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<b>Abstract</b>— <p>The chaperonin family, comprising heat shock proteins with a molecular mass of ~60 kDa, is found in both prokaryotic (including archaea) and eukaryotic organisms. Chaperonins have also been recently found in bacteriophages. These proteins possess the structural and functional properties precluding their identification as members of the already known chaperonin groups. The function of phage chaperonins in the process of viral development remains unknown. In the present work, we generated OBP bacteriophage strains encoding mutant chaperonin forms and showed that these mutations are lethal. It was also shown that the chaperonins of related bacteriophages OBP and EL were not mutually replaceable.</p>

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The CpnOBP Chaperonin Function Is Required for Lytic Cycle Development in the Pseudomonas fluorescens Bacteriophage OBP

  • 期刊论文

  • 发表日期：

    2026年5月25日

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  • D. Zyurkalova,
  • U. F. Dzhus,
  • A. G. Gabdulkhakov,
  • A. S. Glukhov

摘要

Abstract—

The chaperonin family, comprising heat shock proteins with a molecular mass of ~60 kDa, is found in both prokaryotic (including archaea) and eukaryotic organisms. Chaperonins have also been recently found in bacteriophages. These proteins possess the structural and functional properties precluding their identification as members of the already known chaperonin groups. The function of phage chaperonins in the process of viral development remains unknown. In the present work, we generated OBP bacteriophage strains encoding mutant chaperonin forms and showed that these mutations are lethal. It was also shown that the chaperonins of related bacteriophages OBP and EL were not mutually replaceable.