Abstract
LIR-1 is a class I MHC receptor related to natural killer inhibitory receptors (KIRs). Binding of LIR-1 or KIRs to class I molecules results in inhibitory signals. Unlike individual KIRs, LIR-1 recognizes many class I alleles and also binds UL18, a human cytomegalovirus class I MHC homolog. Here, we show that LIR-1 interacts with the relatively nonpolymorphic alpha3 domain of class I proteins and the analogous region of UL18 using its N-terminal immunoglobulin-like domain. The >1000-fold higher affinity of LIR-1 for UL18 than for class I illustrates how a viral protein competes with host proteins to subvert the host immune response. LIR-1 recognition of class I molecules resembles the CD4-class II MHC interaction more than the KIR-class I interaction, implying a functional distinction between LIR-1 and KIRs.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Alleles
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Animals
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Antigens, CD*
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CHO Cells
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Capsid / chemistry
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Capsid / metabolism*
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Capsid Proteins*
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Cricetinae
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Cricetulus
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Cytomegalovirus / immunology
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Glycosylation
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Histocompatibility Antigens Class I / metabolism*
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Humans
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Killer Cells, Natural / immunology
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Killer Cells, Natural / metabolism
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Leukocyte Immunoglobulin-like Receptor B1
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Macromolecular Substances
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Models, Molecular
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Protein Binding
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Protein Denaturation
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Protein Folding
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
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Receptors, Immunologic / classification*
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Receptors, Immunologic / metabolism*
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Receptors, KIR
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Recombinant Fusion Proteins / metabolism
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Solubility
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Transfection
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beta 2-Microglobulin / metabolism
Substances
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Antigens, CD
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Capsid Proteins
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Histocompatibility Antigens Class I
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LILRB1 protein, human
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Leukocyte Immunoglobulin-like Receptor B1
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Macromolecular Substances
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Receptors, Immunologic
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Receptors, KIR
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Recombinant Fusion Proteins
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VP23 protein, Human herpesvirus 1
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beta 2-Microglobulin