Tobacco Necrosis Virus-AC Single Coat Protein Amino Acid Substitutions Determine Host-Specific Systemic Infections of Nicotiana benthamiana and Soybean
| Autor: | Heng Pu, Xian-Bing Wang, Xiaoling Wang, Jialin Yu, Ning Yue, Jingyuan Liu, Zongyu Gao, Chenchen Zhong, Cheng-Gui Han, Ziding Zhang, Dawei Li, Yongliang Zhang |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
food.ingredient Physiology viruses Nicotiana benthamiana 01 natural sciences Microbiology 03 medical and health sciences Tobacco necrosis virus food Plant virus Alphanecrovirus 030304 developmental biology Infectivity 0303 health sciences biology fungi Botany RNA food and beverages General Medicine biology.organism_classification Virology QR1-502 Tombusviridae Virion assembly QK1-989 Agronomy and Crop Science 010606 plant biology & botany |
| Zdroj: | Molecular Plant-Microbe Interactions, Vol 34, Iss 1, Pp 49-61 (2021) |
| ISSN: | 1943-7706 0894-0282 |
| Popis: | Plant viruses often infect several distinct host species. Sometimes, viruses can systemically infect a specific host whereas, in other cases, only local infections occur in other species. How viral and host factors interact to determine systemic infections among different hosts is largely unknown, particularly for icosahedral positive-stranded RNA viruses. The Tobacco necrosis virus-A Chinese isolate belongs to the genus Alphanecrovirus in the family Tombusviridae. In this study, we investigated variations in systemic infections of tobacco necrosis virus-AC (TNV-AC) in Nicotiana benthamiana and Glycine max (soybean) by alanine-scanning mutagenesis of the viral coat protein (CP), which is essential for systemic movement of TNV-AC. We found that three amino acids, R169, K177, and Q233, are key residues that mediate varying degrees of systemic infections of N. benthamiana and soybean. Further analysis revealed that variations in systemic trafficking of TNV-AC CP mutants in N. benthamiana and soybean are associated with virion assembly and stability. The CP amino acids K177 and Q233 are highly conserved among all TNV-A isolates and are replaced by Q and K in the TNV-D isolates. We demonstrated that systemic infectivity of either TNV-AC K177A and Q233A or K177Q and Q233K mutants are correlated with the binding affinity of the mutated CPs to the host-specific Hsc70-2 protein. These results expand our understanding of host-dependent long-distance movement of icosahedral viruses in plants. [Formula: see text] Copyright © 2021 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license . |
| Databáze: | OpenAIRE |
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