Structural lability of Barley stripe mosaic virus virions.
Virions of Barley stripe mosaic virus (BSMV) were neglected for more than thirty years after their basic properties were determined. In this paper, the physicochemical characteristics of BSMV virions and virion-derived viral capsid protein (CP) were analyzed, namely, the absorption and intrinsic flu...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3629216?pdf=render |
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| author | Valentin V Makarov Eugeny V Skurat Pavel I Semenyuk Dmitry A Abashkin Natalya O Kalinina Alexsandr M Arutyunyan Andrey G Solovyev Eugeny N Dobrov |
| author_facet | Valentin V Makarov Eugeny V Skurat Pavel I Semenyuk Dmitry A Abashkin Natalya O Kalinina Alexsandr M Arutyunyan Andrey G Solovyev Eugeny N Dobrov |
| author_sort | Valentin V Makarov |
| collection | DOAJ |
| description | Virions of Barley stripe mosaic virus (BSMV) were neglected for more than thirty years after their basic properties were determined. In this paper, the physicochemical characteristics of BSMV virions and virion-derived viral capsid protein (CP) were analyzed, namely, the absorption and intrinsic fluorescence spectra, circular dichroism spectra, differential scanning calorimetry curves, and size distributions by dynamic laser light scattering. The structural properties of BSMV virions proved to be intermediate between those of Tobacco mosaic virus (TMV), a well-characterized virus with rigid rod-shaped virions, and flexuous filamentous plant viruses. The BSMV virions were found to be considerably more labile than expected from their rod-like morphology and a distant sequence relation of the BSMV and TMV CPs. The circular dichroism spectra of BSMV CP subunits incorporated into the virions, but not subunits of free CP, demonstrated a significant proportion of beta-structure elements, which were proposed to be localized mostly in the protein regions exposed on the virion outer surface. These beta-structure elements likely formed during virion assembly can comprise the N- and C-terminal protein regions unstructured in the non-virion CP and can mediate inter-subunit interactions. Based on computer-assisted structure modeling, a model for BSMV CP subunit structural fold compliant with the available experimental data was proposed. |
| first_indexed | 2024-12-21T10:14:38Z |
| format | Article |
| id | doaj.art-0b91061c65844708a771f82597c74e5c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T10:14:38Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-0b91061c65844708a771f82597c74e5c2022-12-21T19:07:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0184e6094210.1371/journal.pone.0060942Structural lability of Barley stripe mosaic virus virions.Valentin V MakarovEugeny V SkuratPavel I SemenyukDmitry A AbashkinNatalya O KalininaAlexsandr M ArutyunyanAndrey G SolovyevEugeny N DobrovVirions of Barley stripe mosaic virus (BSMV) were neglected for more than thirty years after their basic properties were determined. In this paper, the physicochemical characteristics of BSMV virions and virion-derived viral capsid protein (CP) were analyzed, namely, the absorption and intrinsic fluorescence spectra, circular dichroism spectra, differential scanning calorimetry curves, and size distributions by dynamic laser light scattering. The structural properties of BSMV virions proved to be intermediate between those of Tobacco mosaic virus (TMV), a well-characterized virus with rigid rod-shaped virions, and flexuous filamentous plant viruses. The BSMV virions were found to be considerably more labile than expected from their rod-like morphology and a distant sequence relation of the BSMV and TMV CPs. The circular dichroism spectra of BSMV CP subunits incorporated into the virions, but not subunits of free CP, demonstrated a significant proportion of beta-structure elements, which were proposed to be localized mostly in the protein regions exposed on the virion outer surface. These beta-structure elements likely formed during virion assembly can comprise the N- and C-terminal protein regions unstructured in the non-virion CP and can mediate inter-subunit interactions. Based on computer-assisted structure modeling, a model for BSMV CP subunit structural fold compliant with the available experimental data was proposed.http://europepmc.org/articles/PMC3629216?pdf=render |
| spellingShingle | Valentin V Makarov Eugeny V Skurat Pavel I Semenyuk Dmitry A Abashkin Natalya O Kalinina Alexsandr M Arutyunyan Andrey G Solovyev Eugeny N Dobrov Structural lability of Barley stripe mosaic virus virions. PLoS ONE |
| title | Structural lability of Barley stripe mosaic virus virions. |
| title_full | Structural lability of Barley stripe mosaic virus virions. |
| title_fullStr | Structural lability of Barley stripe mosaic virus virions. |
| title_full_unstemmed | Structural lability of Barley stripe mosaic virus virions. |
| title_short | Structural lability of Barley stripe mosaic virus virions. |
| title_sort | structural lability of barley stripe mosaic virus virions |
| url | http://europepmc.org/articles/PMC3629216?pdf=render |
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