FtsZ contributes to cytoadhesion and interaction with host extracellular matrix components and plasminogen in Mycoplasma bovis.

Mycoplasma bovis causes serious diseases in cattle and is one of the most economically important pathogens threatening the global cattle industry. It is still a great challenge to prevent and control M. bovis infections owing to the increase in antibiotics resistance and unsatisfactorily effective commercial vaccines. FtsZ is commonly considered as a division protein in most bacteria. Owing to the limited genetic manipulation tools of M. bovis, the role of FtsZ in the pathogenicity of M. bovis remains unknown. In this study, FtsZ protein was found to be mainly distributed on the cell membrane, was highly conserved, and had good immunogenicity. FtsZ could bind to embryonic bovine lung cells (EBL) membrane extract, and this binding was inhibited by anti-FtsZ serum. In addition, FtsZ interacted with host extracellular matrix components fibronectin, laminin, vitronectin, and collagen IV in a dose-dependent manner, and promoted tissue diffusion by activating plasminogen through tissue plasminogen activator (tPA). Disruption of the ftsZ gene markedly reduced the adhesion of M. bovis to EBL cells while the complemented strain M. bovis ΔftsZ: ftsZ partly restored the adhesion ability. This is a first description that FtsZ acts as a novel adhesion protein in Mycoplasma, which interacts with host extracellular matrix components and plasminogen, and plays a vital role in adhesion and dissemination. This study expands our understanding of FtsZ significant role in the pathogenicity of M. bovis and provides a new potential vaccine and drug target against M. bovis infections.