The sorting nexins Atg20/Snx42 and Snx41 regulate membrane traffic and endosomal 
protein sorting and are essential for Cvt and/or pexophagy in yeast. Previously, 
we showed that macroautophagy is necessary for conidiation in the rice-blast 
fungus Magnaporthe oryzae. Here, we analyzed the physiological function(s) of 
selective autophagy in Magnaporthe through targeted deletion of MGG_12832, an 
ortholog of yeast SNX41 and ATG20/SNX42. Loss of MGG_12832 (hereafter SNX41) 
abolished conidia formation and pathogenesis in M. oryzae. Snx41-GFP localized 
as dynamic puncta or short tubules that are partially associated with 
autophagosomes and/or autophagic vacuoles. PX domain, but not macroautophagy per 
se, was required for such localization of Snx41-GFP in Magnaporthe. Although not 
required for nonselective autophagy, Snx41 was essential for pexophagy in 
Magnaporthe. We identified Oxp1, an ATP-dependent oxoprolinase in the 
gamma-glutamyl cycle, as a binding partner and potential retrieval target of 
Snx41-dependent protein sorting. The substrate of Oxp1, 5-oxoproline, could 
partially restore conidiation in the snx41Δ. Exogenous glutathione, a product of 
the gamma-glutamyl cycle, significantly restored pathogenicity in the snx41Δ 
mutant, likely through counteracting the oxidative stress imposed by the host. 
We propose that the gamma-glutamyl cycle and glutathione biosynthesis are 
subject to regulation by Snx41-dependent vesicular trafficking, and mediate 
antioxidant defense crucial for in planta growth and pathogenic differentiation 
of Magnaporthe at the onset of blast disease in rice.