Evidence map›Paper›PMID 10438750›Full record

ArticleJournal of bacteriology1999

Staphylococcus aureus cap5P encodes a UDP-N-acetylglucosamine 2-epimerase with functional redundancy.

K B Kiser, N Bhasin, L Deng, J C Lee

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Sensitizing methicillin-resistantAntimicrobial agents and chemotherapy · 2024
    Article
  3. Review
  4. Crystal structure of the capsular polysaccharide-synthesis enzyme CapG from Staphylococcus aureus.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  5. Article
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  8. Article
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  13. Article
  14. Article
  15. Article
  16. Staphylococcus aureus capsular polysaccharides.Clinical microbiology reviews · 2004
    Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

K B KiserChanning Laboratory, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
N Bhasin
L Deng
J C Lee
Brigham and Women's Hospital · USHarvard University · US

Funding

INFECTIOUS DISEASE AND BASIC MICROBIOLOGICAL MECHANISMST32AI007061 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI Marcia B Goldberg · 1985 to 2026
$12.1M
GENETIC ANALYSIS OF S AUREUS CAPSULE PRODUCTIONR01AI029040 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI LEE, JEAN CLAIRE · 1990 to 2005
$1.5M
MECHANISMS IN MICROBIAL PATHOGENESIST32AI007410 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI MEKALANOS, JOHN J · 1992 to 2001
$345k
GENETIC ANALYSIS OF S. AUREUS CAPSULE PRODUCTIONR21AI029040 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI LEE, JEAN CLAIRE · 2000 to 2000
$285k
NIAID NIH HHS AI 29040NIAID NIH HHS R01 AI029040NIAID NIH HHS R21 AI029040NIAID NIH HHS T32 AI007061NIAID NIH HHS T32 AI007410NIAID NIH HHS T32-AI 07061NIAID NIH HHS T32-AI 07410
6 · The paper itself

Abstract

The serotype 5 capsule gene cluster of Staphylococcus aureus comprises 16 genes (cap5A through cap5P), but little is known about how the putative gene products function in capsule biosynthesis. We propose that the N-acetylmannosaminuronic acid (ManNAcA) component of the S. aureus serotype 5 capsular polysaccharide (CP5) is synthesized from a UDP-N-acetylglucosamine (UDP-GlcNAc) precursor that is epimerized to UDP-N-acetylmannosamine (UDP-ManNAc) and then oxidized to UDP-ManNAcA. We report the purification and biochemical characterization of a recombinant UDP-GlcNAc 2-epimerase encoded by S. aureus cap5P. Purified Cap5P converted approximately 10% of UDP-GlcNAc to UDP-ManNAc as detected by gas chromatography-mass spectrometry. The epimerization of UDP-GlcNAc to UDP-ManNAc occurred over a wide pH range and was unaffected by divalent cations. Surprisingly, CP5 expression in S. aureus was unaffected by insertional inactivation of cap5P. Sequence homology searches of the public S. aureus genomic databases revealed the presence of another putative UDP-GlcNAc 2-epimerase on the S. aureus chromosome that showed 61% identity to Cap5P. Redundancy of UDP-GlcNAc 2-epimerase function in S. aureus was demonstrated by cloning the cap5P homologue from strain Newman and complementing an Escherichia coli rffE mutant defective in UDP-GlcNAc 2-epimerase activity. Our results confirm the putative function of the S. aureus cap5P gene product and demonstrate the presence of a second gene on the staphylococcal chromosome with a similar function.

Indexed as

Carrier ProteinsBacterial ProteinsCarbohydrate EpimerasesChromosomes, BacterialDNA PrimersEnzyme ActivationGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHydrogen-Ion ConcentrationMolecular Sequence DataMutagenesis, InsertionalPhenotypeSequence Homology, Nucleic AcidStaphylococcus aureusBacterial ProteinsCap5 protein, StaphylococcusCarbohydrate EpimerasesCarrier ProteinsDNA PrimersN-acyl-D-glucosamine 2-epimerase

Identifiers

PMID10438750
PMCPMC93967
OpenAlexW2157083677

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.