Abstract
Mycoplasma bovis is the causative agent of Mycoplasma bovis-associated disease (MbAD). Although the mechanisms underlying M. bovis adherence to host cells is not clear, recent studies have shown that the cell surface protein α-enolase facilitates bacterial invasion and dissemination in the infected host. In this study, we cloned, expressed and purified recombinant M. bovis α-enolase and induced polyclonal anti-α-enolase antibodies in rabbits. M. bovis α-enolase was detected in the cytoplasmic and membrane protein fractions by these antibodies. Triple immunofluorescence labeling combined with confocal laser scanning microscopy (CLSM) revealed that the plasminogen (Plg) enhanced the adherence of M. bovis to embryonic bovine lung (EBL) cells; the values obtained for adherence and inhibition are consistent with this finding. Interestingly, we found that trace amounts of trypsin acted as a more effective enhancer of cell adherence than Plg. Hence, our data indicate that surface-associated M. bovis α-enolase is an adhesion-related factor of M. bovis that contributes to adherence by binding Plg.
Highlights
The adherence of mycoplasmas to the host cell initiates infection with bacteria of this genus [1]
Identification of enolase of M. bovis The 1365-bp open reading frame (ORF) of a-enolase was identified in the complete genomic sequence of M. bovis strain Hubei
The M. bovis Hubei a-enolase identified showed more than 90% homology to M. bovis PG45 (E4PZX0), M. fermentans (E1PS24), M. agalactiae(A5IYA8), M. hyopneumoniae (Q601S2) and M. gallisepticum (Q7NAY0), respectively
Summary
The adherence of mycoplasmas to the host cell initiates infection with bacteria of this genus [1]. Mycoplasma bovis is the causative agent of Mycoplasma bovis-associated disease (MbAD) [2]. M. bovis, which causes pneumonia, otitis media and arthritis in young calves, has been an important cause of disease in North America,Europe and Asia [4,5,6]. M. bovis was first isolated in the Hubei province of China in 2008 [6], but the economic cost of MbAD has not been reported. Many pathogens have been found to capture Plg, which allows the bacteria to acquire surfaceassociated proteolytic activity that may facilitate bacterial invasion and dissemination in the infected host [9]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
