Identification of the potential matrix protein of invertebrate iridescent virus 6 (IIV6).

Autor: Gencer D; Department of Property Protection and Security, Trabzon University, Trabzon, Turkey., Yesilyurt A; Department of Medical Services and Techniques, Trabzon University, Trabzon, Turkey., Ozsahin E; Department of Molecular and Cellular Biology, University of Guelph, Ontario, Canada., Muratoglu H; Department of Molecular Biology and Genetics, Karadeniz Technical University, Trabzon, Turkey., Acar Yazici Z; Clinical Microbiology Department, Recep Tayyip Erdogan University, Rize, Turkey., Demirbag Z; Department of Biology, Karadeniz Technical University, Trabzon, Turkey., Nalcacioglu R; Department of Biology, Karadeniz Technical University, Trabzon, Turkey. Electronic address: remziye@ktu.edu.tr.
Jazyk: angličtina
Zdroj: Journal of invertebrate pathology [J Invertebr Pathol] 2023 Mar; Vol. 197, pp. 107885. Date of Electronic Publication: 2023 Jan 11.
DOI: 10.1016/j.jip.2023.107885
Abstrakt: Invertebrate iridescent virus 6 (IIV6) is a nucleocytoplasmic virus with a ∼212 kb linear dsDNA genome that encodes 215 putative open reading frames (ORFs). Proteomic analysis has revealed that the IIV6 virion consists of 54 virally encoded proteins. Interactions among the structural proteins were investigated using the yeast two-hybrid system, revealing that the protein of 415R ORF interacts reciprocally with the potential envelope protein 118L and the major capsid protein 274L. This result suggests that 415R might be a matrix protein that plays a role as a bridge between the capsid and the envelope proteins. To elucidate the function of 415R protein, we determined the localization of 415R in IIV6 structure and analyzed the properties of 415R-silenced IIV6. Specific antibodies produced against 415R protein were used to determine the location of the 415R protein in the virion structure. Both western blot hybridization and immunogold electron microscopy analyses showed that the 415R protein was found in virions treated with Triton X-100, which degrades the viral envelope. The 415R gene was silenced by the RNA interference (RNAi) technique. We used gene-specific dsRNA's to target 415R and showed that this treatment resulted in a significant drop in virus titer. Silencing 415R with dsRNA also reduced the transcription levels of other viral genes. These results provide important data on the role and location of IIV6 415R protein in the virion structure. Additionally, these results may also shed light on the identification of the homologs of 415R among the vertebrate iridoviruses.
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 © 2023 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: