Search

Begomovirus/betasatellite disease complex significantly threatens global crop production. Identifying potential plant antiviral genes is crucial for disease control. Nicotiana benthamiana is susceptible to viruses and contains 266 ethylene response transcription factors (ERFs). This study identified 29 NbERFs that were differentially upregulated in tobacco curly shoot virus and its associated betasatellite (TbCSV/TbCSB) infection, with ERF5 being the most common. Nine NbERF5s cluster phylogenetically and Niben101Scf00163g22002 (NbERF5) responds significantly to exogenous ACC treatment. Further analysis confirms the nuclear localization and transcriptional activation activity of NbERF5. Protein interaction assays demonstrate that NbERF5 has no self-interaction and does not interact with the βC1 protein of TbCSB. Silencing NbERF5 enhances TbCSV/TbCSB infection, and overexpression of NbERF5 inhibits TbCSV/TbCSB infection. Importantly, NbERF5 positively regulates the expression of the pathogenesis-related (PR) genes, NbPR1a and NbNPR1. Our findings suggest that NbERF5 enhances TbCSV/TbCSB resistance by activating the PR genes, indicating that NbERF5 is a potential antiviral gene., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Inc.)

Several of the structural proteins of phage P2 and its satellite P4 undergo proteolytic processing during development of mature phage particles. Here, we report that uncleaved shell protein, gpN, is present in immature capsids of both P2 and P4, showing that assembly precedes processing. This excludes the possibility that processing of gpN is involved in capsid size determination. We also find that N*, the fully processed version of gpN, produced from a plasmid, can assemble into both P2- and P4-sized particles, implying that the amino-terminal end of gpN is not required for assembly initiation nor for the formation of a T = 4 shell. As may be expected for a scaffolding protein, we find that gpO coexists with gpN in immature P2, as well as P4, capsids. This result supports the conclusion that gpO is required for both phages and strongly suggests that the O derivative, h7 (found in mature capsids), results from proteolytic cleavage after gpN/gpO coassembly.

The Psu (Polarity suppression) protein of satellite bacteriophage P4 was first characterized as an anti-terminator of transcription termination in Escherichia coli. Psu is also a structural component of mature P4 capsids, where it is present as a decoration protein. Psu is located externally on the capsid surface, and it appears to protect the capsid from loss of DNA through the capsid shell. The ability of Psu to specifically bind to the P4 capsid appears not to be dependent on any P4 specific components such as the capsid protein cleavage products h1 and h2, or P4 DNA. We suggest that Psu binds to the P4 capsid as a result of the special structure of the hexamers in the P4 capsid.