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Protein scaffold involving MSMEG_1285 maintains cell wall organization and mediates penicillin sensitivity in

Romain Veyron-Churlet1, Jean-Michel Saliou1, Camille Locht1

  • 1U1019 - UMR9017 - CIIL - Center for Infection and Immunity of Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, Université de Lille, France.

The FEBS Journal
|January 30, 2020
PubMed

Insights

MSMEG_1285 protein interacts with PonA1, impacting Mycobacterium smegmatis cell wall integrity and antibiotic resistance. This interaction regulates peptidoglycan hydrolysis, offering new targets for drug development.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for mycobacterial physiology, particularly in cell wall biosynthesis.
  • The mycobacterial cell wall is complex and essential for bacterial survival.

Purpose of the Study:

  • To investigate the interaction between MSMEG_1285 and PonA1.
  • To understand the role of MSMEG_1285 in mycobacterial cell wall regulation and antibiotic resistance.

Main Methods:

  • Investigated protein-protein interactions using genetic deletion studies.
  • Analyzed changes in antibiotic resistance, cell wall porin amounts, and peptidoglycan hydrolase activity.

Main Results:

  • MSMEG_1285 interacts with PonA1, a key enzyme in peptidoglycan biosynthesis.
  • Deletion of MSMEG_1285 increases resistance to penicillin antibiotics, an effect amplified by hbhA deletion.
  • Loss of MSMEG_1285 and hbhA leads to reduced porin levels and increased peptidoglycan degradation enzymes.

Conclusions:

  • MSMEG_1285, PonA1, and HbhA form a protein scaffold regulating peptidoglycan hydrolysis.
  • This finding enhances understanding of mycobacterial physiology and aids in developing drugs targeting cell wall synthesis.
Keywords:
Mycobacteriumantibiotic resistancepenicillinprotein-protein interactionstuberculosis

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