Recognition of the major cat allergen Fel d 1 through the XXXX -rich domain of the @entity3913 receptor determines its allergenicity.

@entity1 @entity462 @entity19 @entity566 @entity565 @entity6527 @entity3913 @entity56 @entity3363
Dendritic cells are professional antigen-presenting cells that are specialized in antigen uptake and presentation. @entity566 to cat has increased substantially in recent years and has been shown to be positively associated with @entity565 . We have recently shown that the @entity3913 receptor (MR), a C-type lectin expressed by dendritic cells, recognizes various glycoallergens from diverse sources and is involved in promoting @entity56 responses to a major house dust mite allergen in vitro. Here we investigated the potential role of MR in @entity56 responses to Fel d 1, a major cat allergen. Fel d 1 binding to MR was confirmed by ELISA. Using blocking, gene silencing (siRNA) experiments, and MR knock-out (MR(-/-)) cells, we have demonstrated that MR plays a major role in internalization of Fel d 1 by @entity1 and mouse antigen-presenting cells. Intriguingly, unlike other glycoallergens, recognition of Fel d 1 by MR is mediated by the @entity462 -rich domain, which correlates with the presence of sulfated @entity3363 in natural Fel d 1. WT and MR(-/-) @entity19 were used to study the role of MR in @entity56 sensitization to Fel d 1 in vivo. MR(-/-) @entity19 sensitized with cat dander extract and Fel d 1 produced significantly lower levels of total IgE, Fel d 1-specific-IgE and @entity6527 , the hallmarks of @entity56 response, compared with WT @entity19 . Our data show for the first time that Fel d 1 is a novel ligand of the @entity462 -rich domain of MR and that MR is likely to play a pivotal role in @entity56 sensitization to airborne allergens in vivo.
