The Inhibitory Receptor LIR-1 Uses a Common Binding Interaction to Recognize Class I MHC Molecules and the Viral Homolog UL18
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 α3 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.
Additional Information
© 1999 Cell Press. Received 19 August 1999, Revised 29 September 1999. We thank P. M. Snow and I. Nangiana for assistance with protein expression, T. S. Ramalingam for helpful discussions and assistance with cell staining, D. Cosman, J. Kim, J. A. Lebrón, A. P. West, L. M. Sánchez, and H. Shen for protein samples, G. Hathaway and the Caltech PPMAL for peptide analyses, P. Poon for performing the analytical ultracentrifugation studies, and D. Cosman, B. Wilcox, and members of the Bjorkman laboratory for critical reading of the manuscript. This work was supported by a National Defense Science and Engineering Pre-Doctoral Fellowship (T. L. C.) and a grant from the Arthritis Foundation (P. J. B.).Additional details
- Eprint ID
- 75775
- Resolver ID
- CaltechAUTHORS:20170406-074314342
- National Defense Science and Engineering Graduate (NDSEG) Fellowship
- Arthritis Foundation
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2017-04-06Created from EPrint's datestamp field
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2021-11-15Created from EPrint's last_modified field