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Virology. 2014 Nov;468-470:226-237. doi: 10.1016/j.virol.2014.07.043. Epub 2014 Sep 6.

Complementation for an essential ancillary non-structural protein function across parvovirus genera.

Author information

1
Department of Laboratory Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
2
Department of Laboratory Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA; Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA. Electronic address: peter.tattersall@yale.edu.

Abstract

Parvoviruses encode a small number of ancillary proteins that differ substantially between genera. Within the genus Protoparvovirus, minute virus of mice (MVM) encodes three isoforms of its ancillary protein NS2, while human bocavirus 1 (HBoV1), in the genus Bocaparvovirus, encodes an NP1 protein that is unrelated in primary sequence to MVM NS2. To search for functional overlap between NS2 and NP1, we generated murine A9 cell populations that inducibly express HBoV1 NP1. These were used to test whether NP1 expression could complement specific defects resulting from depletion of MVM NS2 isoforms. NP1 induction had little impact on cell viability or cell cycle progression in uninfected cells, and was unable to complement late defects in MVM virion production associated with low NS2 levels. However, NP1 did relocate to MVM replication centers, and supports both the normal expansion of these foci and overcomes the early paralysis of DNA replication in NS2-null infections.

KEYWORDS:

DNA replication block; Functional complementation; Human bocavirus 1 (HBoV1); Minute virus of mice (MVM); NP1; NS2; Non-structural proteins; Parvovirus

PMID:
25194919
PMCID:
PMC4254310
DOI:
10.1016/j.virol.2014.07.043
[Indexed for MEDLINE]
Free PMC Article

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