J 2009

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

PLEVKA, Pavel, Kaspars TARS a Lars LILJAS

Základní údaje

Originální název

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

Autoři

PLEVKA, Pavel, Kaspars TARS a Lars LILJAS

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.937

Organizační jednotka

Středoevropský technologický institut

DOI

UT WoS

000268882100009

Klíčová slova anglicky

virus; structure; assembly; stability

Štítky

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

Anotace

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.