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The C‐type lectin superfamily in the immune system
Abstract
Summary: Protein‐carbohydrate interactions serve multiple functions in the immune system. Many animal lectins (sugar‐binding proteins) mediate both pathogen recognition and cell‐cell interactions using structurally related Ca 2+‐dependent carbohydrate‐recognition domains (C‐type CRDs). Pathogen recognition by soluble collections such as serum mannose‐binding protein and pulmonary surfactant proteins, and also the macrophage cell‐surface mannose receptor, is effected by binding of terminal monosaccharide residues characteristic of bacterial and fungal cell surfaces. The broad selectivity of the monosaccharide‐binding site and the geometrical arrangement of multiple CRDs in the intact lectins explains the ability of the proteins to mediate discrimination between self and non‐self. In contrast, the much narrower binding specificity of selectin cell adhesion molecules results from an extended binding site within a single CRD. Other proteins, particularly receptors on the surface of natural killer cells, contain C‐type lectin‐like domains (CTLDs) that are evolutionarily divergent from the C‐type lectins and which would be predicted to function through different mechanisms.
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Cites
Selectins and their ligands: Current concepts and controversies
Kansas, G. (1996) · Blood · doi:10.1182/blood.v88.9.3259.bloodjournal8893259 · Cited by 1,415
Varki, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7390 · Cited by 946
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Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
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Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A. (2001) · Science · doi:10.1126/science.291.5512.2370 · Cited by 1,588
Brown, G. D., & Gordon, S. (2001) · Nature · doi:10.1038/35092620 · Cited by 1,579
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Kishore, U., Greenhough, T. J., Waters, P., Shrive, A. K., Ghai, R., Kamran, M. F., Bernal, A. L., Reid, K. B. M., Madan, T., & Chakraborty, T. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2005.08.004 · Cited by 523
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Wu, H., Kuzmenko, A., Wan, S., Schaffer, L., Weiss, A., Fisher, J. H., Kim, K. S., & McCormack, F. X. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16889 · Cited by 412
Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein
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Humoral Pattern Recognition and the Complement System
Degn, S. E., & Thiel, S. (2013) · Scandinavian Journal of Immunology · doi:10.1111/sji.12070 · Cited by 141
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de Kivit, S., Kraneveld, A. D., Garssen, J., & Willemsen, L. E. M. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.05.086 · Cited by 94
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Le Luyer, J., Schull, Q., Auffret, P., Lopez, P., Crusot, M., Belliard, C., Basset, C., Carradec, Q., Poulain, J., Planes, S., et al. (2021) · Animal Microbiome · doi:10.1186/s42523-021-00097-1 · Cited by 16
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Metadata
- Authors
- Weis, W. I., Taylor, M. E., & Drickamer, K.
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 1998-06
- Volume
- 163
- Issue
- 1
- Pages
- 19-34
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- OpenAlex
- W2101994976
- Cited by
- 1,047
- References
- 2
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- closed
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