{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T18:24:43Z","timestamp":1770747883955,"version":"3.49.0"},"reference-count":39,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2019,3,20]],"date-time":"2019-03-20T00:00:00Z","timestamp":1553040000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Plants are constantly subjected to a variety of environmental stresses and have evolved regulatory responses to overcome unfavorable conditions that might reduce or adversely change a plant\u2019s growth or development. Among these, the regulated production of reactive oxygen species (ROS) as a signaling molecule occurs during plant development and pathogen defense. This study demonstrates the possible antifungal activity of Oryza sativa Tetratricopeptide Domain-containing thioredoxin (OsTDX) protein against various fungal pathogens. The transcription of OsTDX was induced by various environmental stresses known to elicit the generation of ROS in plant cells. OsTDX protein showed potent antifungal activity, with minimum inhibitory concentrations (MICs) against yeast and filamentous fungi ranging between 1.56 and 6.25 and 50 and 100 \u00b5g\/mL, respectively. The uptake of SYTOX-Green into fungal cells and efflux of calcein from artificial fungus-like liposomes suggest that its killing mechanism involves membrane permeabilization and damage. In addition, irregular blebs and holes apparent on the surfaces of OsTDX-treated fungal cells indicate the membranolytic action of this protein. Our results suggest that the OsTDX protein represents a potentially useful lead for the development of pathogen-resistant plants.<\/jats:p>","DOI":"10.3390\/ijms20061413","type":"journal-article","created":{"date-parts":[[2019,3,21]],"date-time":"2019-03-21T04:11:56Z","timestamp":1553141516000},"page":"1413","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Functional Mechanisms Underlying the Antimicrobial Activity of the Oryza sativa Trx-like Protein"],"prefix":"10.3390","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9051-0183","authenticated-orcid":false,"given":"Seong-Cheol","family":"Park","sequence":"first","affiliation":[{"name":"Department of Polymer Science and Engineering, Sunchon National University, Suncheon 57922, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Il Ryong","family":"Kim","sequence":"additional","affiliation":[{"name":"National Institute of Ecology, 1210 Geumgang-ro, Maseo-myeon, Seocheon-gun 33657, Korea"},{"name":"Division of Applied Life Science (BK21+ Program) and PMBBRC, Gyeongsang National University, Jinju 52828, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jung Eun","family":"Hwang","sequence":"additional","affiliation":[{"name":"National Institute of Ecology, 1210 Geumgang-ro, Maseo-myeon, Seocheon-gun 33657, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jin-Young","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Polymer Science and Engineering, Sunchon National University, Suncheon 57922, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Young Jun","family":"Jung","sequence":"additional","affiliation":[{"name":"National Institute of Ecology, 1210 Geumgang-ro, Maseo-myeon, Seocheon-gun 33657, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wonkyun","family":"Choi","sequence":"additional","affiliation":[{"name":"National Institute of Ecology, 1210 Geumgang-ro, Maseo-myeon, Seocheon-gun 33657, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7443-7502","authenticated-orcid":false,"given":"Yongjae","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Nutrition and Food Science, Texas A&amp;M University, College Station, TX 77843, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mi-Kyeong","family":"Jang","sequence":"additional","affiliation":[{"name":"Department of Polymer Science and Engineering, Sunchon National University, Suncheon 57922, Korea"},{"name":"The Research Institute for Sanitation and Environment of Coastal Areas, Sunchon National University, Suncheon 57922, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9596-3330","authenticated-orcid":false,"given":"Jung Ro","family":"Lee","sequence":"additional","affiliation":[{"name":"National Institute of Ecology, 1210 Geumgang-ro, Maseo-myeon, Seocheon-gun 33657, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2019,3,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.1126\/science.1067747","article-title":"Regulatory role of SGT1 in early R gene-mediated plant defenses","volume":"295","author":"Austin","year":"2002","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1146\/annurev.arplant.55.031903.141701","article-title":"Reactive oxygen species: Metabolism, oxidative stress, and signal transduction","volume":"55","author":"Apel","year":"2004","journal-title":"Annu. Rev. Plant Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1016\/j.tplants.2004.08.009","article-title":"Reactive oxygen gene network of plants","volume":"9","author":"Mittler","year":"2004","journal-title":"Trends Plant Sci."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1111\/j.1365-313X.2010.04124.x","article-title":"Research on plant abiotic stress responses in the post-genome era: Past, present and future","volume":"61","author":"Hirayama","year":"2010","journal-title":"Plant J."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1104\/pp.002857","article-title":"Transcriptional profiling reveals novel interactions between wounding, pathogen, abiotic stress, and hormonal responses in Arabidopsis","volume":"129","author":"Cheong","year":"2002","journal-title":"Plant Physiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1016\/S1369-5266(02)00289-3","article-title":"Transcription factors in plant defense and stress responses","volume":"5","author":"Singh","year":"2002","journal-title":"Curr. Opin. Plant Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.pbi.2005.05.015","article-title":"The role of abscisic acid in plant-pathogen interactions","volume":"8","author":"Mauch","year":"2005","journal-title":"Curr. Opin. Plant Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.pbi.2006.05.014","article-title":"Crosstalk between abiotic and biotic stress responses: A current view from the points of convergence in the stress signaling networks","volume":"9","author":"Fujita","year":"2006","journal-title":"Curr. Opin. Plant Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"3523","DOI":"10.1093\/jxb\/ers100","article-title":"The interaction of plant biotic and abiotic stresses: From genes to the field","volume":"63","author":"Atkinson","year":"2012","journal-title":"J. Exp. Bot."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1007\/s11103-004-0685-1","article-title":"Crosstalk in the responses to abiotic and biotic stresses in Arabidopsis: Analysis of gene expression in cytochrome P450 gene superfamily by cDNA microarray","volume":"55","author":"Narusaka","year":"2004","journal-title":"Plant Mol. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"6498","DOI":"10.1002\/pmic.200600367","article-title":"Proteomic responses of rice young panicles to salinity","volume":"6","author":"Dooki","year":"2006","journal-title":"Proteomics"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1016\/j.jprot.2011.02.006","article-title":"Plant proteome changes under abiotic stress--Contribution of proteomics studies to understanding plant stress response","volume":"74","author":"Renaut","year":"2011","journal-title":"J. Proteomics"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1104\/pp.111.182808","article-title":"An apoplastic h-type thioredoxin is involved in the stress response through regulation of the apoplastic reactive oxygen species in rice","volume":"157","author":"Zhang","year":"2011","journal-title":"Plant Physiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/BF03030408","article-title":"Ultrastructural changes of cell organelles in Arabidopsis stems after gamma irradation","volume":"48","author":"Wi","year":"2005","journal-title":"J. Plant Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1016\/j.jprot.2011.03.025","article-title":"Application of proteomics to the assessment of the response to ionising radiation in Arabidopsis thaliana","volume":"74","author":"Gicquel","year":"2011","journal-title":"J. Proteomic"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.envexpbot.2010.01.007","article-title":"Ionizing radiation: Advances in plant response","volume":"68","author":"Esnault","year":"2010","journal-title":"Environ. Exp. Bot."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/j.plaphy.2009.12.007","article-title":"The cellular redox state in plant stress biology\u2014A charging concept","volume":"48","author":"Potters","year":"2010","journal-title":"Plant Physiol. Biochem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1126\/science.1156970","article-title":"Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins","volume":"321","author":"Tada","year":"2008","journal-title":"Science"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1007\/s12257-017-0074-7","article-title":"Functional characterization of thioredoxin h type 5 with antimicrobial activity from Arabidopsis thaliana","volume":"22","author":"Park","year":"2017","journal-title":"Biotechnol. Bioprocess Eng."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2213","DOI":"10.1016\/j.bbapap.2010.09.005","article-title":"Redox properties of a thioredoxin-like Arabidopsis protein, AtTDX","volume":"1804","author":"Kim","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2734","DOI":"10.1016\/j.febslet.2009.07.057","article-title":"A cold-induced thioredoxin h of rice, OsTrx23, negatively regulates kinase activities of OsMPK3 and OsMPK6 in vitro","volume":"583","author":"Xie","year":"2009","journal-title":"FEBS Lett."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.bbrc.2006.02.090","article-title":"Investigation of toroidal pore and oligomerization by melittin using transmission electron microscopy","volume":"343","author":"Park","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1016\/j.bbamem.2010.02.023","article-title":"Antimicrobial peptides bind more strongly to membrane pores","volume":"1798","author":"Mihajlovic","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1038\/nrmicro.2015.21","article-title":"Interactions of fungal pathogens with phagocytes","volume":"14","author":"Erwig","year":"2016","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/1746-4811-3-7","article-title":"A quantitative RT-PCR platform for high-throughput expression profiling of 2500 rice transcription factors","volume":"3","author":"Caldana","year":"2007","journal-title":"Plant Methods"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1105\/tpc.16.00408","article-title":"Dynamic interactions of Arabidopsis TEN1: Stabilizing telomeres in response to heat stress","volume":"28","author":"Lee","year":"2016","journal-title":"Plant Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1016\/j.bbagen.2018.07.028","article-title":"Molecular mechanism of Arabidopsis thaliana profilins as antifungal proteins","volume":"1862","author":"Park","year":"2018","journal-title":"Biochim. Biophys. Acta (BBA) Gen. Subj."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/0003-2697(82)90113-0","article-title":"Electrophoresis buffers for polyacrylamide gels at various pH","volume":"126","author":"McLellan","year":"1982","journal-title":"Anal. Biochem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1007\/s12257-016-0390-3","article-title":"Deletion of the carboxyl terminal of thioredoxin reductase C of Arabidopsis facilitates oligomerization","volume":"21","author":"Moon","year":"2016","journal-title":"Biotechnol. Bioprocess Eng."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.jconrel.2017.04.023","article-title":"Targeting and synergistic action of an antifungal peptide in an antibiotic drug-delivery system","volume":"256","author":"Park","year":"2017","journal-title":"J. Control. Release"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"9299","DOI":"10.1021\/jf902005g","article-title":"Antifungal mechanism of a novel antifungal protein from pumpkin rinds against various fungal pathogens","volume":"57","author":"Park","year":"2009","journal-title":"J. Agric. Food Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.bbrc.2007.07.188","article-title":"Characterization of a heat-stable protein with antimicrobial activity from Arabidopsis thaliana","volume":"362","author":"Park","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1002\/bip.20679","article-title":"Structure-activity relationship of HP (2-20) analog peptide: Enhanced antimicrobial activity by N-terminal random coil region deletion","volume":"88","author":"Park","year":"2007","journal-title":"Biopolymers"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1093\/genetics\/136.2.517","article-title":"Identification and characterization of Aspergillus nidulans mutants defective in cytokinesis","volume":"136","author":"Harris","year":"1994","journal-title":"Genetics"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1002\/psc.1155","article-title":"Effect of Leucine and Lysine substitution on the antimicrobial activity and evaluation of the mechanism of the HPA3NT3 analog peptide","volume":"15","author":"Gopal","year":"2009","journal-title":"J. Pept. Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1023\/A:1018996817529","article-title":"A sensitive, high-volume, colorimetric assay for protein phosphatases","volume":"11","author":"Fisher","year":"1994","journal-title":"Pharm. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/0005-2736(80)90118-2","article-title":"Serum-induced leakage of liposome contents","volume":"597","author":"Allen","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.bbamem.2007.09.020","article-title":"Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: Pore formation mechanism in various lipid compositions","volume":"1778","author":"Park","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Park, S.C., Kim, J.Y., Kim, E.J., Cheong, G.W., Lee, Y., Choi, W., Lee, J.R., and Jang, M.K. (2018). Hydrophilic linear peptide with histidine and lysine residues as a key factor affecting antifungal activity. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19123781"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/6\/1413\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T12:39:24Z","timestamp":1760186364000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/6\/1413"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,3,20]]},"references-count":39,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2019,3]]}},"alternative-id":["ijms20061413"],"URL":"https:\/\/doi.org\/10.3390\/ijms20061413","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,3,20]]}}}