The oligomeric states of elicitins affect the hypersensitive response and resistance in tobacco

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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SOLANSKÝ Martin MIKULÁŠEK Kamil ZAPLETALOVÁ Martina PETŘIVALSKÝ Marek CHILTZ Annick ZDRÁHAL Zbyněk LEBORGNE-CASTEL Nathalie LOCHMAN Jan

Rok publikování 2021
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Experimental Botany
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www https://academic.oup.com/jxb/article/72/8/3219/6105174
Doi http://dx.doi.org/10.1093/jxb/erab011
Klíčová slova Cell wall; elicitin beta-CRY; ELICITIN RESPONSE; hypersensitive response; Nicotiana tabacum; oligomeric structure; Phytophthora; resistance; signalling; SUPPRESSOR OF BIR1-1 (SOBIR1); tobacco
Popis Successful plant defence against microbial pathogens is based on early recognition and fast activation of inducible responses. Key mechanisms include detection of microbe-associated molecular patterns by membrane-localized pattern recognition receptors that induce a basal resistance response. A well-described model of such responses to pathogens involves the interactions between Solanaceae plants and proteinaceous elicitors secreted by oomycetes, called elicitins. It has been hypothesized that the formation of oligomeric structures by elicitins could be involved in their recognition and activation of defensive transduction cascades. In this study, we tested this hypothesis using several approaches, and we observed differences in tobacco plant responses induced by the elicitin beta-cryptogein (beta-CRY) and its homodimer, beta-CRYDIM. We also found that the C-terminal domain of elicitins of other ELI (true-elicitin) clades plays a significant role in stabilization of their oligomeric structure and restraint in the cell wall. In addition, covalently cross-linking beta-CRYDIM impaired the formation of signalling complexes, thereby reducing its capacity to elicit the hypersensitive response and resistance in the host plant, with no significant changes in pathogenesis-related protein expression. By revealing the details of the effects of beta-CRY dimerization on recognition and defence responses in tobacco, our results shed light on the poorly understood role of elicitins' oligomeric structures in the interactions between oomycetes and plants.
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