Evidence map›Paper›PMID 25245810›Full record

ArticleInfection and immunity2014

Lactate dehydrogenase is the key enzyme for pneumococcal pyruvate metabolism and pneumococcal survival in blood.

Paula Gaspar, Firas A Y Al-Bayati, Peter W Andrew, Ana Rute Neves, Hasan Yesilkaya

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

47 citing papers in PubMed, 75 citations in OpenAlex.

  1. Lactate Oxidase (LctO) Acts as a Metabolic Checkpoint RestrainingbioRxiv : the preprint server for biology · 2026
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  11. Lactate dehydrogenase is the Achilles' heel of Lyme disease bacteriumbioRxiv : the preprint server for biology · 2025
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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 3 institutions in 3 countries.

Paula GasparInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Firas A Y Al-BayatiDepartment of Infection, Immunity & Inflammation, University of Leicester, Leicester, United Kingdom Department of Biology, College of Education, University of Mosul, Mosul, Iraq.
Peter W AndrewDepartment of Infection, Immunity & Inflammation, University of Leicester, Leicester, United Kingdom.
Ana Rute NevesInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Hasan YesilkayaDepartment of Infection, Immunity & Inflammation, University of Leicester, Leicester, United Kingdom hy3@le.ac.uk.
Universidade Nova de Lisboa · PTUniversity of Leicester · GBUniversity of Mosul · IQ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pneumoniae is a fermentative microorganism and causes serious diseases in humans, including otitis media, bacteremia, meningitis, and pneumonia. However, the mechanisms enabling pneumococcal survival in the host and causing disease in different tissues are incompletely understood. The available evidence indicates a strong link between the central metabolism and pneumococcal virulence. To further our knowledge on pneumococcal virulence, we investigated the role of lactate dehydrogenase (LDH), which converts pyruvate to lactate and is an essential enzyme for redox balance, in the pneumococcal central metabolism and virulence using an isogenic ldh mutant. Loss of LDH led to a dramatic reduction of the growth rate, pinpointing the key role of this enzyme in fermentative metabolism. The pattern of end products was altered, and lactate production was totally blocked. The fermentation profile was confirmed by in vivo nuclear magnetic resonance (NMR) measurements of glucose metabolism in nongrowing cell suspensions of the ldh mutant. In this strain, a bottleneck in the fermentative steps is evident from the accumulation of pyruvate, revealing LDH as the most efficient enzyme in pyruvate conversion. An increase in ethanol production was also observed, indicating that in the absence of LDH the redox balance is maintained through alcohol dehydrogenase activity. We also found that the absence of LDH renders the pneumococci avirulent after intravenous infection and leads to a significant reduction in virulence in a model of pneumonia that develops after intranasal infection, likely due to a decrease in energy generation and virulence gene expression.

Indexed as

Microbial ViabilityAnimalsBacteremiaBloodDisease Models, AnimalFemaleFermentationGene DeletionLactic AcidL-Lactate DehydrogenaseMicePneumonia, PneumococcalPyruvic AcidStreptococcus pneumoniaeVirulenceLactic AcidL-Lactate DehydrogenasePyruvic Acid

Identifiers

PMID25245810
PMCPMC4249287
OpenAlexW2104762874

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.