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The mechanism of the phage-encoded protein antibiotic from ΦX174

Anna K Orta1, Nadia Riera1, Yancheng E Li1

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Science (New York, N.Y.)
|July 13, 2023
PubMed

Insights

Bacteriophage protein E forms a complex with bacterial proteins MraY and SlyD, inhibiting cell wall synthesis and causing bacterial lysis. This discovery clarifies phage lysis mechanisms and aids in developing new phage therapies.

Area of Science:

  • Structural biology
  • Microbiology
  • Virology

Background:

  • Bacteriophage ΦX174 employs protein E, a 91-residue protein antibiotic, to induce lysis in its host bacteria.
  • The precise mechanism by which protein E mediates bacterial lysis has remained incompletely understood.

Purpose of the Study:

  • To elucidate the structural basis of bacteriophage ΦX174 protein E-mediated bacterial lysis.
  • To characterize the structure of the Escherichia coli MraY enzyme and the SlyD chaperone.

Main Methods:

  • Single-particle electron cryo-microscopy (cryo-EM) was utilized to determine the structure of the MraY-protein E-SlyD complex.
  • Structural characterization of Escherichia coli MraY and SlyD was performed.

Main Results:

  • Protein E bridges bacterial MraY and SlyD, forming the transmembrane YES complex.
  • Protein E obstructs the MraY active site, inhibiting peptidoglycan biosynthesis by blocking lipid I production.
  • Structural details of E. coli MraY and SlyD were revealed.

Conclusions:

  • A detailed model for phage-mediated bacterial lysis involving the YES complex is proposed.
  • The findings unify previous experimental data and provide structural insights into essential bacterial enzymes.
  • The determined structures offer a foundation for structure-based design of novel phage therapeutics.

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