Abstract
The cysteine-rich domain (CR) of the mannose receptor binds sulfated glycoprotein CR ligand (CRL) expressed by subpopulations of myeloid cells in secondary lymphoid organs (CRL(+) cells). In naïve mice, these CRL(+) cells, metallophilic macrophages (M) in spleen and subcapsular sinus M in lymph nodes, are located strategically for antigen capture and are adjacent to B cell follicles, but their role in the immune response is unknown. We have exploited the lectin activity of CR to develop a highly specific system for targeting protein to CRL(+) M. We demonstrate that the sulfated carbohydrates recognized by CR are exposed to the extracellular milieu and mediate highly specific targeting of CR-containing proteins. This model will allow the dissection of the role of metallophilic M in an immune response in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cattle
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Complement Activation
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Complement System Proteins / immunology
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Cysteine / analysis
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Cysteine / metabolism
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Humans
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Immunoglobulin Fc Fragments / immunology
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Lectins / metabolism
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Lectins, C-Type / chemistry
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Lectins, C-Type / genetics
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Lectins, C-Type / metabolism
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Ligands
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Luteinizing Hormone / metabolism
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Macrophages / immunology*
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Macrophages / metabolism*
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Mannose Receptor
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Mannose-Binding Lectins / chemistry
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Mannose-Binding Lectins / genetics
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Mannose-Binding Lectins / metabolism
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Metals / metabolism*
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Mice
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Mice, Inbred BALB C
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Mice, Inbred C57BL
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Mice, Mutant Strains
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Mutation / genetics
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Protein Binding
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Proteins / metabolism*
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / metabolism
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Substrate Specificity
Substances
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Immunoglobulin Fc Fragments
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Lectins
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Lectins, C-Type
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Ligands
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Mannose Receptor
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Mannose-Binding Lectins
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Metals
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Proteins
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Receptors, Cell Surface
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Luteinizing Hormone
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Complement System Proteins
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Cysteine