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Glycosylation of a Streptomyces coelicolor A3(2) cell envelope protein is required for infection by bacteriophage phi

D A Cowlishaw1, M C Smith

  • 1Institute of Genetics, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, UK.

Molecular Microbiology
|September 5, 2001
PubMed

Insights

Streptomyces coelicolor mutants resistant to phage phi C31 were identified. The phage receptor is proposed to be a cell wall glycoprotein, with mutations affecting glycosylation blocking phage infection.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Virology

Background:

  • Streptomyces coelicolor is a model organism for studying bacterial genetics and secondary metabolite production.
  • Bacteriophages are viruses that infect bacteria and play crucial roles in microbial ecosystems.
  • Understanding phage-host interactions is vital for controlling bacterial infections and phage therapy.

Purpose of the Study:

  • To investigate the mechanism of resistance in Streptomyces coelicolor mutants to the temperate phage phi C31.
  • To identify the genetic basis of phage resistance and characterize the phage receptor.
  • To elucidate the role of glycosylation in phage adsorption and infection.

Main Methods:

  • Isolation and characterization of phage-resistant mutants of Streptomyces coelicolor.
  • Genetic complementation using a cosmid library to identify responsible genes.
  • Biochemical assays using Concanavalin A (ConA) to probe for glycosylated proteins.
  • Phage infection assays with wild-type and mutant strains, including analysis of phage DNA transfection and infective center formation.

Main Results:

  • Mutants resistant to phage phi C31 were isolated, with resistance mapped to the adsorption/DNA injection step.
  • A class I mutant was complemented by gene SCE87.05, homologous to O-D-mannosyltransferases, suggesting a role in protein glycosylation.
  • Concanavalin A inhibited phi C31 infection, and glycosylated proteins were detected in wild-type but not in class I mutants.
  • Mutants showed sensitivity to phi C31hc and phi DT4002 phages, suggesting the phi C31h mutation compensates for altered receptor glycosylation.

Conclusions:

  • The receptor for phage phi C31 on Streptomyces coelicolor is likely a cell wall glycoprotein.
  • Mutations affecting the glycosylation of this receptor confer resistance to phi C31.
  • The phi C31h mutation may enable the phage to infect bacteria with altered receptor glycosylation patterns.

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