Evidence map›Paper›PMID 41130968›Full record

ArticleScientific reports2025

Structural basis for antibiotic resistance by chloramphenicol acetyltransferase type A in Staphylococcus aureus.

Kaiyue Wang, Junwei Chen, Wanfang Li, Min Wang, Tingwen Fan, Dongbo Bu, Sheng Ye

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

7 authors.

Kaiyue WangSchool of Biomedical Science and Medicine Engineering, Beihang University, Beijing, 100191, China.
Junwei ChenSchool of Biomedical Science and Medicine Engineering, Beihang University, Beijing, 100191, China.
Wanfang LiSchool of Arts and Sciences, Rutgers University, New Brunswick, NJ, 08901, USA.
Min WangState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Tingwen FanState Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Dongbo BuSKLP, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, 100190, China. dbu@ict.ac.cn.
Sheng YeSchool of Biomedical Science and Medicine Engineering, Beihang University, Beijing, 100191, China. yesheng@buaa.edu.cn.

Funding

Beijing Municipal Science & Technology Commission grant Z221100003522020
6 · The paper itself

Abstract

Methicillin-resistant Staphylococcus aureus (MRSA) exemplifies high-level antibiotic resistance in this major human pathogen. Its resistance to chloramphenicol is majorly conferred by enzymatic inactivation via chloramphenicol acetyltransferases (CATs). This modification sterically blocks the antibiotic's ribosomal binding and thus neutralizes its inhibitory potency. Although CATs have been structurally studied across diverse bacteria species, the structures of S. aureus CATs (saCATs) have remained uncharacterized. To address this gap and elucidate species-specific resistance mechanisms, we determined the first high-resolution crystal structure of saCAT1, the prototypical saCAT enzyme. Structural analysis delineates the active site architecture and reveals the molecular basis for substrate recognition of both chloramphenicol and fusidic acid (FA). Further enzymatic assays demonstrated that the K

Indexed as

Bacterial ProteinsChloramphenicol O-AcetyltransferaseDrug Resistance, BacterialMethicillin-Resistant Staphylococcus aureusStaphylococcus aureusAnti-Bacterial AgentsCatalytic DomainChloramphenicolCrystallography, X-RayFusidic AcidHumansModels, MolecularSubstrate SpecificityAnti-Bacterial AgentsBacterial ProteinsChloramphenicolChloramphenicol O-AcetyltransferaseFusidic AcidAntibiotic resistanceChloramphenicolChloramphenicol acetyltransferaseFusidic acidStaphylococcus aureus

Identifiers

PMID41130968
PMCPMC12549896

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.