The adhesion activity of Pasteurella glycolytic enzymes

Abstract:

Pasteurella, mainly Pasteurella multocida, can cause a variety of diseases (pasteurellosis) and also human infection and diseases.[Objective] The aim of this work was to characterize the adhesion activity of Pasteurella glycolytic enzymes to host cells (rabbit kidney cells) and two common host molecules, plasminogen (Plg) and fibronectin (Fn).[Methods] The glycolytic enzymes of P. multocida were expressed by prokaryotic expression system, then purified, and their polyclonal antibodies were prepared. The adhesion activity of P. asteurella glycolytic enzymes was studied by cell surface localization detection, adhesion and adhesion inhibition experiments.[Results] Seven glycolytic enzymes except enolase and pyruvate kinase were found on the surface of P. multocida cells. The seven glycolytic enzymes all could adhere to rabbit kidney cells, but only PGI polyclonal antibodies could inhibit the adhesion of P. multocida. Far Western blotting showed that all nine glycolytic enzymes could bind to the host Plg and Fn. The recruitment inhibition experiments showed that the antibodies of phosophoglucose isomerase, aldolase and phosphoglycerate mutase could inhibit the binding of P. multocida to both Plg and Fn, while the antibodies of phosphofructokinase, triose phosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase could only inhibit the binding of P. multocida to either Plg or Fn.[Conclusion]] The phosophoglucose isomerase, phosphofructokinase, aldolase, triose phosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and phosphoglycerate mutase of P. multocida play an important role in the adhesion of P. multocida to host cells or molecules. The completion of this study will deepen the understanding of molecular pathogenesis of Pasteurellosis, and provide basic data for new diagnostic markers, new vaccines, and new drug targets.