Hsc70-2 is required for Beet black scorch virus infection through interaction with replication and capsid proteins.

Abstract:

:Dissecting the complex molecular interplay between the host plant and invading virus improves our understanding of the mechanisms underlying viral pathogenesis. In this study, immunoprecipitation together with the mass spectrometry analysis revealed that the heat shock protein 70 (Hsp70) family homolog, Hsc70-2, was co-purified with beet black scorch virus (BBSV) replication protein p23 and coat protein (CP), respectively. Further experiments demonstrated that Hsc70-2 interacts directly with both p23 and CP, whereas there is no interaction between p23 and CP. Hsc70-2 expression is induced slightly during BBSV infection of Nicotiana benthamiana, and overexpression of Hsc70-2 promotes BBSV accumulation, while knockdown of Hsc70-2 in N. benthamiana leads to drastic reduction of BBSV accumulation. Infection experiments revealed that CP negatively regulates BBSV replication, which can be mitigated by overexpression of Hsc70-2. Further experiments indicate that CP impairs the interaction between Hsc70-2 and p23 in a dose-dependent manner. Altogether, we provide evidence that besides specific functions of Hsp70 family proteins in certain aspects of viral infection, they can serve as a mediator for the orchestration of virus infection by interacting with different viral components. Our results provide new insight into the role of Hsp70 family proteins in virus infection.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Wang X,Cao X,Liu M,Zhang R,Zhang X,Gao Z,Zhao X,Xu K,Li D,Zhang Y

doi

10.1038/s41598-018-22778-9

subject

Has Abstract

pub_date

2018-03-14 00:00:00

pages

4526

issue

1

issn

2045-2322

pii

10.1038/s41598-018-22778-9

journal_volume

8

pub_type

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