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Mechanistic insight into mycobacterial MmpL protein function.

R Székely1, S T Cole1

  • 1Ecole Polytechnique Fédérale de Lausanne, Global Health Institute, CH1015, Lausanne, Switzerland.

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|December 30, 2015
PubMed
Summary
This summary is machine-generated.

A mutation in the MmpL4a transporter of Mycobacterium bolletii prevents glycopeptidolipid export, altering cell wall structure and increasing virulence. This finding reveals a critical residue for transporter function and has implications for understanding mycobacterial cell wall biogenesis.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Mycobacterial cell walls possess complex lipid structures influencing virulence.
  • Understanding lipid export mechanisms is crucial for cell wall biogenesis research.

Purpose of the Study:

  • Investigate the structure and function of MmpL proteins, key transporters in the resistance-nodulation-cell division (RND) superfamily.
  • Elucidate the role of a specific mutation in the mmpL4a gene of Mycobacterium bolletii on glycopeptidolipid export and virulence.

Main Methods:

  • Structural and functional investigation of MmpL proteins.
  • Site-directed mutagenesis (Tyr842His in mmpL4a) and cross-species residue replacement (MmpL3 in Mycobacterium tuberculosis).
  • Structural modeling and experimental validation.

Main Results:

  • A Tyr842His mutation in mmpL4a caused a failure in glycopeptidolipid (GPL) export, leading to a smooth-to-rough morphotype change in Mycobacterium bolletii.
  • This mutation significantly increased pathogen virulence in infection models.
  • Tyr842 was identified as a critical residue for mediating the proton motive force essential for GPL export, a finding conserved across MmpL proteins.

Conclusions:

  • The study identifies a critical functional residue (Tyr842) in MmpL transporters essential for lipid export and virulence.
  • Mechanistic insights into MmpL4a function provide a broader understanding applicable to MmpL family and RND transporters.
  • Findings contribute to understanding mycobacterial cell wall biogenesis and potential therapeutic targets.