Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity

Laurence S. Boutemy, Stuart R. F. King, Joe Win, Richard K. Hughes, Thomas A. Clarke, Tharin M. A. Blumenschein, Sophien Kamoun, Mark J. Banfield

Research output: Contribution to journalArticlepeer-review

147 Citations (Scopus)
15 Downloads (Pure)

Abstract

Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing
Original languageEnglish
Pages (from-to)35834-35842
Number of pages9
JournalJournal of Biological Chemistry
Volume286
Issue number41
DOIs
Publication statusPublished - 14 Oct 2011

Cite this