Contagious caprine pleuropneumonia (CCPP), caused by Mycoplasma capricolum subsp. capripneumoniae (Mccp), is a severe respiratory disease affecting global goat farming. 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 in Escherichia coli BL21(DE3) pLysS and subsequently purified from the supernatant, and mouse antibodies confirmed its presence on the Mccp cell surface. Indirect immunofluorescence showed rMccpDLD binds to GTEC epithelial cells, indicating 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 results suggest DLD acts as both a virulence factor and adhesin during Mccp infection, making it a potential target for developing new CCPP treatments and vaccines.

To Cite This Article: Wang Z, Ge J, Song G, Liu Y, Li Q, Li R, Gao P, Zheng F, Chu Y 2025. Dihydrolipoylehydrogenase from Mycoplasma capricolum subsp. capripneumoniae: an immunogenic plasminogen-binding putative adhesin. Pak Vet J. http://dx.doi.org/10.29261/pakvetj/2025.219