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      Mannose binding lectin plays a crucial role in innate immunity against yeast by enhanced complement activation and enhanced uptake of polymorphonuclear cells

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          Abstract

          Background

          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. We investigated the contribution of MBL to antifungal innate immunity towards C. parapsilosis in vitro.

          Results

          High 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.

          Conclusion

          Our results suggest that MBL plays a crucial role in the innate immunity against infections caused by yeast by increasing uptake by PMN.

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          Most cited references44

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          Mannose-binding lectin binds to a range of clinically relevant microorganisms and promotes complement deposition.

          M. Turner, H Holzel, N Klein … (2000)
          Mannose-binding lectin (MBL) is a collagenous serum lectin believed to be of importance in innate immunity. Genetically determined low levels of the protein are known to predispose to infections. In this study the binding of purified MBL to pathogens isolated from immunocompromised children was investigated by flow cytometry. Diverse Candida species, Aspergillus fumigatus, Staphylococcus aureus, and beta-hemolytic group A streptococci exhibited strong binding of MBL, whereas Escherichia coli, Klebsiella species, and Haemophilus influenzae type b were characterized by heterogeneous binding patterns. In contrast, beta-hemolytic group B streptococci, Streptococcus pneumoniae, and Staphylococcus epidermidis showed low levels of binding. Bound MBL was able to promote C4 deposition in a concentration-dependent manner. We conclude that MBL may be of importance in first-line immune defense against several important pathogens.
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            Impact of mannose-binding lectin on susceptibility to infectious diseases.

            Damon P. Eisen, Robyn M. Minchinton (2003)
            When the adaptive immune response is either immature or compromised, the innate immune system constitutes the principle defense against infection. Mannose-binding lectin (MBL) is a C-type serum lectin that plays a central role in the innate immune response. MBL binds microbial surface carbohydrates and mediates opsonophagocytosis directly and by activation of the lectin complement pathway. A wide variety of clinical isolates of bacteria, fungi, viruses, and parasites are bound by MBL. Three polymorphisms in the structural gene MBL2) and 2 promoter gene polymorphisms are commonly found that result in production of low serum levels of MBL. Clinical studies have shown that MBL insufficiency is associated with bacterial infection in patients with neutropenia and meningococcal sepsis. Low MBL levels appear to predispose persons to HIV infection. Numerous other potential infectious disease associations have been described. Therapy to supplement low MBL levels is being explored using either plasma-derived or recombinant material.
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              Mannose-binding lectin: the pluripotent molecule of the innate immune system.

              M TURNER (1996)
              Article 0 comments Cited 71 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): BMC Microbiol
                Title: BMC Microbiology
                Publisher: BioMed Central
                ISSN (Electronic): 1471-2180
                Publication date Collection: 2008
                Publication date (Electronic): 18 December 2008
                Volume: 8
                Page: 229
                Affiliations
                [1 ]Eijkman-Winkler Institute for Medical & Clinical Microbiology, Utrecht University Hospital, Utrecht, the Netherlands
                [2 ]Department of Internal Medicine & Infectious Diseases, Utrecht University Hospital, Utrecht, the Netherlands
                [3 ]Department of Medical Microbiology & Immunology, St. Antonius Hospital Nieuwegein, the Netherlands
                Article
                Publisher ID: 1471-2180-8-229
                DOI: 10.1186/1471-2180-8-229
                PMC ID: 2627907
                PubMed ID: 19094203
                SO-VID: 6433a38b-d3df-46a1-880e-e509865f2995
                Copyright © Copyright © 2008 van Asbeck et al; licensee BioMed Central Ltd.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 3 June 2008
                Date accepted : 18 December 2008
                Categories
                Subject: Research Article

                ScienceOpen disciplines: Microbiology & Virology
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology

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