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Structural basis for bacteriophage phi X174 assembly and eclipse as defined by temperature-sensitive mutations

L L Ilag1, N L Incardona

  • 1Department of Microbiology and Immunology, University of Tennessee, Memphis.

Virology
|October 1, 1993
PubMed
Summary
This summary is machine-generated.

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A new screening method classifies bacteriophage phi X174 mutants. Most mutants affect late functions, with structural proteins F, G, and H implicated in maturation and DNA ejection.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Bacteriophage phi X174 is a model system for studying viral replication and assembly.
  • Understanding the functions of viral genes is crucial for deciphering the viral life cycle.

Purpose of the Study:

  • To develop and validate a screening procedure for classifying bacteriophage phi X174 temperature-sensitive (ts) mutants.
  • To identify the specific genes and functions affected by these mutations.

Main Methods:

  • Application of a novel screening procedure to 108 ts mutants.
  • Quantitative one-step growth curve analysis.
  • Genetic mapping of mutations.
  • Analysis of amino acid substitutions within the atomic structure of wild-type (wt) virions.

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Main Results:

  • The screening procedure classified most mutants as defective in "late" functions (22/27).
  • Mutations in "late" and "intermediate" classes primarily affected genes F, G, and H (structural proteins).
  • Amino acid substitutions in F and G proteins suggest defects in protein-protein interactions during maturation and altered viral eclipse kinetics.

Conclusions:

  • The F capsid protein plays a critical role in DNA ejection from the bacteriophage phi X174 capsid.
  • The screening procedure effectively categorizes viral mutants, aiding in the study of viral mechanisms.
  • Structural analysis of mutations provides insights into the molecular basis of viral assembly and function.