Evidence map›Paper›PMID 11948150›Full record

ArticleJournal of bacteriology2002

Endotoxin of Neisseria meningitidis composed only of intact lipid A: inactivation of the meningococcal 3-deoxy-D-manno-octulosonic acid transferase.

Yih-Ling Tzeng, Anup Datta, V Kumar Kolli, Russell W Carlson, David S Stephens

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

30 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Interplays of mutations inFrontiers in cellular and infection microbiology · 2023
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  11. Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. Acyltransferases in bacteria.Microbiology and molecular biology reviews : MMBR · 2013
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

5 authors at 2 institutions in 1 country.

Yih-Ling TzengDivision of Infectious Diseases, Department of Medicine, Emory University School of Medicine, Atlanta, GA 30303, USA.
Anup Datta
V Kumar Kolli
Russell W Carlson
David S Stephens
University of Georgia · USEmory University · US

Funding

MENINGOCOCCAL LIPOOLIGOSACCHARIDE &MUCOSAL PATHOGENESISR01AI033517 · NIAID · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 1993 to 2007
$1.7M
REGULATION OF CAPSULE BIOSYNTHESIS IN N MENINGITIDISR01AI040247 · NIAID · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 1997 to 2006
$1.2M
REGULATION OF CAPSULE BIOSYNTHESIS IN N MENINGITIDISR21AI040247 · NIAID · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 1996 to 1996
–
NIAID NIH HHS AI-33517NIAID NIH HHS AI40247NIAID NIH HHS R01 AI033517NIAID NIH HHS R01 AI040247
6 · The paper itself

Abstract

Lipopolysaccharide, lipooligosaccharide (LOS), or endotoxin is important in bacterial survival and the pathogenesis of gram-negative bacteria. A necessary step in endotoxin biosynthesis is 3-deoxy-D-manno-octulosonic acid (Kdo) glycosylation of lipid A, catalyzed by the Kdo transferase KdtA (WaaA). In enteric gram-negative bacteria, this step is essential for survival. A nonpolar kdtA::aphA-3 mutation was created in Neisseria meningitidis via allelic exchange, and the mutant was viable. Detailed structural analysis demonstrated that the endotoxin of the kdtA::aphA-3 mutant was composed of fully acylated lipid A with variable phosphorylation but without Kdo glycosylation. In contrast to what happens in other gram-negative bacteria, tetra-acylated lipid IV(A) did not accumulate. The LOS structure of the kdtA::aphA-3 mutant was restored to the wild-type structure by complementation with kdtA from N. meningitidis or Escherichia coli. The expression of a fully acylated, unglycosylated lipid A indicates that lipid A biosynthesis in N. meningitidis can proceed without the addition of Kdo and that KdtA is not essential for survival of the meningococcus.

Indexed as

AllelesElectrophoresis, Polyacrylamide GelEndopeptidase KGenetic Complementation TestGenetic VectorsGenotypeLipid ALipopolysaccharidesMolecular StructureMutationNeisseria meningitidisPhosphorylationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSugar AcidsTransferases2-keto-3-deoxyoctonate3-deoxy-D-manno-octulosonate transferaseEndopeptidase KLipid Alipid-linked oligosaccharidesLipopolysaccharidesSugar AcidsTransferases

Identifiers

PMID11948150
PMCPMC134985
OpenAlexW2110299601

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.