Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus

Abstract White spot syndrome virus (WSSV) is one of the most devastating pathogens in penaeid shrimp and can cause massive damage in shrimp aquaculture industries. Previously, the WSSV structural protein VP15 was identified as an antigenic reagent against WSSV infections. In this study, we truncated...

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Autores principales:	Jirayu Boonyakida, Jian Xu, Jun Satoh, Takafumi Nakanishi, Tohru Mekata, Tatsuya Kato, Enoch Y. Park
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/55318a81648e4186979ba8cfc7dd9698
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spelling	oai:doaj.org-article:55318a81648e4186979ba8cfc7dd96982021-12-02T17:39:53ZIdentification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus10.1038/s41598-021-92002-82045-2322https://doaj.org/article/55318a81648e4186979ba8cfc7dd96982021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-92002-8https://doaj.org/toc/2045-2322Abstract White spot syndrome virus (WSSV) is one of the most devastating pathogens in penaeid shrimp and can cause massive damage in shrimp aquaculture industries. Previously, the WSSV structural protein VP15 was identified as an antigenic reagent against WSSV infections. In this study, we truncated this protein into VP15(1–25), VP15(26–57), VP15(58–80), and VP15(1–25,58–80). The purified proteins from the E. coli expression system were assayed as potential protective agents in Kuruma shrimp (Marsupenaeus japonicus) using the prime-and-boost strategy. Among the four truncated constructs, VP15(26–57) provided a significant improvement in the shrimp survival rate after 20 days of viral infection. Subsequently, four peptides (KR11, SR11, SK10, and KK13) from VP15(26–57) were synthesized and applied in an in vivo assay. Our results showed that SR11 could significantly enhance the shrimp survival rate, as determined from the accumulated survival rate. Moreover, a multiligand binding protein with a role in the host immune response and a possible VP15-binding partner, MjgC1qR, from the host M. japonicus were employed to test its binding with the VP15 protein. GST pull-down assays revealed that MjgC1qR binds with VP15, VP15(26–57), and SR11. Taken together, we conclude that SR11 is a determinant antigenic peptide of VP15 conferring antiviral activity against WSSV.Jirayu BoonyakidaJian XuJun SatohTakafumi NakanishiTohru MekataTatsuya KatoEnoch Y. ParkNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jirayu Boonyakida Jian Xu Jun Satoh Takafumi Nakanishi Tohru Mekata Tatsuya Kato Enoch Y. Park Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus
description	Abstract White spot syndrome virus (WSSV) is one of the most devastating pathogens in penaeid shrimp and can cause massive damage in shrimp aquaculture industries. Previously, the WSSV structural protein VP15 was identified as an antigenic reagent against WSSV infections. In this study, we truncated this protein into VP15(1–25), VP15(26–57), VP15(58–80), and VP15(1–25,58–80). The purified proteins from the E. coli expression system were assayed as potential protective agents in Kuruma shrimp (Marsupenaeus japonicus) using the prime-and-boost strategy. Among the four truncated constructs, VP15(26–57) provided a significant improvement in the shrimp survival rate after 20 days of viral infection. Subsequently, four peptides (KR11, SR11, SK10, and KK13) from VP15(26–57) were synthesized and applied in an in vivo assay. Our results showed that SR11 could significantly enhance the shrimp survival rate, as determined from the accumulated survival rate. Moreover, a multiligand binding protein with a role in the host immune response and a possible VP15-binding partner, MjgC1qR, from the host M. japonicus were employed to test its binding with the VP15 protein. GST pull-down assays revealed that MjgC1qR binds with VP15, VP15(26–57), and SR11. Taken together, we conclude that SR11 is a determinant antigenic peptide of VP15 conferring antiviral activity against WSSV.
format	article
author	Jirayu Boonyakida Jian Xu Jun Satoh Takafumi Nakanishi Tohru Mekata Tatsuya Kato Enoch Y. Park
author_facet	Jirayu Boonyakida Jian Xu Jun Satoh Takafumi Nakanishi Tohru Mekata Tatsuya Kato Enoch Y. Park
author_sort	Jirayu Boonyakida
title	Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus
title_short	Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus
title_full	Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus
title_fullStr	Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus
title_full_unstemmed	Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus
title_sort	identification of antigenic domains and peptides from vp15 of white spot syndrome virus and their antiviral effects in marsupenaeus japonicus
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/55318a81648e4186979ba8cfc7dd9698
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Identification of antigenic domains and peptides from VP15 of white spot syndrome virus and their antiviral effects in Marsupenaeus japonicus

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