Dihydrolipoyl Dehydrogenase from Mycoplasma capricolum subsp. capripneumoniae: An Immunogenic Plasminogen-Binding Putative Adhesin
文献类型: 外文期刊
作者: Ziqing Wang;Jiazhen Ge;Guodong Song;Yijian Liu;Qianqian Li;Renge Li;Pengcheng Gao;Fuying Zheng;Yuefeng Chu
作者机构:
关键词: Adhesin Dihydrolipoyl dehydrogenase;Capripneumoniae;Mycoplasma capricolum;Plasminogen;Subcellular localization;subsp
期刊名称: Pakistan Veterinary Journal
ISSN: 2074-7764
年卷期: 2025 年 45 卷 3 期
页码:
收录情况: SCIE(2025版)
摘要: Contagious caprine pleuropneumonia (CCPP), caused by Mycoplasma capricolum ubsp. capripneumoniae (Mccp), is a severe respiratory disease affecting global goat arming. Mccp infection relies on its adhesion to the host respiratory tract. Dihydrolipoamide dehydrogenase (DLD) is a flavoprotein oxidoreductase that forms disulfide bonds using flavin adenine dinucleotide (FAD). It typically exists as a homodimer, with each 51 kDa subunit covalently linked to one FAD molecule. Although DLD's structure and enzymatic function are well understood, its role in Mccp pathogenicity remains unclear. In our study, rDLD (rMccpDLD) was expressed n Escherichia coli BL21(DE3) pLysS and subsequently purified from the upernatant, and mouse antibodies confirmed its presence on the Mccp cell surface. ndirect immunofluorescence showed rMccpDLD binds to GTEC epithelial cells, ndicating its role in adhesion. Mouse anti-rMccpDLD serum significantly inhibited M1601 strain adhesion to these cells. Additionally, DLD interacts with host plasminogen, with molecular dynamics simulations confirming stable binding. These esults suggest DLD acts as both a virulence factor and adhesin during Mccp nfection, making it a potential target for developing new CCPP treatments and vaccines.
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