Unraveling the Entry Mechanism of Oomycete and Fungal Effector Proteins into host cells

dc.contributor.authorKale, Shiv D.en
dc.contributor.authorRumore, A. C.en
dc.contributor.authorGU, B.en
dc.contributor.authorShan, C. B.en
dc.contributor.authorLawrence, D.en
dc.contributor.authorCapelluto, Daniel G. S.en
dc.contributor.authorTyler, B. M.en
dc.contributor.departmentBiological Sciencesen
dc.contributor.departmentFralin Life Sciences Instituteen
dc.coverage.spatialSt. Paul Minnesotaen
dc.date.accessioned2017-08-15T15:06:04Zen
dc.date.available2017-08-15T15:06:04Zen
dc.date.issued2015-11-30en
dc.description.abstractOomycetes and fungi facilitate pathogenesis via secretion of effector proteins that have apoplastic and intracellular localizations. These effector proteins have a diverse array of functions that aid in pathogenesis, including modification of defense responses. In the oomycetes, well characterized effector proteins that can translocate into the host cells share a pair of conserved N-terminal motifs known as RXLR and dEER. The RXLR motif has been shown to mediate translocation of the oomycete avirulence proteins Avr1b and Avr3a into host cells. Detailed mutagenesis of the RXLR motif of Avr1b revealed that the motif is tolerant to several amino acid substitutions while retaining functional translocation activity, resulting in the definition of a broadened RXLR-like motif, [R,K,H] X[L/M/I/F/Y/W]X. This motif has been used to identify functional translocation motifs in several fungal effector proteins, AvrL567, Avr2, and AvrLm6. Effectors with both RXLR and RXLR-like motifs bind phosphatidylinositol- 3-phosphate (PI-3-P) to mediate translocation via lipid raft mediated endocytosis. Mutations in RXLR or RXLRlike motifs result in loss of phospholipid binding and translocation by effectors. Effector entry into plant cells can be blocked by proteins and inositides that disrupt binding to PI-3-P, suggesting effector-blocking technologies that could be used in agriculturally important plant species.en
dc.description.notesBorlaug Global Rust Initiative Technical Workshopen
dc.description.notestrue (Invited?)en
dc.description.notesfalse (Extension publication?)en
dc.identifier.urihttp://hdl.handle.net/10919/78702en
dc.relation.urihttp://www.globalrust.org/content/unraveling-entry-mechanism-oomycete-and-fungal-effector-proteins-host-cellsen
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.titleUnraveling the Entry Mechanism of Oomycete and Fungal Effector Proteins into host cellsen
dc.typePresentationen
dc.type.otherWorkshopen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Biocomplexity Instituteen
pubs.organisational-group/Virginia Tech/University Research Institutes/Biocomplexity Institute/Researchersen

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