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Harpins, such as HrpN ofErwinia amylovora , are extracellular glycine-rich proteins that elicit the hypersensitive reaction (HR). We identifiedhrpW ofE. amylovora , which encodes a protein similar to known harpins in that it is acidic, rich in glycine and serine, and lacks cysteine. A putative HrpL-dependent promoter was identified upstream ofhrpW , and Western blot analysis ofhrpL mutants indicated that the production of HrpW is regulated byhrpL . HrpW is secreted via the Hrp (type III) pathway based on analysis of wild-type strains andhrp secretion mutants. When infiltrated into plants, HrpW induced rapid tissue collapse, which required active plant metabolism. The HR-eliciting activity was heat stable and protease sensitive. Thus, we concluded that HrpW is a new harpin. HrpW ofE. amylovora consists of two domains connected by a Pro and Ser-rich sequence. A fragment containing the N-terminal domain was sufficient to elicit the HR. Although no pectate lyase activity was detected, the C-terminal region of HrpW is homologous to pectate lyases of a unique class, suggesting that HrpW may be targeted to the plant cell wall. Southern analysis indicated thathrpW is conserved among severalErwinia species, andhrpW , provided intrans , enhanced the HR-inducing ability of ahrpN mutant. However, HrpW did not increase the virulence of ahrpN mutant in host tissue, andhrpW mutants retained the wild-type ability to elicit the HR in nonhosts and to cause disease in hosts.

HrpW of Erwinia amylovora , a New Harpin That Contains a Domain Homologous to Pectate Lyases of a Distinct Class