VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae

Verticillium dahliae causes a serious wilt disease of important crops and is difficult to control. Few plasma-membrane transport proteins for nutrient acquisition have been identified for this fungus, and their involvement in the disease process is unknown. Here, a plasma-membrane protein, the V. da...

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Main Authors: Xiliang Qi, Xiaofeng Su, Huiming Guo, Juncang Qi, Hongmei Cheng
Format: Article
Language:English
Published: The American Phytopathological Society 2016-07-01
Series:Molecular Plant-Microbe Interactions
Online Access:https://apsjournals.apsnet.org/doi/10.1094/MPMI-03-16-0057-R
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author Xiliang Qi
Xiaofeng Su
Huiming Guo
Juncang Qi
Hongmei Cheng
author_facet Xiliang Qi
Xiaofeng Su
Huiming Guo
Juncang Qi
Hongmei Cheng
author_sort Xiliang Qi
collection DOAJ
description Verticillium dahliae causes a serious wilt disease of important crops and is difficult to control. Few plasma-membrane transport proteins for nutrient acquisition have been identified for this fungus, and their involvement in the disease process is unknown. Here, a plasma-membrane protein, the V. dahliae thiamine transporter protein VdThit, was characterized functionally by deletion of the VdThit gene in V. dahliae. Disruption strains were viable, but growth and conidial germination and production were reduced and virulence was impaired. Interestingly, by supplementing exogenous thiamine, growth, conidiation, and virulence of the VdΔThit mutants were partially restored. Stress-tolerance assays showed that the VdΔThit mutant strains were markedly more susceptible to oxidative stress and UV damage. High-pressure liquid chromatography-mass spectrometry (HPLC-MS) and gas chromatography-mass spectrometry (GC-MS) analyses showed low levels of pyruvate metabolism intermediates acetoin and acetyl coenzyme A (acetyl-CoA) in the VdΔThit mutant strains, suggesting that pyruvate metabolism was suppressed. Expression analysis of VdThit confirmed the importance of VdThit in vegetative growth, reproduction, and invasive hyphal growth. Furthermore, a green fluorescent protein (GFP)-labeled VdΔThit mutant (VdΔThit-7-GFP) was suppressed in initial infection and root colonization, as viewed with light microscopy. Together, these results showed that VdThit plays an indispensable role in the pathogenicity of V. dahliae.
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spelling doaj.art-ab1fad7e92694f07822612f4b559cb112022-12-22T03:04:50ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062016-07-0129754555910.1094/MPMI-03-16-0057-RVdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliaeXiliang Qi0Xiaofeng Su1Huiming Guo2Juncang Qi3Hongmei Cheng4Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; andBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; andBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; andAgriculture College of Shihezi University, Shihezi 832000, ChinaBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; andVerticillium dahliae causes a serious wilt disease of important crops and is difficult to control. Few plasma-membrane transport proteins for nutrient acquisition have been identified for this fungus, and their involvement in the disease process is unknown. Here, a plasma-membrane protein, the V. dahliae thiamine transporter protein VdThit, was characterized functionally by deletion of the VdThit gene in V. dahliae. Disruption strains were viable, but growth and conidial germination and production were reduced and virulence was impaired. Interestingly, by supplementing exogenous thiamine, growth, conidiation, and virulence of the VdΔThit mutants were partially restored. Stress-tolerance assays showed that the VdΔThit mutant strains were markedly more susceptible to oxidative stress and UV damage. High-pressure liquid chromatography-mass spectrometry (HPLC-MS) and gas chromatography-mass spectrometry (GC-MS) analyses showed low levels of pyruvate metabolism intermediates acetoin and acetyl coenzyme A (acetyl-CoA) in the VdΔThit mutant strains, suggesting that pyruvate metabolism was suppressed. Expression analysis of VdThit confirmed the importance of VdThit in vegetative growth, reproduction, and invasive hyphal growth. Furthermore, a green fluorescent protein (GFP)-labeled VdΔThit mutant (VdΔThit-7-GFP) was suppressed in initial infection and root colonization, as viewed with light microscopy. Together, these results showed that VdThit plays an indispensable role in the pathogenicity of V. dahliae.https://apsjournals.apsnet.org/doi/10.1094/MPMI-03-16-0057-R
spellingShingle Xiliang Qi
Xiaofeng Su
Huiming Guo
Juncang Qi
Hongmei Cheng
VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae
Molecular Plant-Microbe Interactions
title VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae
title_full VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae
title_fullStr VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae
title_full_unstemmed VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae
title_short VdThit, a Thiamine Transport Protein, Is Required for Pathogenicity of the Vascular Pathogen Verticillium dahliae
title_sort vdthit a thiamine transport protein is required for pathogenicity of the vascular pathogen verticillium dahliae
url https://apsjournals.apsnet.org/doi/10.1094/MPMI-03-16-0057-R
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