of Iowa · USUniversity of California, San Francisco · US

Funding

Studies of the capsular-like antigen of F. tularensisP01AI044642 · NIAID · UNIVERSITY OF IOWA · PI APICELLA, MICHAEL A. · 1999 to 2014
$18.2M
THE BIOLOGY OF PATHOGENIC NEISSERIAR01AI045728 · NIAID · UNIVERSITY OF IOWA · PI APICELLA, MICHAEL A. · 1999 to 2010
$3.7M
NIAID NIH HHS AI44642NIAID NIH HHS AI45728NIAID NIH HHS P01 AI044642NIAID NIH HHS R01 AI045728PHS HHS 06164PHS HHS T32A107511
6 · The paper itself

Abstract

A deletion-insertion mutation in msbB, a gene that encodes a lipid A acyltransferase, was introduced into encapsulated Neisseria meningitidis serogroup B strain NMB and an acapsular mutant of the same strain. These mutants were designated NMBA11K3 and NMBA11K3cap-, respectively. Neither lipooligosaccharide (LOS) nor lipid A could be isolated from NMBA11K3 although a number of techniques were tried, but both were easily extracted from NMBA11K3cap-. Immunoelectron microscopy using monoclonal antibody (MAb) 6B4, which recognizes the terminal Galbeta1-4GlcNAc of LOS, demonstrated that NMB, NMBcap-, and NMBA11K3cap- expressed LOS circumferentially, while MAb 6B4 did not bind to the surface of NMBA11K3. However, cytoplasmic staining of NMBA11K3 with MAb 6B4 was a consistent observation. Mass-spectrometric analyses demonstrated that the relative amounts of the lipid A-specific C12:0 3-OH and C14:0 3-OH present in the membrane preparations (MP) from NMBA11K3 were substantially decreased (25- and 23-fold, respectively) compared to the amount in MP from its parent strain, NMB. Western blot analyses of MP from NMBA11K3 demonstrated that the levels of porin in the outer membrane of NMBA11K3 were also substantially decreased. These studies suggest that the lipid A acylation defect in encapsulated NMBA11K3 influences the assembly of the lipid A and consequently the incorporation of porin in the outer membrane.

Indexed as

AcyltransferasesMutationBacterial ProteinsBlotting, WesternCell MembraneCloning, MolecularFatty AcidsGene DeletionLipid ALipopolysaccharidesMass SpectrometryMicroscopy, ElectronMicroscopy, Electron, ScanningMicroscopy, ImmunoelectronNeisseria meningitidisPolymerase Chain ReactionAcyltransferasesBacterial ProteinsFatty AcidsLipid Alipid-linked oligosaccharidesLipopolysaccharides

Identifiers

PMID12540541
PMCPMC145375
OpenAlexW2145704725

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.