A1 Journal article (refereed)
Parvovirus nonstructural protein 2 interacts with chromatin-regulating cellular proteins (2022)


Mattola, S., Salokas, K., Aho, V., Mäntylä, E., Salminen, S., Hakanen, S., Niskanen, E. A., Svirskaite, J., Ihalainen, T. O., Airenne, K. J., Kaikkonen-Määttä, M., Parrish, C. R., Varjosalo, M., & Vihinen-Ranta, M. (2022). Parvovirus nonstructural protein 2 interacts with chromatin-regulating cellular proteins. PLoS Pathogens, 18(4), Article e1010353. https://doi.org/10.1371/journal.ppat.1010353


JYU authors or editors


Publication details

All authors or editorsMattola, Salla; Salokas, Kari; Aho, Vesa; Mäntylä, Elina; Salminen, Sami; Hakanen, Satu; Niskanen, Einari A.; Svirskaite, Julija; Ihalainen, Teemu O.; Airenne, Kari J.; et al.

Journal or seriesPLoS Pathogens

ISSN1553-7366

eISSN1553-7374

Publication year2022

Publication date08/04/2022

Volume18

Issue number4

Article numbere1010353

PublisherPublic Library of Science (PLoS)

Publication countryUnited States

Publication languageEnglish

DOIhttps://doi.org/10.1371/journal.ppat.1010353

Publication open accessOpenly available

Publication channel open accessOpen Access channel

Publication is parallel published (JYX)https://jyx.jyu.fi/handle/123456789/81225


Abstract

Autonomous parvoviruses encode at least two nonstructural proteins, NS1 and NS2. While NS1 is linked to important nuclear processes required for viral replication, much less is known about the role of NS2. Specifically, the function of canine parvovirus (CPV) NS2 has remained undefined. Here we have used proximity-dependent biotin identification (BioID) to screen for nuclear proteins that associate with CPV NS2. Many of these associations were seen both in noninfected and infected cells, however, the major type of interacting proteins shifted from nuclear envelope proteins to chromatin-associated proteins in infected cells. BioID interactions revealed a potential role for NS2 in DNA remodeling and damage response. Studies of mutant viral genomes with truncated forms of the NS2 protein suggested a change in host chromatin accessibility. Moreover, further studies with NS2 mutants indicated that NS2 performs functions that affect the quantity and distribution of proteins linked to DNA damage response. Notably, mutation in the splice donor site of the NS2 led to a preferred formation of small viral replication center foci instead of the large coalescent centers seen in wild-type infection. Collectively, our results provide insights into potential roles of CPV NS2 in controlling chromatin remodeling and DNA damage response during parvoviral replication.


Keywordsparvovirusesinfectionsproteins

Free keywordsparvoviruses; cellular proteins


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Ministry reportingYes

Reporting Year2022

JUFO rating2


Last updated on 2024-03-04 at 18:36