Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures

Abstract Nervous necrosis virus (NNV) is a pathogenic fish virus belonging to family Nodaviridae. The objective of this study was to analyze stabilities of NNV surface protrusion and free coat protein (CP) conformational structures by analyzing changes of NNV infectivity and antigenicity after incub...

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Autores principales:	Hyun Jung Gye, Toyohiko Nishizawa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/33faaa16d8ec4c0c845bfa5df244d48d
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spelling	oai:doaj.org-article:33faaa16d8ec4c0c845bfa5df244d48d2021-12-02T15:08:59ZAltered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures10.1038/s41598-019-45094-22045-2322https://doaj.org/article/33faaa16d8ec4c0c845bfa5df244d48d2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-45094-2https://doaj.org/toc/2045-2322Abstract Nervous necrosis virus (NNV) is a pathogenic fish virus belonging to family Nodaviridae. The objective of this study was to analyze stabilities of NNV surface protrusion and free coat protein (CP) conformational structures by analyzing changes of NNV infectivity and antigenicity after incubation at moderate-low temperatures. When cultured NNV suspension was incubated at 45 °C, its infectivity declined gradually but its antigenicity maintained. In contrast, both infectivity and antigenicity of purified NNV declined after incubation at 45 °C. After heat-treatment, surface protrusions of NNV particles disappeared completely, although viral particle structures maintained. Therefore, the reduction in NNV infectivity appeared to specifically occur as a result of heat-denaturation of virus surface protrusions. The loss of NNV infectivity in the presence of fetal bovine serum (FBS) was delayed compared to virus heated in the absence of FBS, demonstrating that FBS could function as a stabilizer for conformational structures of NNV surface protrusions. Moreover, the stabilizing function of FBS changed depending on salt concentration. Continued maintenance of antigenicity for heated cultured NNV suspension containing free-CPs may suggest that conformational structures corresponding to protrusion-domain of free-CP are more heat-stable than those of surface protrusions on NNV particles.Hyun Jung GyeToyohiko NishizawaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hyun Jung Gye Toyohiko Nishizawa Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
description	Abstract Nervous necrosis virus (NNV) is a pathogenic fish virus belonging to family Nodaviridae. The objective of this study was to analyze stabilities of NNV surface protrusion and free coat protein (CP) conformational structures by analyzing changes of NNV infectivity and antigenicity after incubation at moderate-low temperatures. When cultured NNV suspension was incubated at 45 °C, its infectivity declined gradually but its antigenicity maintained. In contrast, both infectivity and antigenicity of purified NNV declined after incubation at 45 °C. After heat-treatment, surface protrusions of NNV particles disappeared completely, although viral particle structures maintained. Therefore, the reduction in NNV infectivity appeared to specifically occur as a result of heat-denaturation of virus surface protrusions. The loss of NNV infectivity in the presence of fetal bovine serum (FBS) was delayed compared to virus heated in the absence of FBS, demonstrating that FBS could function as a stabilizer for conformational structures of NNV surface protrusions. Moreover, the stabilizing function of FBS changed depending on salt concentration. Continued maintenance of antigenicity for heated cultured NNV suspension containing free-CPs may suggest that conformational structures corresponding to protrusion-domain of free-CP are more heat-stable than those of surface protrusions on NNV particles.
format	article
author	Hyun Jung Gye Toyohiko Nishizawa
author_facet	Hyun Jung Gye Toyohiko Nishizawa
author_sort	Hyun Jung Gye
title	Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
title_short	Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
title_full	Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
title_fullStr	Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
title_full_unstemmed	Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
title_sort	altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/33faaa16d8ec4c0c845bfa5df244d48d
work_keys_str_mv	AT hyunjunggye alteredconformationalstructuresofnervousnecrosisvirussurfaceprotrusionsandfreecoatproteinsafterincubationatmoderatelowtemperatures AT toyohikonishizawa alteredconformationalstructuresofnervousnecrosisvirussurfaceprotrusionsandfreecoatproteinsafterincubationatmoderatelowtemperatures
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Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures

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