Hong Lu, Panpan Ge, Yonghuan Ma, Feng Lin, Dedao Jing, Tong Zhou, Feng Cui
{"title":"两个pd相关蛋白的功能缺失赋予水稻条纹病毒抗性。","authors":"Hong Lu, Panpan Ge, Yonghuan Ma, Feng Lin, Dedao Jing, Tong Zhou, Feng Cui","doi":"10.1111/mpp.70121","DOIUrl":null,"url":null,"abstract":"<p><p>Plant viruses usually exploit plasmodesmata (PDs) to achieve cellular infection in host plants. Although PD-associated proteins are commonly implicated in the regulation of PD pore size, a few limited cases demonstrate their roles as viral targets suitable for resistance breeding. Here we screened the importin α protein family of rice to identify the PD-associated members and explored their effects on the infection of rice stripe virus (RSV), one of the most notorious pathogens threatening rice yields. Both Importin α1b and α4 were found to be localised on the plasma membrane and PD. Only importin α4 knockout mutant rice exhibited resistance to RSV infection while the role of importin α1b in RSV infection was negligible. The absence of importin α4 enhanced callose deposition at PDs, which impeded viral intercellular movement. Flotillin 1 is another PD-associated protein in rice and was previously reported to facilitate RSV infection. When flotillin1 and importin α4 were simultaneously knocked out, the double-knockout mutant exhibited a synergically higher resistance level to RSV not only in the greenhouse but also in natural fields without affecting agronomic traits. This study proposed the potential of the two PD-associated proteins as targets for engineering virus resistance in future.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"26 7","pages":"e70121"},"PeriodicalIF":4.8000,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12227655/pdf/","citationCount":"0","resultStr":"{\"title\":\"Loss-of-Function of Two PD-Associated Proteins Confers Resistance to Rice Stripe Virus.\",\"authors\":\"Hong Lu, Panpan Ge, Yonghuan Ma, Feng Lin, Dedao Jing, Tong Zhou, Feng Cui\",\"doi\":\"10.1111/mpp.70121\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Plant viruses usually exploit plasmodesmata (PDs) to achieve cellular infection in host plants. Although PD-associated proteins are commonly implicated in the regulation of PD pore size, a few limited cases demonstrate their roles as viral targets suitable for resistance breeding. Here we screened the importin α protein family of rice to identify the PD-associated members and explored their effects on the infection of rice stripe virus (RSV), one of the most notorious pathogens threatening rice yields. Both Importin α1b and α4 were found to be localised on the plasma membrane and PD. Only importin α4 knockout mutant rice exhibited resistance to RSV infection while the role of importin α1b in RSV infection was negligible. The absence of importin α4 enhanced callose deposition at PDs, which impeded viral intercellular movement. Flotillin 1 is another PD-associated protein in rice and was previously reported to facilitate RSV infection. When flotillin1 and importin α4 were simultaneously knocked out, the double-knockout mutant exhibited a synergically higher resistance level to RSV not only in the greenhouse but also in natural fields without affecting agronomic traits. This study proposed the potential of the two PD-associated proteins as targets for engineering virus resistance in future.</p>\",\"PeriodicalId\":18763,\"journal\":{\"name\":\"Molecular plant pathology\",\"volume\":\"26 7\",\"pages\":\"e70121\"},\"PeriodicalIF\":4.8000,\"publicationDate\":\"2025-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12227655/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular plant pathology\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1111/mpp.70121\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PLANT SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular plant pathology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1111/mpp.70121","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
Loss-of-Function of Two PD-Associated Proteins Confers Resistance to Rice Stripe Virus.
Plant viruses usually exploit plasmodesmata (PDs) to achieve cellular infection in host plants. Although PD-associated proteins are commonly implicated in the regulation of PD pore size, a few limited cases demonstrate their roles as viral targets suitable for resistance breeding. Here we screened the importin α protein family of rice to identify the PD-associated members and explored their effects on the infection of rice stripe virus (RSV), one of the most notorious pathogens threatening rice yields. Both Importin α1b and α4 were found to be localised on the plasma membrane and PD. Only importin α4 knockout mutant rice exhibited resistance to RSV infection while the role of importin α1b in RSV infection was negligible. The absence of importin α4 enhanced callose deposition at PDs, which impeded viral intercellular movement. Flotillin 1 is another PD-associated protein in rice and was previously reported to facilitate RSV infection. When flotillin1 and importin α4 were simultaneously knocked out, the double-knockout mutant exhibited a synergically higher resistance level to RSV not only in the greenhouse but also in natural fields without affecting agronomic traits. This study proposed the potential of the two PD-associated proteins as targets for engineering virus resistance in future.
期刊介绍:
Molecular Plant Pathology is now an open access journal. Authors pay an article processing charge to publish in the journal and all articles will be freely available to anyone. BSPP members will be granted a 20% discount on article charges. The Editorial focus and policy of the journal has not be changed and the editorial team will continue to apply the same rigorous standards of peer review and acceptance criteria.