Direct interaction between phosphotransferase LpxT and ArnT modulates polymyxin B resistance in <i>Pseudomonas aeruginosa</i>

Treatment of <i>Pseudomonas aeruginosa</i> infections is challenging due to its antibiotic resistance. Polymyxins are considered last-resort options for treating serious infections caused by multidrug-resistant <i>P. aeruginosa</i>. Understanding the molecular mechanisms of polymyxin resistance may provide clues for the development of new therapeutic strategies against <i>P. aeruginosa</i>. In this study, we demonstrated that the phosphatidic acid-phosphatase family (PAP2) protein LpxT interacts with L-Ara4N transferase ArnT and controls polymyxin B resistance in <i>P. aeruginosa</i>. Our findings reveal a novel role for lpxT and its molecular mechanism to defend against polymyxin B in <i>P. aeruginosa</i>.

Authors

Institutions

Publication Details

Journal
Microbiology Spectrum
Published
2026-03-23
DOI
https://doi.org/10.1128/spectrum.01852-25
Primary Topic
Antibiotic Resistance in Bacteria
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Direct interaction between phosphotransferase LpxT and ArnT modulates polymyxin B resistance in Pseudomonas aeruginosa

Weihui Wu, Yu Zhen Yuan, Zhihui Cheng, Fang Bai et al.
Microbiology Spectrum
Antibiotic Resistance in Bacteria
article

Direct interaction between phosphotransferase LpxT and ArnT modulates polymyxin B resistance in Pseudomonas aeruginosa

Weihui Wu, Yu Zhen Yuan, Zhihui Cheng, Fang Bai, Yuxi Bai, Yongxin Jin, Un-Hwan Ha, Yue Zhao, Shouguang Jin
article en

Abstract

Treatment of <i>Pseudomonas aeruginosa</i> infections is challenging due to its antibiotic resistance. Polymyxins are considered last-resort options for treating serious infections caused by multidrug-resistant <i>P. aeruginosa</i>. Understanding the molecular mechanisms of polymyxin resistance may provide clues for the development of new therapeutic strategies against <i>P. aeruginosa</i>. In this study, we demonstrated that the phosphatidic acid-phosphatase family (PAP2) protein LpxT interacts with L-Ara4N transferase ArnT and controls polymyxin B resistance in <i>P. aeruginosa</i>. Our findings reveal a novel role for lpxT and its molecular mechanism to defend against polymyxin B in <i>P. aeruginosa</i>.

Microbiology Spectrum
Korea University (KR), Nankai University (CN), State Key Laboratory of Medicinal Chemical Biology
Good health and well-being
Openalex Percentile: Top 12%
Antibiotic Resistance in Bacteria
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Direct interaction between phosphotransferase LpxT and ArnT modulates polymyxin B resistance in <i>Pseudomonas aeruginosa</i> — Weihui Wu, Yu Zhen Yuan, et al. · Microbiology Spectrum (2026) | TGRS Research Map | TGRS