Details

Autor(en) / Beteiligte

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

Titel

Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

Ist Teil von

• Virus research, 2014-01, Vol.179, p.44-52

Ort / Verlag

Netherlands: Elsevier B.V

Erscheinungsjahr

2014

Quelle

ScienceDirect

Beschreibungen/Notizen

• •Membrane-containing virus PRD1 infecting Escherichia coli was used as a model.•We create a vector library for production of fluorescent fusion proteins.•We localize the fluorescent fusion proteins in living bacteria by confocal microscopy.•Mainly multimeric proteins were found in specific loci in Escherichia coli. 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.