SMART accession number:SM01187
Description: Elicitins form a novel class of plant necrotic proteins which are secreted by Phytophthora and Pythium fungi, parasites of many economically important crops. These proteins induce leaf necrosis in infected plants and elicit an incompatible hypersensitive-like reaction, leading to the development of a systemic acquired resistance against a range of fungal and bacterial plant pathogens (PUBMED:8994969).
Interpro abstract (IPR002200):

Elicitins are small, highly-conserved proteins secreted by phytopathogenic fungi belonging to the phytophthora species [ (PUBMED:7753775) ]. They are toxic proteins reponsible for inducing a necrotic and systemic hypersensitive response in plants from the solanaceae and cruciferae families. Leaf necrosis provides immediate control of fungal invasion and induces systemic acquired resistance; both responses mediate basic protection against subsequent pathogen inoculation.

Members of this family share a high level of sequence similarity, but they differ in net charge, dividing them into two classes: alpha and beta [ (PUBMED:7753775) (PUBMED:24186785) ]. Alpha-elicitins are highly acidic, with a valine residue at position 13, whereas beta-elicitins are basic, with a lysine at the same position. Residue 13 is known to be involved in the control of necrosis and, being exposed, is thought to be involved in ligand/receptor binding [ (PUBMED:24186785) (PUBMED:9385630) ]. Phenotypically, the two classes can be distinguished by their necrotic properties: beta-elicitins are 100-fold more toxic and provide better subsequent protection [ (PUBMED:7753775) ].

GO process:pathogenesis (GO:0009405)
GO component:extracellular region (GO:0005576)
Family alignment:
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There are 740 Elicitin domains in 634 proteins in SMART's nrdb database.

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