Pneumologie 2012; 66 - P1_004
DOI: 10.1055/s-0032-1329795

Cellular responses to animal dander allergens are mediated by interactions between Allergen, Lipid and Toll-Like Receptors

J Herre 1, H Grönlund 2, T Monie 3, M Gangloff 3, N Opaleye 3, B Murton 3, H Brookes 4, K Fitzgerald 5, L Waggoner 3, M Willart 6, B Lambrecht 6, E Chilvers 1, N Gay 4, C Bryant 4
  • 1Department of Respiratory Medicine, University of Cambridge, Cambridge, UK
  • 2Department of Medicine, Clinical Immunology and Allergy Unit, Karolinska Institutet, Stockholm, Sweden
  • 3University of Cambridge, Department of Biochemistry, Cambridge, UK
  • 4University of Cambridge, Department of Veterinary Med, Cambridge, UK
  • 5Division of Infectious Diseases and Immunology, Department of Medicine, University of Massachusetts Medical School, Worcester, MA, USA
  • 6Laboratory of Immunoregulation and Mucosal Immunology, University of Ghent, Ghent, Belgium

Allergic responses can be triggered by a range of different proteins. The structure of many protein allergens is known, but there are no common features that explain why these should be allergens and how they are recognized by the host. Many allergens have the capacity to bind lipids. Recently the house dust mite protein Der p2 was shown to activate TLR4, by mimicking MD2, but it also sensitises the responses of TLR4 to its main ligand lipopolysaccharide (LPS). The dander protein Fel d1 is highly abundant indoors and is one of the commonest causes of cat allergy in people. Structurally it has an alpha helical structure whereas Der p2 has an anti-parallel beta-2-sheet conformation. Like Der p2, Fel d 1 has a lipid binding cavity, but is structurally unrelated to MD2. As yet there are no data describing how Fel d1, or other dander proteins, are recognized by the host.