{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T19:30:22Z","timestamp":1787167822365,"version":"build-2736575974"},"reference-count":77,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2021,10,6]],"date-time":"2021-10-06T00:00:00Z","timestamp":1633478400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["bsppjournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Plant Pathology"],"published-print":{"date-parts":[[2022,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Asparagine synthetase is a key enzyme that catalyses the conversion of amide groups from glutamine or ammonium to aspartate, which leads to the generation of asparagine. However, the role of asparagine synthetase in plant immunity remains largely unknown. Here, we identified a\n                    <jats:italic>Nicotiana benthamiana<\/jats:italic>\n                    asparagine synthetase B (NbAS\u2010B) that associates with tomato mosaic virus coat protein\u2010interacting protein L (IP\u2010L) using the yeast two\u2010hybrid assay and examined its role in tobacco mosaic virus (TMV) resistance. The association of IP\u2010L with NbAS\u2010B was further confirmed by in vivo co\u2010immunoprecipitation, luciferase complementation imaging, and bimolecular fluorescence complementation assays. IP\u2010L and NbAS\u2010B interact in the nucleus and cytosol and IP\u2010L apparently stabilizes NbAS\u2010B, thus enhancing its accumulation. The expressions of\n                    <jats:italic>IP\u2010L<\/jats:italic>\n                    and\n                    <jats:italic>NbAS\u2010B<\/jats:italic>\n                    are continuously induced on TMV\u2010green fluorescent protein (GFP) infection. Co\u2010silencing of\n                    <jats:italic>IP\u2010L<\/jats:italic>\n                    and\n                    <jats:italic>NbAS\u2010B<\/jats:italic>\n                    facilitates TMV\u2010GFP infection. Overexpression of\n                    <jats:italic>NbAS\u2010B<\/jats:italic>\n                    in tobacco reduces TMV\u2010GFP infection by significantly improving the synthesis of asparagine. Furthermore, the external application of asparagine significantly inhibits the infection of TMV\u2010GFP by activating the salicylic acid signalling pathway. These findings hold the potential for the future application of asparagine in the control of TMV.\n                  <\/jats:p>","DOI":"10.1111\/mpp.13143","type":"journal-article","created":{"date-parts":[[2021,10,8]],"date-time":"2021-10-08T20:27:49Z","timestamp":1633724869000},"page":"60-77","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["<i>Nicotiana benthamiana<\/i>\n                    asparagine synthetase associates with IP\u2010L and confers resistance against tobacco mosaic virus via the asparagine\u2010induced salicylic acid signalling pathway"],"prefix":"10.1111","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1683-5101","authenticated-orcid":false,"given":"Changyun","family":"Liu","sequence":"first","affiliation":[{"name":"College of Plant Protection Southwest University Chongqing 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