The 2.3-angstrom structure of porcine circovirus 2.

Abstract:

:Porcine circovirus 2 (PCV2) is a T=1 nonenveloped icosahedral virus that has had severe impact on the swine industry. Here we report the crystal structure of an N-terminally truncated PCV2 virus-like particle at 2.3-Å resolution, and the cryo-electron microscopy (cryo-EM) image reconstruction of a full-length PCV2 virus-like particle at 9.6-Å resolution. This is the first atomic structure of a circovirus. The crystal structure revealed that the capsid protein fold is a canonical viral jelly roll. The loops connecting the strands of the jelly roll define the limited features of the surface. Sulfate ions interacting with the surface and electrostatic potential calculations strongly suggest a heparan sulfate binding site that allows PCV2 to gain entry into the cell. The crystal structure also allowed previously determined epitopes of the capsid to be visualized. The cryo-EM image reconstruction showed that the location of the N terminus, absent in the crystal structure, is inside the capsid. As the N terminus was previously shown to be antigenic, it may externalize through viral "breathing."

journal_name

J Virol

journal_title

Journal of virology

authors

Khayat R,Brunn N,Speir JA,Hardham JM,Ankenbauer RG,Schneemann A,Johnson JE

doi

10.1128/JVI.00737-11

subject

Has Abstract

pub_date

2011-08-01 00:00:00

pages

7856-62

issue

15

eissn

0022-538X

issn

1098-5514

pii

JVI.00737-11

journal_volume

85

pub_type

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