Abstract
BackgroundMannose binding lectin (MBL) is an important host defence protein against opportunistic fungal pathogens. This carbohydrate-binding protein, an opsonin and lectin pathway activator, binds through multiple lectin domains to the repeating sugar arrays displayed on the surface of a wide range of clinically relevant microbial species. We investigated the contribution of MBL to antifungal innate immunity towards C. parapsilosis in vitro.ResultsHigh avidity binding was observed between MBL and C. albicans and C. parapsilosis. Addition of MBL to MBL deficient serum increased the deposition of C4 and C3b and enhanced the uptake of C. albicans, C. parapsilosis and acapsular C. neoformans by polymorphonuclear cells (PMNs). Compared to other microorganisms, such as Escherichia coli, Staphylococcus aureus and Cryptococcus neoformans, C. parapsilosis and Candida albicans were potent activators of the lectin pathway.ConclusionOur results suggest that MBL plays a crucial role in the innate immunity against infections caused by yeast by increasing uptake by PMN.
Highlights
Mannose binding lectin (MBL) is an important host defence protein against opportunistic fungal pathogens
In this study we evaluated the role of MBL in the opsonophagocytosis of C. parapsilosis
Almost no binding of MBL was observed to S. aureus, E. coli and encapsulated C. neoformans
Summary
Mannose binding lectin (MBL) is an important host defence protein against opportunistic fungal pathogens This carbohydrate-binding protein, an opsonin and lectin pathway activator, binds through multiple lectin domains to the repeating sugar arrays displayed on the surface of a wide range of clinically relevant microbial species. Mannose binding lectin [1], a plasma protein of hepatic origin that belongs to the family of calcium-dependent collagenous lectins (collectin), is an important protein of the innate immune system [1,2,3,4,5,6] This carbohydrate-binding protein binds mannose and N-acetylglucosamine (GlcNAc) sugars and their derivates present on the surface of a wide range of clinically relevant microbial species and has the ability to distinguish self from nonself [4,5,7,8]. It is unclear whether MBL acts as a direct opsonin or is merely enhances other complement pathways and/or antibodymediated phagocytosis [5]
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