Identification of an Activating Chicken Ig-like Receptor Recognizing Avian Influenza Viruses.
Chicken Ig-like receptors (CHIRs) represent a multigene family encoded by the leukocyte receptor complex that encodes a variety of receptors that are subdivided into activating CHIR-A, inhibitory CHIR-B, and bifunctional CHIR-AB. Apart from CHIR-AB, which functions as an Fc receptor, CHIR ligands are unknown. In the current study, we used a panel of different BWZ.36 CHIR reporter cells to identify an interaction between specific CHIRs and avian influenza virus (AIV). The specificity of the CHIR-AIV interaction was further demonstrated using CHIR fusion proteins that bound to AIV-coated plates and were able to reduce the interaction of reporter cells with AIV. There was no difference in binding of CHIR to different AIV strains. Furthermore, CHIR fusion proteins reduced AIV-induced in vitro activation of NK cells obtained from lungs of AIV-infected animals, as judged by the lower frequency of CD107+cells. Because the original CHIR reporter lines were generated based on sequence information about extracellular CHIR domains, we next identified a full-length CHIR that displayed similar binding to AIV. The sequence analysis identified this CHIR as a CHIR-A. Neuraminidase treatment of coated CHIR-human Ig proteins reduced binding of trimeric H5 proteins to CHIR. This suggests that the interaction is dependent on sialic acid moieties on the receptor. In conclusion, this article identifies AIV as a ligand of CHIR-A and describes the functional consequences of this interaction.
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands; and.
Christine A
CA
Jansen
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands; and.
Daphne A
DA
van Haarlem
Institute for Animal Physiology, Department of Veterinary Sciences, Ludwig Maximilian University Munich, 80539 Munich, Germany.
Beatrice
B
Sperling
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands; and.
Peter J
0000-0002-0948-1117
PJ
van Kooten
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands; and.
Erik
E
de Vries
Institute for Animal Physiology, Department of Veterinary Sciences, Ludwig Maximilian University Munich, 80539 Munich, Germany.
Birgit C
BC
Viertlboeck
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands; and.
Lonneke
0000-0003-2241-1743
L
Vervelde
Institute for Animal Physiology, Department of Veterinary Sciences, Ludwig Maximilian University Munich, 80539 Munich, Germany goebel@lmu.de.
Thomas W
TW
Göbel
D000595:Amino Acid Sequence; D000818:Animals; D030161:Avian Proteins / Q000235:genetics / Q000378:metabolism*; D002645:Chickens / Q000276:immunology*; D004285:Dogs; D000070557:Immunoglobulin Domains / Q000235:genetics; D053127:Influenza A Virus, H9N2 Subtype / Q000276:immunology*; D005585:Influenza in Birds / Q000276:immunology*; D007694:Killer Cells, Natural / Q000276:immunology* / Q000821:virology; D008168:Lung / Q000473:pathology*; D008213:Lymphocyte Activation; D061985:Madin Darby Canine Kidney Cells; D051379:Mice; D005810:Multigene Family / Q000235:genetics; D015202:Protein Engineering; D011961:Receptors, Fc / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics
D030161:Avian Proteins; D011961:Receptors, Fc; D011993:Recombinant Fusion Proteins