Journal
JOURNAL OF IMMUNOLOGY
Volume 200, Issue 7, Pages 2247-2252Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1701421
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Funding
- National Research, Development and Innovation Office/Hungarian Scientific Research Fund [K108642, K119374, K119386]
- MedInProt Protein Science Research Synergy Program of the Hungarian Academy of Sciences
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The complement system is a sophisticated network of proteases. In this article, we describe an unexpected link between two linear activation routes of the complement system: the lectin pathway (LP) and the alternative pathway (AP). Mannose-lectin binding-associated serine protease (MASP)-1 is known to be the initiator protease of the LP. Using a specific and potent inhibitor of MASP-1, SGMI-1, as well as other MASP-1 inhibitors with different mechanisms of action, we demonstrated that, in addition to its functions in the LP, MASP-1 is essential for bacterial LPS-induced AP activation, whereas it has little effect on zymosan-induced AP activation. We have shown that MASP-1 inhibition prevents AP activation, as well as attenuates the already initiated AP activity on the LPS surface. This newly recognized function of MASP-1 can be important for the defense against certain bacterial infections. Our results also emphasize that the mechanism of AP activation depends on the activator surface.
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