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- Title
Zn<sup>2+</sup>-dependent association of cysteine-rich protein with virion orchestrates morphogenesis of rod-shaped viruses.
- Authors
Yue, Ning; Jiang, Zhihao; Pi, Qinglin; Yang, Meng; Gao, Zongyu; Wang, Xueting; Zhang, He; Wu, Fengtong; Jin, Xuejiao; Li, Menglin; Wang, Ying; Zhang, Yongliang; Li, Dawei
- Abstract
The majority of rod-shaped and some filamentous plant viruses encode a cysteine-rich protein (CRP) that functions in viral virulence; however, the roles of these CRPs in viral infection remain largely unknown. Here, we used barley stripe mosaic virus (BSMV) as a model to investigate the essential role of its CRP in virus morphogenesis. The CRP protein γb directly interacts with BSMV coat protein (CP), the mutations either on the His-85 site in γb predicted to generate a potential CCCH motif or on the His-13 site in CP exposed to the surface of the virions abolish the zinc-binding activity and their interaction. Immunogold-labeling assays show that γb binds to the surface of rod-shaped BSMV virions in a Zn2+-dependent manner, which enhances the RNA binding activity of CP and facilitates virion assembly and stability, suggesting that the Zn2+-dependent physical association of γb with the virion is crucial for BSMV morphogenesis. Intriguingly, the tightly binding of diverse CRPs to their rod-shaped virions is a general feature employed by the members in the families Virgaviridae (excluding the genus Tobamovirus) and Benyviridae. Together, these results reveal a hitherto unknown role of CRPs in the assembly and stability of virus particles, and expand our understanding of the molecular mechanism underlying virus morphogenesis. Author summary: The symmetrical structures of plant RNA viruses are usually composed of numerous identical coat protein (CP) subunits encapsidated one molecule of viral genomic RNA. Interestingly, a large number of rod-shaped and filamentous plant viruses encode a cysteine-rich protein (CRP), which usually function as viral suppressors of RNA silencing and pathogenicity determinants during viral infection. However, their roles in viral life cycle remain poorly understood. Here, our study reveals the essential role of CRPs in virus morphogenesis. The cysteine-rich γb protein binds to the surface of rod-shaped barley stripe mosaic virus (BSMV) virion by interacting with CP in a Zn2+-dependent manner, thereby facilitating virion assembly and stability. Both His-85 site in γb predicted to generate a potential CCCH motif and His-13 site in CP exposed to the surface of the virions are key amino acids in γb-CP interaction and the zinc-binding activity. Attractively, the phenomenon of CRPs being tightly bound to their rod-shaped virions occurs in a broad range of distantly related viruses, implying a conserved role for the CRPs in orchestrating virus morphogenesis.
- Subjects
VIRION; LIFE cycles (Biology); MORPHOGENESIS; PLANT viruses; PLANT RNA; CUCUMBER mosaic virus
- Publication
PLoS Pathogens, 2024, Vol 20, Issue 6, p1
- ISSN
1553-7366
- Publication type
Article
- DOI
10.1371/journal.ppat.1012311