In this work,the GW63K(Mg-6.54Gd-3.93Y-0.41Zr,wt.%)alloy wire was utilized as the feedstock material and the thin-walled component was fabricated using wire-arc additive manufacturing technology(WAAM).The microstructu...In this work,the GW63K(Mg-6.54Gd-3.93Y-0.41Zr,wt.%)alloy wire was utilized as the feedstock material and the thin-walled component was fabricated using wire-arc additive manufacturing technology(WAAM).The microstructural evolution during deposition and subsequent heat treatment was explained through multi-scale microstructural characterization techniques,and the impact of heat treatment on the strengthductility synergy of the deposited alloy was systematically compared.The results showed that the microstructure of the deposited sample was mainly composed of fine equiaxedα-Mg grains and Mg_(24)(Gd,Y)_(5) phase.The optimized solution heat treatment(450℃×2 h)had little effect on the grain size,but can effectively reduce the Mg_(24)(Gd,Y)_(5) eutectic phase on the grain boundary,resulting in a significant increase in elongation from 13.7% to 26.6%.After peak-aging treatment,the strength of the GW63K alloy increased to 370 MPa,which was significantly higher than the as-built state(267 MPa).The superior strength in this study is attributed to the refinement strengthening imparted by the fine microstructure inherited in the as-built GW63K alloy,as well as the precipitation strengthening due to the formation of dense β’precipitates with a pronounced plate-like aspect ratio.展开更多
Plant fungal pathogens secrete numerous proteins into the apoplast at the plant–fungus contact sites to facilitate colonization.However,only a few secretory proteins were functionally characterized in Magnaporthe ory...Plant fungal pathogens secrete numerous proteins into the apoplast at the plant–fungus contact sites to facilitate colonization.However,only a few secretory proteins were functionally characterized in Magnaporthe oryzae,the fungal pathogen causing rice blast disease worldwide.Asparagine-linked glycosylation 3(Alg3)is an a-1,3-mannosyltransferase functioning in the Nglycan synthesis of N-glycosylated secretory proteins.Fungal pathogenicity and cell wall integrity are impaired inΔalg3 mutants,but the secreted proteins affected inΔalg3 mutants are largely unknown.In this study,we compared the secretomes of the wild-type strain and theΔalg3 mutant and identified 51 proteins that require Alg3 for proper secretion.These proteins were predicted to be involved in metabolic processes,interspecies interactions,cell wall organization,and response to chemicals.Nine proteins were selected for further validation.We found that these proteins were localized at the apoplastic region surrounding the fungal infection hyphae.Moreover,the Nglycosylation of these proteins was significantly changed in theΔalg3 mutant,leading to the decreased protein secretion and abnormal protein localization.Furthermore,we tested the biological functions of two genes,INV1(encoding invertase 1,a secreted invertase)and AMCase(encoding acid mammalian chinitase,a secreted chitinase).The fungal virulence was significantly reduced,and the cell wall integrity was altered in theΔinv1 andΔamcase mutant strains.Moreover,the N-glycosylation was essential for the function and secretion of AMCase.Taken together,our study provides new insight into the role of N-glycosylated secretory proteins in fungal virulence and cell wall integrity.展开更多
基金Supported by the Industrial Collaborative Innovation Project of Shanghai(Grant No XTCX-KJ-2022-2-11)the National Natural Science Foundation of China(Grant No52073176)。
文摘In this work,the GW63K(Mg-6.54Gd-3.93Y-0.41Zr,wt.%)alloy wire was utilized as the feedstock material and the thin-walled component was fabricated using wire-arc additive manufacturing technology(WAAM).The microstructural evolution during deposition and subsequent heat treatment was explained through multi-scale microstructural characterization techniques,and the impact of heat treatment on the strengthductility synergy of the deposited alloy was systematically compared.The results showed that the microstructure of the deposited sample was mainly composed of fine equiaxedα-Mg grains and Mg_(24)(Gd,Y)_(5) phase.The optimized solution heat treatment(450℃×2 h)had little effect on the grain size,but can effectively reduce the Mg_(24)(Gd,Y)_(5) eutectic phase on the grain boundary,resulting in a significant increase in elongation from 13.7% to 26.6%.After peak-aging treatment,the strength of the GW63K alloy increased to 370 MPa,which was significantly higher than the as-built state(267 MPa).The superior strength in this study is attributed to the refinement strengthening imparted by the fine microstructure inherited in the as-built GW63K alloy,as well as the precipitation strengthening due to the formation of dense β’precipitates with a pronounced plate-like aspect ratio.
基金supported by the National Key R&D Plan of China(Grant No.2016YFD0300703)the China Agricultural Research System(Grant No.CARS-01-33)+2 种基金the Program for Changjiang Scholars and Innovative Research Team in University(Grant No.IRT1042)the 111 Project(Grant No.B13006)to YLPthe National Natural Science Foundation of China(Grant No.32001848)to XL。
文摘Plant fungal pathogens secrete numerous proteins into the apoplast at the plant–fungus contact sites to facilitate colonization.However,only a few secretory proteins were functionally characterized in Magnaporthe oryzae,the fungal pathogen causing rice blast disease worldwide.Asparagine-linked glycosylation 3(Alg3)is an a-1,3-mannosyltransferase functioning in the Nglycan synthesis of N-glycosylated secretory proteins.Fungal pathogenicity and cell wall integrity are impaired inΔalg3 mutants,but the secreted proteins affected inΔalg3 mutants are largely unknown.In this study,we compared the secretomes of the wild-type strain and theΔalg3 mutant and identified 51 proteins that require Alg3 for proper secretion.These proteins were predicted to be involved in metabolic processes,interspecies interactions,cell wall organization,and response to chemicals.Nine proteins were selected for further validation.We found that these proteins were localized at the apoplastic region surrounding the fungal infection hyphae.Moreover,the Nglycosylation of these proteins was significantly changed in theΔalg3 mutant,leading to the decreased protein secretion and abnormal protein localization.Furthermore,we tested the biological functions of two genes,INV1(encoding invertase 1,a secreted invertase)and AMCase(encoding acid mammalian chinitase,a secreted chitinase).The fungal virulence was significantly reduced,and the cell wall integrity was altered in theΔinv1 andΔamcase mutant strains.Moreover,the N-glycosylation was essential for the function and secretion of AMCase.Taken together,our study provides new insight into the role of N-glycosylated secretory proteins in fungal virulence and cell wall integrity.
