A positive‐charged patch and stabilized hydrophobic core are essential for avirulence function of AvrPib in the rice blast fungus

• DOI: 10.1111/tpj.14023
• Publication Date: 2018-07-10T10:26:27Z
• Authors: Xin Zhang; Dan He; Yanxiang Zhao; Xilan Cheng; Wensheng Zhao; Ian A. Taylor; Jun Yang; Junfeng Liu; You‐Liang Peng
• Keywords: Blast disease

Fungal avirulence effectors, a key weapon utilized by pathogens to promote their infection, are recognized immune receptors boost host R gene-mediated resistance. Many effectors share sparse sequence homology proteins with known functions, and molecular biochemical functions together the evolutionary relationship among different members remain largely unknown. Here, crystal structure of AvrPib, an effector from Magnaporthe oryzae, was determined showed high degree similarity M. oryzae Avrs ToxB (MAX) effectors. Compared other MAX AvrPib has distinct positive-charge patch formed five positive-charged residues (K29, K30, R50, K52 K70) on surface. These were essential function affected its nuclear localization into cells. Moreover, V39 V58, which locate in hydrophobic core structure, cause loss single-point mutation natural isolates. In comparison wild-type V39A or V58A mutations resulted partial entire secondary elements. Taken together, our results suggest that differences surface charge distribution could be one major bases for variation effector-receptor specificity, destabilization is mechanisms employed fungus evade recognition resistance factors cell.