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The human mannose-binding protein functions as an opsonin.
Open accessAbstract
The human mannose-binding protein (MBP) is a multimeric serum protein that is divided into three domains: a cysteine-rich NH2-terminal domain that stabilizes the alpha-helix of the second collagen-like domain, and a third COOH-terminal carbohydrate binding region. The function of MBP is unknown, although a role in host defense is suggested by its ability to bind yeast mannans. In this report we show that native and recombinant human MBP can serve in an opsonic role in serum and thereby enhance clearance of mannose rich pathogens by phagocytes. MBP binds to wild-type virulent Salmonella montevideo that express a mannose-rich O-polysaccharide. Interaction of MBP with these organisms results in attachment, uptake, and killing of the opsonized bacteria by phagocytes. These results demonstrate that MBP plays a role in first line host defense against certain pathogenic organisms.
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Neth, O., Jack, D. L., Dodds, A. W., Holzel, H., Klein, N. J., & Turner, M. W. (2000) · Infection and Immunity · doi:10.1128/iai.68.2.688-693.2000 · Cited by 561
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A Novel Human Serum Lectin with Collagen- and Fibrinogen-like Domains That Functions as an Opsonin
Matsushita, M., Endo, Y., Taira, S., Sato, Y., Fujita, T., Ichikawa, N., Nakata, M., & Mizuochi, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2448 · Cited by 329
Mannose-Binding Lectin in Severe Acute Respiratory Syndrome Coronavirus Infection
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Metadata
- Authors
- Kuhlman, M., Joiner, K., & Ezekowitz, R. A.
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1989-05-01
- Volume
- 169
- Issue
- 5
- Pages
- 1733-1745
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2119799948
- Cited by
- 434
- References
- 0
- FWCI
- 7.83
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kuhlman, M., Joiner, K., & Ezekowitz, R. A. (1989). The human mannose-binding protein functions as an opsonin. The Journal of experimental medicine. https://doi.org/10.1084/jem.169.5.1733
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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