Characterization of tail sheath protein of giant bacteriophage φKZ Pseudomonas aeruginosa

被引:5
作者
Kurochkina, Lidia P. [1 ]
Aksyuk, Anastasia A. [2 ]
Sachkova, Maria Yu. [1 ]
Sykilinda, Nina N. [1 ]
Mesyanzhinov, Vadim V. [1 ]
机构
[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia
[2] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
关键词
Bacteriophage phi KZ; Bacteriophage T4; Pseudomonas aeruginosa; Tail sheath protein; Immunoelectron microscopy; LYTIC TRANSGLYCOSYLASE; MICROSCOPY; MORPHOGENESIS; ARCHITECTURE; EVOLUTION; GENOME; PHAGES; GP144; EL;
D O I
10.1016/j.virol.2009.09.015
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The tail sheath protein of giant bacteriophage phi KZ 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 phi KZ proteins to proteins of other bacteriophages, some characteristic biochemical properties of gp29 revealed similarities to the tail sheath protein of bacteriophage T4. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:312 / 317
页数:6
相关论文
共 28 条
[1]   Bacteriophage observations and evolution [J].
Ackermann, HW .
RESEARCH IN MICROBIOLOGY, 2003, 154 (04) :245-251
[2]   The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria [J].
Aksyuk, Anastasia A. ;
Leiman, Petr G. ;
Kurochkina, Lidia P. ;
Shneider, Mikhail M. ;
Kostyuchenko, Victor A. ;
Mesyanzhinov, Vadim V. ;
Rossmann, Michael G. .
EMBO JOURNAL, 2009, 28 (07) :821-829
[3]   STRUCTURAL STUDIES OF THE CONTRACTILE TAIL SHEATH PROTEIN OF BACTERIOPHAGE-T4 .2. STRUCTURAL-ANALYSES OF THE TAIL SHEATH PROTEIN, GP18, BY LIMITED PROTEOLYSIS, IMMUNOBLOTTING, AND IMMUNOELECTRON MICROSCOPY [J].
ARISAKA, F ;
TAKEDA, S ;
FUNANE, K ;
NISHIJIMA, N ;
ISHII, S .
BIOCHEMISTRY, 1990, 29 (21) :5057-5062
[4]   Does common architecture reveal a viral lineage spanning all three domains of life? [J].
Benson, SD ;
Bamford, JKH ;
Bamford, DH ;
Burnett, RM .
MOLECULAR CELL, 2004, 16 (05) :673-685
[5]   Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages φKZ and EL [J].
Briers, Yves ;
Volckaert, Guido ;
Cornelissen, Anneleen ;
Lagaert, Stijn ;
Michiels, Chris W. ;
Hertveldt, Kirsten ;
Lavigne, Rob .
MOLECULAR MICROBIOLOGY, 2007, 65 (05) :1334-1344
[6]   PROTEIN COMPOSITION OF TAIL AND CONTRACTED SHEATH OF BACTERIOPHAGE-T4 [J].
DICKSON, RC .
VIROLOGY, 1974, 59 (01) :123-138
[7]   Shared architecture of bacteriophage SPO1 and herpesvirus capsids [J].
Duda, RL ;
Hendrix, RW ;
Huang, WM ;
Conway, JF .
CURRENT BIOLOGY, 2006, 16 (01) :R11-R13
[8]   Engineering of bacteriophage T4 tail sheath protein [J].
Efimov, AV ;
Kurochkina, LP ;
Mesyanzhinov, VV .
BIOCHEMISTRY-MOSCOW, 2002, 67 (12) :1366-1370
[9]   A three-dimensional cryo-electron microscopy structure of the bacteriophage φKZ head [J].
Fokine, A ;
Kostyuchenko, VA ;
Efimov, AV ;
Kurochkina, LP ;
Sykilinda, NN ;
Robben, J ;
Volckaert, G ;
Hoenger, A ;
Chipman, PR ;
Battisti, AJ ;
Rossmann, MG ;
Mesyanzhinov, VV .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 352 (01) :117-124
[10]   Structure of the bacteriophage φKZ lytic transglycosylase gp144 [J].
Fokine, Andrei ;
Miroshnikov, Konstantin A. ;
Shneider, Mikhail M. ;
Mesyanzhinov, Vadim V. ;
Rossmann, Michael G. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (11) :7242-7250