Riemerella anatipestifer extracellular protease S blocks complement activation via the classical and lectin pathways

ABSTRACTRiemerella anatipestifer (RA) is the causative agent of infectious serositis in ducklings and other avian species. It is difficult to control the disease due to its 21 serotypes, poor cross-protection, and bacterial resistance to antimicrobial agents. The complement system is an important component of the innate immune system. However, bacterial pathogens exploit several strategies to evade detection by the complement system. Here, we purified and identified a 59-kDa RA extracellular protease S (EcpS) consisting of a gelatinase. In this study, we aimed to determine how EcpS interferes with complement activation and whether it could block complement-dependent neutrophil function. We found that EcpS potently blocked RA phagocytosis and killing by duck neutrophils. Furthermore, EcpS inhibited the opsonization of bacteria by complement 3b. EcpS specifically blocked complement 3b and complement 4b deposition via the classical and lectin pathways, whereas the alternative pathway was not affected. In sum...