| PLEVKA, Pavel, Kaspars TARS and Lars LILJAS. Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2. Protein Science. HOBOKEN: JOHN WILEY & SONS INC, 2009, vol. 18, No 8, p. 1653-1661. ISSN 0961-8368. Available from: https://dx.doi.org/10.1002/pro.184. |
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@article{1376896,
author = {Plevka, Pavel and Tars, Kaspars and Liljas, Lars},
article_location = {HOBOKEN},
article_number = {8},
doi = {http://dx.doi.org/10.1002/pro.184},
keywords = {virus; structure; assembly; stability},
language = {eng},
issn = {0961-8368},
journal = {Protein Science},
title = {Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2},
volume = {18},
year = {2009}
}
TY - JOUR
ID - 1376896
AU - Plevka, Pavel - Tars, Kaspars - Liljas, Lars
PY - 2009
TI - Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2
JF - Protein Science
VL - 18
IS - 8
SP - 1653-1661
EP - 1653-1661
PB - JOHN WILEY & SONS INC
SN - 09618368
KW - virus
KW - structure
KW - assembly
KW - stability
N2 - Particles formed by the bacteriophage MS2 coat protein mutants with insertions in their surface loops induce a strong immune response against the inserted epitopes. The covalent dimers created by fusion of two copies of the coat protein gene are more tolerant to various insertions into the surface loops than the single subunits. We determined a 4.7-angstrom resolution crystal structure of an icosahedral particle assembled from covalent dimers and compared its stability with wild-type virions. The structure resembled the wild-type virion except for the intersubunit linker regions. The covalent dimer orientation was random with respect to both icosahedral twofold and quasi-twofold symmetry axes. A fraction of the particles was unstable in phosphate buffer because of assembly defects. Our results provide a structural background for design of modified covalent coat protein dimer subunits for use in immunization.
ER -
PLEVKA, Pavel, Kaspars TARS and Lars LILJAS. Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2. \textit{Protein Science}. HOBOKEN: JOHN WILEY \&{}amp; SONS INC, 2009, vol.~18, No~8, p.~1653-1661. ISSN~0961-8368. Available from: https://dx.doi.org/10.1002/pro.184.
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