Evidence map›Paper›PMID 33846132›Full record

ArticleAntimicrobial agents and chemotherapy2021

Escherichia coli GyrA Tower Domain Interacts with QnrB1 Loop B and Plays an Important Role in QnrB1 Protection from Quinolone Inhibition.

Chunhui Chen, Yin Wang, Hidemasa Nakaminami, Eu Suk Kim, George A Jacoby, David C Hooper

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 58% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Review
  2. Review
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 4 institutions in 3 countries.

Chunhui ChenDivision of Infectious Diseases, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Yin WangDivision of Infectious Diseases, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Hidemasa NakaminamiDepartment of Microbiology, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Eu Suk KimDivision of Infectious Diseases, Seoul National University Bundang Hospital, Seongnam, Gyeonggi-do, Republic of Korea.
George A JacobyLahey Hospital and Medical Center, Burlington, Massachusetts, USA.
David C HooperDivision of Infectious Diseases, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Harvard University · USLahey Medical Center · USSeoul National University Bundang Hospital · KRTokyo University of Pharmacy and Life Sciences · JP

Funding

Plasmid-mediated Quinolone ResistanceR01AI057576 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI HOOPER, DAVID C · 2004 to 2018
$5.3M
NIAID NIH HHS R01 AI057576
6 · The paper itself

Abstract

The Qnr pentapeptide repeat proteins interact with DNA gyrase and protect it from quinolone inhibition. The two external loops, particularly the larger loop B, of Qnr proteins are essential for quinolone protection of DNA gyrase. The specific QnrB1 interaction sites on DNA gyrase are not known. In this study, we investigated the interaction between GyrA and QnrB1 using site-specific photo-cross-linking of QnrB1 loop B combined with mass spectrometry. We found that amino acid residues 286 to 298 on the tower domain of GyrA interact with QnrB1 and play a key role in QnrB1 protection of gyrase from quinolone inhibition. Alanine replacement of arginine at residue 293 and a small deletion of amino acids 286 to 289 of GyrA resulted in a decrease in the QnrB1-mediated increase in quinolone MICs and also abolished the QnrB1 protection of purified DNA gyrase from ciprofloxacin inhibition.

Indexed as

DNA GyraseEscherichia coli ProteinsQuinolonesCiprofloxacinEscherichia coliMutationCiprofloxacinDNA GyraseEscherichia coli ProteinsQuinolonesgyraseprotein-protein interactionsQnrQnrB1quinolone

Identifiers

PMID33846132
PMCPMC8373224
OpenAlexW3153839459

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.