Virus-like particles of a fish nodavirus display a capsid subunit domain organization different from that of insect nodaviruses.

Abstract:

:The structure of recombinant virus-like particles of malabaricus grouper nervous necrosis virus (MGNNV), a fish nodavirus isolated from the grouper Epinephelus malabaricus, was determined by electron cryomicroscopy (cryoEM) and three-dimensional reconstruction at 23-A resolution. The cryoEM structure, sequence comparison, and protein fold recognition analysis indicate that the coat protein of MGNNV has two domains resembling those of tomato bushy stunt virus and Norwalk virus, rather than the expected single-domain coat protein of insect nodaviruses. The analysis implies that residues 83 to 216 fold as a beta-sandwich which forms the inner shell of the T=3 capsid and residues 217 to 308 form the trimeric surface protrusions observed in the cryoEM map. The structural similarities between fish nodaviruses and members of the tombusvirus and calicivirus groups provide significant new data for understanding the evolution of the nodavirus family.

journal_name

J Virol

journal_title

Journal of virology

authors

Tang L,Lin CS,Krishna NK,Yeager M,Schneemann A,Johnson JE

doi

10.1128/jvi.76.12.6370-6375.2002

subject

Has Abstract

pub_date

2002-06-01 00:00:00

pages

6370-5

issue

12

eissn

0022-538X

issn

1098-5514

journal_volume

76

pub_type

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