VPg unlinkase/TDP2 in cardiovirus infected cells: Re-localization and proteolytic cleavage.

Abstract:

:Cardioviruses cause diseases in many animals including, in rare cases, humans. Although they share common features with all picornaviruses, cardioviruses have unique properties that distinguish them from other family members, including enteroviruses. One feature shared by all picornaviruses is the covalent attachment of VPg to the 5' end of genomic RNA via a phosphotyrosyl linkage. For enteroviruses, this linkage is cleaved by a host cell protein, TDP2. Since TDP2 is divergently required during enterovirus infections, we determined if TDP2 is necessary during infection by the prototype cardiovirus, EMCV. We found that EMCV yields are reduced in the absence of TDP2. We observed a decrease in viral protein accumulation and viral RNA replication in the absence of TDP2. In contrast to enterovirus infections, we found that TDP2 is modified at peak times of EMCV infection. This finding suggests a unique mechanism for cardioviruses to regulate TDP2 activity during infection.

journal_name

Virology

journal_title

Virology

authors

Maciejewski S,Ullmer W,Semler BL

doi

10.1016/j.virol.2018.01.010

subject

Has Abstract

pub_date

2018-03-01 00:00:00

pages

139-146

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(18)30010-2

journal_volume

516

pub_type

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