Peroxisomal alanine: glyoxylate aminotransferase AGT1 is indispensable for appressorium function of the rice blast pathogen, Magnaporthe oryzae.

PloS One
Vijai BhadauriaYangdou Wei

Abstract

The role of β-oxidation and the glyoxylate cycle in fungal pathogenesis is well documented. However, an ambiguity still remains over their interaction in peroxisomes to facilitate fungal pathogenicity and virulence. In this report, we characterize a gene encoding an alanine, glyoxylate aminotransferase 1 (AGT1) in Magnaporthe oryzae, the causative agent of rice blast disease, and demonstrate that AGT1 is required for pathogenicity of M. oryzae. Targeted deletion of AGT1 resulted in the failure of penetration via appressoria; therefore, mutants lacking the gene were unable to induce blast symptoms on the hosts rice and barley. This penetration failure may be associated with a disruption in lipid mobilization during conidial germination as turgor generation in the appressorium requires mobilization of lipid reserves from the conidium. Analysis of enhanced green fluorescent protein expression using the transcriptional and translational fusion with the AGT1 promoter and open reading frame, respectively, revealed that AGT1 expressed constitutively in all in vitro grown cell types and during in planta colonization, and localized in peroxisomes. Peroxisomal localization was further confirmed by colocalization with red fluorescent prot...Continue Reading

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Citations

Aug 8, 2015·Environmental Microbiology·Joon-Hee HanKyoung Su Kim
Sep 10, 2016·BioMed Research International·Xiao-Lin ChenCaiyun Liu
Apr 2, 2019·Molecular Plant-microbe Interactions : MPMI·Yuxin YanJianping Lu

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Methods Mentioned

BETA
phosphotransferase
PCR
confocal microscopy

Software Mentioned

BLAST

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