Evidence map›Paper›PMID 42027460›Full record

ArticleFrontiers in microbiology2026

The bacterial phosphotransferase system-mediated rifampicin phosphorylation: ancestral links to rifampicin-inactivating enzyme.

Šárka Bobková, Michaela Plechatá, Tomáš Kovaľ, Hana Šanderová, Simona Blažková, Rüveyda Akçin, Zdeněk Kameník, Jan Dohnálek, Libor Krásný, Jana Wiedermannová

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Šárka BobkováLaboratory of Microbial Genetics and Gene Expression, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Michaela PlechatáLaboratory of Antibiotic Resistance and Microbial Metabolomics, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Tomáš KovaľLaboratory of Structure and Function of Biomolecules, Institute of Biotechnology of the Czech Academy of Sciences, Vestec, Czechia.
Hana ŠanderováLaboratory of Microbial Genetics and Gene Expression, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Simona BlažkováLaboratory of Microbial Genetics and Gene Expression, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Rüveyda AkçinLaboratory of Microbial Genetics and Gene Expression, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Zdeněk KameníkLaboratory of Antibiotic Resistance and Microbial Metabolomics, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Jan DohnálekLaboratory of Structure and Function of Biomolecules, Institute of Biotechnology of the Czech Academy of Sciences, Vestec, Czechia.
Libor KrásnýLaboratory of Microbial Genetics and Gene Expression, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.
Jana WiedermannováLaboratory of Microbial Genetics and Gene Expression, Institute of Microbiology of the Czech Academy of Sciences, Prague, Czechia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: The bacterial phosphotransferase system (PTS) transports and phosphorylates sugars. Some PTS proteins share structural motifs with rifampicin phosphotransferases (RPHs), which inactivate rifampicin by phosphorylation. This homology suggests that the PTS may represent an evolutionary ancestor of the multi domain RPHs, though direct biochemical evidence has been lacking. Methods: Results: Deletion of Conclusion: This study shows that part of the PTS, protein EI, can phosphorylate rifampicin, supporting its evolutionary link to RPHs. We also establish that RphT, a putative rifampicin phosphotransferase misannotated as phosphoenolpyruvate synthase (Pps), is a

Indexed as

ancestral proteinantibiotic resistanceEnzyme Iphosphotransferase systemPTSrifampicinrifampicin phosphotransferase

Identifiers

PMID42027460
PMCPMC13099321

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.