Characterization of host plasminogen exploitation of Pasteurella multocida

Abstract

Pasteurella multocida is the causative agent of a wide range of disease (pasteurellosis) and a zoonotic pathogen in humans. Some pathogenic bacteria are able to exploit host plasminogen for migration across tissue barriers or evade from host innate immunity. However, there is no study on host plasminogen exploitation of P. multocida. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) has been reported to be a plasminogen receptor in many pathogenic bacteria, but its role in P. multocida exploiting plasminogen has not yet been characterized. The aim of this study was to detect the activity of P. multocida to exploit host plasminogen and evaluate the ability of GAPDH to act as a receptor in the recruitment process. P. multocida could recruit host plasminogen and exhibited plasmin activity when stimulated by urokinase. GAPDH exhibited binding activity to plasminogen. GAPDH Antiserum significantly decrease the plasminogen recruitment activity of P. multocida. In conclusion, P. multocida is able to exploit host plasminogen via GAPDH. To our knowledge, this is the first report on host plasminogen exploitation of P. multocida.