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

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...

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Autores principales: Gye, Hyun Jung, Nishizawa, Toyohiko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6573060/
https://www.ncbi.nlm.nih.gov/pubmed/31201359
http://dx.doi.org/10.1038/s41598-019-45094-2
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author Gye, Hyun Jung
Nishizawa, Toyohiko
author_facet Gye, Hyun Jung
Nishizawa, Toyohiko
author_sort Gye, Hyun Jung
collection PubMed
description 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.
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spelling pubmed-65730602019-06-24 Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures Gye, Hyun Jung Nishizawa, Toyohiko Sci Rep Article 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. Nature Publishing Group UK 2019-06-14 /pmc/articles/PMC6573060/ /pubmed/31201359 http://dx.doi.org/10.1038/s41598-019-45094-2 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Gye, Hyun Jung
Nishizawa, Toyohiko
Altered conformational structures of nervous necrosis virus surface protrusions and free coat proteins after incubation at moderate-low temperatures
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6573060/
https://www.ncbi.nlm.nih.gov/pubmed/31201359
http://dx.doi.org/10.1038/s41598-019-45094-2
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