Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

Jenni Karttunen, Sari Mäntynen, Teemu O. Ihalainen, Heli Lehtivuori, Nikolai V. Tkachenko, Maija Vihinen-Ranta, Janne A. Ihalainen, Jaana K H Bamford, Hanna M. Oksanen*

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their localization in living cells by confocal microscopy, indicated that multimeric PRD1 proteins were prone to localize in the cell poles. Furthermore, PRD1 spike complex proteins P5 and P31, as fusion proteins, were shown to be functional in the virion assembly. In addition, they were shown to co-localize in the specific polar area of the cells, which might have a role in the multimerization and formation of viral protein complexes.

Original languageEnglish
Pages (from-to)44-52
Number of pages9
JournalVirus Research
Volume179
DOIs
Publication statusPublished - 22 Jan 2014

Keywords

  • Bacteria
  • Confocal microscopy
  • Membrane virus
  • Protein interactions
  • Virus assembly

Fingerprint Dive into the research topics of 'Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli'. Together they form a unique fingerprint.

Cite this