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Title: Characterization of tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa

Abstract

The tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa encoded by gene 29 was identified and its expression system was developed. Localization of the protein on the virion was confirmed by immunoelectron microscopy. Properties of gene product (gp) 29 were studied by electron microscopy, immunoblotting and limited trypsinolysis. Recombinant gp29 assembles into the regular tubular structures (polysheaths) of variable length. Trypsin digestion of gp29 within polysheaths or extended sheath of virion results in specific cleavage of the peptide bond between Arg135 and Asp136. However, this cleavage does not affect polymeric structure of polysheaths, sheaths and viral infectivity. Digestion by trypsin of the C-truncated gp29 mutant, lacking the ability to self-assemble, results in formation of a stable protease-resistant fragment. Although there is no sequence homology of phiKZ proteins to proteins of other bacteriophages, some characteristic biochemical properties of gp29 revealed similarities to the tail sheath protein of bacteriophage T4.

Authors:
 [1]; ; ;  [2]
  1. Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054 (United States)
  2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow 117997 (Russian Federation)
Publication Date:
OSTI Identifier:
21357578
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 395; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2009.09.015; PII: S0042-6822(09)00575-3; Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; BACTERIOPHAGES; CLEAVAGE; ELECTRON MICROSCOPY; GENES; INFECTIVITY; MUTANTS; PEPTIDES; PSEUDOMONAS; TRYPSIN; BACTERIA; ENZYMES; HYDROLASES; MICROORGANISMS; MICROSCOPY; MICROSTRUCTURE; ORGANIC COMPOUNDS; PARASITES; PEPTIDE HYDROLASES; PROTEINS; SERINE PROTEINASES; VIRUSES

Citation Formats

Kurochkina, Lidia P., E-mail: lpk@ibch.r, Aksyuk, Anastasia A, Sachkova, Maria Yu, Sykilinda, Nina N, and Mesyanzhinov, Vadim V. Characterization of tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa. United States: N. p., 2009. Web. doi:10.1016/j.virol.2009.09.015.
Kurochkina, Lidia P., E-mail: lpk@ibch.r, Aksyuk, Anastasia A, Sachkova, Maria Yu, Sykilinda, Nina N, & Mesyanzhinov, Vadim V. Characterization of tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa. United States. https://doi.org/10.1016/j.virol.2009.09.015
Kurochkina, Lidia P., E-mail: lpk@ibch.r, Aksyuk, Anastasia A, Sachkova, Maria Yu, Sykilinda, Nina N, and Mesyanzhinov, Vadim V. 2009. "Characterization of tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa". United States. https://doi.org/10.1016/j.virol.2009.09.015.
@article{osti_21357578,
title = {Characterization of tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa},
author = {Kurochkina, Lidia P., E-mail: lpk@ibch.r and Aksyuk, Anastasia A and Sachkova, Maria Yu and Sykilinda, Nina N and Mesyanzhinov, Vadim V},
abstractNote = {The tail sheath protein of giant bacteriophage phiKZ Pseudomonas aeruginosa encoded by gene 29 was identified and its expression system was developed. Localization of the protein on the virion was confirmed by immunoelectron microscopy. Properties of gene product (gp) 29 were studied by electron microscopy, immunoblotting and limited trypsinolysis. Recombinant gp29 assembles into the regular tubular structures (polysheaths) of variable length. Trypsin digestion of gp29 within polysheaths or extended sheath of virion results in specific cleavage of the peptide bond between Arg135 and Asp136. However, this cleavage does not affect polymeric structure of polysheaths, sheaths and viral infectivity. Digestion by trypsin of the C-truncated gp29 mutant, lacking the ability to self-assemble, results in formation of a stable protease-resistant fragment. Although there is no sequence homology of phiKZ proteins to proteins of other bacteriophages, some characteristic biochemical properties of gp29 revealed similarities to the tail sheath protein of bacteriophage T4.},
doi = {10.1016/j.virol.2009.09.015},
url = {https://www.osti.gov/biblio/21357578}, journal = {Virology},
issn = {0042-6822},
number = 2,
volume = 395,
place = {United States},
year = {Sun Dec 20 00:00:00 EST 2009},
month = {Sun Dec 20 00:00:00 EST 2009}
}