MoVrp1, a putative verprolin protein, is required for asexual development and infection in the rice blast fungus Magnaporthe oryzae

Lin Huang,Haifeng Zhang,Shengpei Zhang,Ziyi Yin,Zhengguang Zhang,Muxing Liu,Xiaobo Zheng,Ping Wang,Bing Li

doi:10.1038/srep41148

Abstract

Endocytosis is a crucial cellular process in eukaryotic cells which involves clathrin and/or adaptor proteins, lipid kinases, phosphatases and the actin cytoskeleton. Verprolin proteins, such as Vrp1 in Saccharomyces cerevisiae, are conserved family proteins that regulate actin binding and endocytosis. Here, we identified and characterized MoVrp1 as the yeast Vrp1 homolog in Magnaporthe oryzae. Deletion of the MoVRP1 gene resulted in defects in vegetative growth, asexual development, and infection of the host plant. The ∆Movrp1 mutants also exhibited decreased extracellular peroxidase and laccase activities and showed defects in colony pigmentation, hyphal surface hydrophobicity, cell wall integrity, autophagy, endocytosis, and secretion of avirulent effector. Our studies provided new evidences that MoVrp1 involved in actin cytoskeleton is important for growth, morphogenesis, cellular trafficking, and fungal pathogenesis.

Highlights

Gene-product (CR16) and WIP-related (WIRE)[20,21,22]
We found that deletion of the Qc-sensitive factor attachment protein receptors (SNAREs) protein MoSyn[8] resulted in reduction and alternation in distribution of F-actin patches
We found that the RFP signals were distributed in the cytosol of the mutant, in contrast to the normal actin patch localization pattern in wildtype Guy[11] (Fig. 12), indicating that MoVrp[1] plays a crucial in regulating the proper localization of actin in M. oryzae

Summary

Introduction

Gene-product (CR16) and WIP-related (WIRE)[20,21,22]. Verprolins have important roles in signaling to actin dynamics which were mainly mediated by the WASP proteins, and influence the actin polymerisation machinery independent on the WASP proteins[19]. Loss of Vrp[1] leads to defects in polarization of cortical actin patches, internalization of receptor-bound and fluid-phase endocytic cargo, and inviability at elevated temperatures[18,24,25]. Despite these important findings, functions of Vrp[1] proteins in filamentous fungi remain unclear. We identified and characterized the yeast Vrp[1] homolog MoVrp[1] in M. oryzae, and showed that MoVrp[1] is localized to the actin patches and important for endocytosis, hyphal growth, conidial development, stress response, cell wall integrity, and pathogenicity

Methods

Results

Conclusion