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In an attempt to enhance the antimicrobial efficacy of DrsB1, the DrsB1 encoding 93\u00a0bp sequence was either fused to the N or C terminus of sequence encoding chitin\u2010binding domain (CBD) of <jats:italic>Avr<\/jats:italic>4 gene from <jats:italic>Cladosporium fulvum<\/jats:italic>. Tobacco leaf disk explants were inoculated with <jats:italic>Agrobacterium rhizogenes<\/jats:italic> harboring pGSA\/CBD\u2010DrsB1 and pGSA\/DrsB1\u2010CBD expression vectors to produce hairy roots (HRs). Polymerase chain reaction (PCR) was employed to screen putative transgenic tobacco lines. Semi\u2010quantitative RT\u2010PCR and western blotting analysis indicated that the expression of recombinant genes were significantly higher, and recombinant proteins were produced in transgenic HRs. The recombinant proteins were extracted from the tobacco HRs and used against <jats:italic>Pectobacterium carotovorum<\/jats:italic>, <jats:italic>Agrobacterium tumefaciens<\/jats:italic>, <jats:italic>Ralstonia solanacearum<\/jats:italic>, and <jats:italic>Xanthomonas campestris<\/jats:italic> pathogenic bacteria and <jats:italic>Alternaria alternata<\/jats:italic> and <jats:italic>Pythium <\/jats:italic>sp. fungi. Two recombinant proteins had a statistically significant (<jats:italic>p<\/jats:italic>\u00a0&lt;\u00a00.01) inhibitory effect on the growth and development of plant pathogens. The CBD\u2010DrsB1 recombinant protein demonstrated a higher antibacterial effect, whereas the DrsB1\u2010CBD recombinant protein demonstrated greater antifungal activity. Scanning electron microscopy images revealed that the structure of the fungal mycelia appeared segmented, adhered to each other, and crushed following the antimicrobial activity of the recombinant proteins. Due to the high antimicrobial activity of the recombinant proteins against plant pathogens, this strategy can be used to generate stable transgenic crop plants resistant to devastating plant pathogens.<\/jats:p>","DOI":"10.1002\/mbo3.837","type":"journal-article","created":{"date-parts":[[2019,3,26]],"date-time":"2019-03-26T02:41:04Z","timestamp":1553568064000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Targeting microbial pathogens by expression of new recombinant dermaseptin peptides in tobacco"],"prefix":"10.1002","volume":"8","author":[{"given":"Mitra","family":"Khademi","sequence":"first","affiliation":[{"name":"Agronomy and Plant Breeding Department, Faculty of Agriculture Lorestan University Khorramabad Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8291-3887","authenticated-orcid":false,"given":"Farhad","family":"Nazarian\u2010Firouzabadi","sequence":"additional","affiliation":[{"name":"Agronomy and Plant Breeding Department, Faculty of Agriculture Lorestan University Khorramabad Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmad","family":"Ismaili","sequence":"additional","affiliation":[{"name":"Agronomy and Plant Breeding Department, Faculty of Agriculture Lorestan University Khorramabad Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reza","family":"Shirzadian Khorramabad","sequence":"additional","affiliation":[{"name":"Agricultural Biotechnology Department, Faculty of Agricultural Sciences University of Guilan Rasht Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,3,25]]},"reference":[{"key":"e_1_2_10_2_1","first-page":"45","article-title":"Rhizosecretion of the recombinant antimicrobial peptide ranalexin from transgenic tobacco hairy roots","volume":"1","author":"Aleinein R.","year":"2015","journal-title":"Journal of Botanical Sciences"},{"key":"e_1_2_10_3_1","volume-title":"Expression of a Dermaseptin B1 peptide in tobacco to produce transgenic plants resistance to pathogens","author":"Alibakhshi A.","year":"2017"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj3220815"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1007\/s13205-018-1416-7"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1093\/ajcp\/45.4_ts.493"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(94)00753-5"},{"key":"e_1_2_10_8_1","volume-title":"Proteins methods","author":"Bollag D. 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