Evidence map›Paper›PMID 20662782›Full record

ArticleMolecular microbiology2010

A two-component Kdo hydrolase in the inner membrane of Francisella novicida.

Jinshi Zhao, Christian R H Raetz

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Aminosugar-based immunomodulator lipid A: synthetic approaches.Beilstein journal of organic chemistry · 2018
    Review
  3. Article
  4. Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Biological reviews of the Cambridge Philosophical Society · 2015
    Review
  5. From the Outside-In: The Francisella tularensis Envelope and Virulence.Frontiers in cellular and infection microbiology · 2015
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Subversion of host recognition and defense systems by Francisella spp.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Jinshi ZhaoDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Christian R H Raetz
Duke University Hospital · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
LIPID A MODIFICATION SYSTEMS IN GRAM-NEGATIVE BACTERIAR37GM051796 · NIGMS · DUKE UNIVERSITY · PI RAETZ, CHRISTIAN R · 1999 to 2008
$3.0M
Lipid A Modification Systems in Gram-Negative BacteriaR01GM051796 · NIGMS · DUKE UNIVERSITY · PI ZHOU, PEI · 1995 to 2012
$1.5M
NIGMS NIH HHS GM-51796NIGMS NIH HHS R01 GM051796NIGMS NIH HHS R37 GM051796NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

Lipid A coats the outer surface of the outer membrane of Gram-negative bacteria. In Francisella tularensis subspecies novicida lipid A is present either as the covalently attached anchor of lipopolysaccharide (LPS) or as free lipid A. The lipid A moiety of Francisella LPS is linked to the core domain by a single 2-keto-3-deoxy-D-manno-octulosonic acid (Kdo) residue. F. novicida KdtA is bi-functional, but F. novicida contains a membrane-bound Kdo hydrolase that removes the outer Kdo unit. The hydrolase consists of two proteins (KdoH1 and KdoH2), which are expressed from adjacent, co-transcribed genes. KdoH1 (related to sialidases) has a single predicted N-terminal transmembrane segment. KdoH2 contains 7 putative transmembrane sequences. Neither protein alone catalyses Kdo cleavage when expressed in E. coli. Activity requires simultaneous expression of both proteins or mixing of membranes from strains expressing the individual proteins under in vitro assay conditions in the presence of non-ionic detergent. In E. coli expressing KdoH1 and KdoH2, hydrolase activity is localized in the inner membrane. WBB06, a heptose-deficient E. coli mutant that makes Kdo(2) -lipid A as its sole LPS, accumulates Kdo-lipid A when expressing the both hydrolase components, and 1-dephospho-Kdo-lipid A when expressing both the hydrolase and the Francisella lipid A 1-phosphatase (LpxE).

Indexed as

DNA, BacterialEscherichia coliEscherichia coli ProteinsFrancisella tularensisGlycoside HydrolasesMembrane ProteinsMolecular Sequence DataSequence Analysis, DNADNA, BacterialEscherichia coli ProteinsGlycoside Hydrolasesinner membrane protein, E coliMembrane Proteins

Identifiers

PMID20662782
PMCPMC2978271
OpenAlexW2105693309

What OpenQuestion holds

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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.