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A recombinant flagellin fragment, which includes the epitopes flg22 and flgII-28, provides a useful tool to study flagellin-triggered immunity
- Ciarroni, Serena, Clarke, ChristopherR., Liu, Haijie, Eckshtain-Levi, Noam, Mazzaglia, Angelo, Balestra, GiorgioM., Vinatzer, BorisA.
- Journal of general plant pathology 2018 v.84 no.3 pp. 169-175
- Actinidia arguta, Arabidopsis thaliana, Pseudomonas syringae, amino acids, animals, epitopes, flagellin, flagellum, gene overexpression, innate immunity, kiwifruit, leaves, oxygen, plants (botany)
- Plants and animals independently evolved the ability to recognize flagellin (also called FliC), the building block of the bacterial flagellum, as part of their innate immune response. While animals recognize a relatively large region of FliC, most plants recognize one or two short epitopes of FliC: flg22 and flgII-28. However, since most research in plants has focused on flg22 and flgII-28 and not the actual FliC protein, the importance of any FliC region beyond the two epitopes in plant immunity is poorly understood. Here we report cloning, overexpression, and purification of a Pseudomonas syringae FliC fragment from amino acid 1 to 143, which includes both FliC epitopes and the adjacent alpha helices. Exposing Arabidopsis thaliana leaves to FliC₁–₁₄₃ did not reveal any additional FliC recognition capabilities beyond flg22. However, while the kiwifruit species Actinidia arguta did not respond to either flg22 or flgII-28, treatment of A. arguta leaves with FliC₁–₁₄₃ triggered a significant reactive oxygen response, indicating recognition. This result suggests that in some plant species, recognition of FliC requires regions of FliC beyond the two well-known epitopes and that FliC₁–₁₄₃ represents a useful tool in the study of plant immunity.