Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment

Abstract Virus-like particles are an emerging class of nano-biotechnology with the Tobacco Mosaic Virus (TMV) having found a wide range of applications in imaging, drug delivery, and vaccine development. TMV is typically produced in planta, and, as an RNA virus, is highly susceptible to natural muta...

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Autores principales:	Jenica L. Lumata, Darby Ball, Arezoo Shahrivarkevishahi, Michael A. Luzuriaga, Fabian C. Herbert, Olivia Brohlin, Hamilton Lee, Laurel M. Hagge, Sheena D’Arcy, Jeremiah J. Gassensmith
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d69d7ca991e7467d9ab0800e5535d8db
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spelling	oai:doaj.org-article:d69d7ca991e7467d9ab0800e5535d8db2021-12-02T16:26:38ZIdentification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment10.1038/s41598-021-94561-22045-2322https://doaj.org/article/d69d7ca991e7467d9ab0800e5535d8db2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-94561-2https://doaj.org/toc/2045-2322Abstract Virus-like particles are an emerging class of nano-biotechnology with the Tobacco Mosaic Virus (TMV) having found a wide range of applications in imaging, drug delivery, and vaccine development. TMV is typically produced in planta, and, as an RNA virus, is highly susceptible to natural mutation that may impact its properties. Over the course of 2 years, from 2018 until 2020, our laboratory followed a spontaneous point mutation in the TMV coat protein—first observed as a 30 Da difference in electrospray ionization mass spectrometry (ESI–MS). The mutation would have been difficult to notice by electrophoretic mobility in agarose or SDS-PAGE and does not alter viral morphology as assessed by transmission electron microscopy. The mutation responsible for the 30 Da difference between the wild-type (wTMV) and mutant (mTMV) coat proteins was identified by a bottom-up proteomic approach as a change from glycine to serine at position 155 based on collision-induced dissociation data. Since residue 155 is located on the outer surface of the TMV rod, it is feasible that the mutation alters TMV surface chemistry. However, enzyme-linked immunosorbent assays found no difference in binding between mTMV and wTMV. Functionalization of a nearby residue, tyrosine 139, with diazonium salt, also appears unaffected. Overall, this study highlights the necessity of standard workflows to quality-control viral stocks. We suggest that ESI–MS is a straightforward and low-cost way to identify emerging mutants in coat proteins.Jenica L. LumataDarby BallArezoo ShahrivarkevishahiMichael A. LuzuriagaFabian C. HerbertOlivia BrohlinHamilton LeeLaurel M. HaggeSheena D’ArcyJeremiah J. GassensmithNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jenica L. Lumata Darby Ball Arezoo Shahrivarkevishahi Michael A. Luzuriaga Fabian C. Herbert Olivia Brohlin Hamilton Lee Laurel M. Hagge Sheena D’Arcy Jeremiah J. Gassensmith Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
description	Abstract Virus-like particles are an emerging class of nano-biotechnology with the Tobacco Mosaic Virus (TMV) having found a wide range of applications in imaging, drug delivery, and vaccine development. TMV is typically produced in planta, and, as an RNA virus, is highly susceptible to natural mutation that may impact its properties. Over the course of 2 years, from 2018 until 2020, our laboratory followed a spontaneous point mutation in the TMV coat protein—first observed as a 30 Da difference in electrospray ionization mass spectrometry (ESI–MS). The mutation would have been difficult to notice by electrophoretic mobility in agarose or SDS-PAGE and does not alter viral morphology as assessed by transmission electron microscopy. The mutation responsible for the 30 Da difference between the wild-type (wTMV) and mutant (mTMV) coat proteins was identified by a bottom-up proteomic approach as a change from glycine to serine at position 155 based on collision-induced dissociation data. Since residue 155 is located on the outer surface of the TMV rod, it is feasible that the mutation alters TMV surface chemistry. However, enzyme-linked immunosorbent assays found no difference in binding between mTMV and wTMV. Functionalization of a nearby residue, tyrosine 139, with diazonium salt, also appears unaffected. Overall, this study highlights the necessity of standard workflows to quality-control viral stocks. We suggest that ESI–MS is a straightforward and low-cost way to identify emerging mutants in coat proteins.
format	article
author	Jenica L. Lumata Darby Ball Arezoo Shahrivarkevishahi Michael A. Luzuriaga Fabian C. Herbert Olivia Brohlin Hamilton Lee Laurel M. Hagge Sheena D’Arcy Jeremiah J. Gassensmith
author_facet	Jenica L. Lumata Darby Ball Arezoo Shahrivarkevishahi Michael A. Luzuriaga Fabian C. Herbert Olivia Brohlin Hamilton Lee Laurel M. Hagge Sheena D’Arcy Jeremiah J. Gassensmith
author_sort	Jenica L. Lumata
title	Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
title_short	Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
title_full	Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
title_fullStr	Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
title_full_unstemmed	Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
title_sort	identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/d69d7ca991e7467d9ab0800e5535d8db
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Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment

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