J 2009

Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2

PLEVKA, Pavel, Kaspars TARS and Lars LILJAS

Basic information

Original name

Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2

Authors

PLEVKA, Pavel, Kaspars TARS and Lars LILJAS

Edition

Protein Science, HOBOKEN, JOHN WILEY & SONS INC, 2009, 0961-8368

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 2.937

Organization unit

Central European Institute of Technology

DOI

UT WoS

000268882100009

Keywords in English

virus; structure; assembly; stability

Tags

Změněno: 30/3/2017 11:22, Mgr. Eva Špillingová

Abstract

V originále

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.