Evidence map›Paper›PMID 15731025›Full record

ArticleInfection and immunity2005

Sialic Acid metabolism and systemic pasteurellosis.

Susan M Steenbergen, Carol A Lichtensteiger, Ruth Caughlan, Jackie Garfinkle, Troy E Fuller, Eric R Vimr

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Pasteurella multocida: Genotypes and Genomics.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Bacterial periplasmic sialic acid-binding proteins exhibit a conserved binding site.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

6 authors at 2 institutions in 1 country.

Susan M SteenbergenLaboratory of Sialobiology, Department of Pathobiology, Universityof Illinois at Urbana-Champaign, Urbana, IL 61802, USA.
Carol A Lichtensteiger
Ruth Caughlan
Jackie Garfinkle
Troy E Fuller
Eric R Vimr
University of Illinois Urbana-Champaign · USPfizer (United States) · US

Funding

Regulation of the Poly Sialic Virulence FactorR01AI042015 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI VIMR, ERIC ROSS · 1998 to 2014
$2.6M
NIAID NIH HHS 2R01 AI42015NIAID NIH HHS R01 AI042015
6 · The paper itself

Abstract

Pasteurella multocida subsp. multocida is a commensal and opportunistic pathogen of food animals, wildlife, and pets and a zoonotic cause of human infection arising from contacts with these animals. Here, an investigation of multiple serotype A strains demonstrated the occurrence of membrane sialyltransferase. Although P. multocida lacks the genes for the two earliest steps in de novo sialic acid synthesis, adding sialic acid to the growth medium resulted in uptake, activation, and subsequent transfer of sialic acid to a membrane acceptor resembling lipooligosaccharide. Two candidate-activating enzymes with homology to Escherichia coli cytidine 5'-monophospho-N-acetylneuraminate synthetase were overproduced as histidine-tagged polypeptides. The synthetase encoded by pm0187 was at least 37 times more active than the pm1710 gene product, suggesting pm0187 encodes the primary sialic acid cytidylyltransferase in P. multocida. A sialate aldolase (pm1715) mutant unable to initiate dissimilation of internalized sialic acid was not attenuated in the CD-1 mouse model of systemic pasteurellosis, indicating that the nutritional function of sialate catabolism is not required for systemic disease. In contrast, the attenuation of a sialate uptake-deficient mutant supports the essential role in pathogenesis of a sialylation mechanism that is dependent on an environmental (host) supply of sialic acid. The combined results provide the first direct evidence of sialylation by a precursor scavenging mechanism in pasteurellae and of a potential tripartite ATP-independent periplasmic sialate transporter in any species.

Indexed as

AnimalsAnimals, Outbred StrainsCattleCytidine Monophosphate N-Acetylneuraminic AcidDisease Models, AnimalFemaleFructose-Bisphosphate AldolaseHumansMiceOpen Reading FramesPasteurella InfectionsPasteurella multocidaSialic AcidsSialyltransferasesVirulenceCytidine Monophosphate N-Acetylneuraminic AcidFructose-Bisphosphate AldolaseSialic AcidsSialyltransferases

Identifiers

PMID15731025
PMCPMC1064920
OpenAlexW2140684243

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.