BACKGROUND: Allergic reactions to house dust mites of the genus Dermatophagoides play an important role in the pathogenesis of asthma and other atopic diseases. Dermatophagoides siboney has been described as a species from Cuba. Together with D. pteronyssinus and Blomia tropicalis, it is frequently found in house dust from homes of asthmatics. OBJECTIVES: The aim of this study was to investigate the allergenic composition from the house dust mite D. siboney. METHODS: The characterization of D. siboney extract was performed by SDS-gPAGE and immunoblotting. Purification of individual components was performed by affinity chromatography. RESULTS: At least 16 components between 13 and 98 kDa stained by Coomassie Blue were found. Using a panel of 35 sera from atopic mite sensitive patients 13 components reacted to different extent with patient IgE. Two components, 25 and 14 kDa, bound to specific IgE strongly and frequently, i.e. 80 and 91% of the patients, respectively. Affinity chromatography using crossreacting monoclonal antibodies to group 1 and 2 allergens resulted in purified preparations of 25 and 14 kDa proteins, which showed IgE-binding with the majority of the human sera when tested by immuno-dot. CONCLUSION: Based on the IgE binding profile of D. siboney and on the capacity to react with crossreacting monoclonal antibodies for groups 1 and 2, it is proposed to name these two allergens, 25 and 14 kDa, Der s 1 and Der s 2, respectively.
BACKGROUND: Allergic reactions to house dust mites of the genus Dermatophagoides play an important role in the pathogenesis of asthma and other atopic diseases. Dermatophagoides siboney has been described as a species from Cuba. Together with D. pteronyssinus and Blomia tropicalis, it is frequently found in house dust from homes of asthmatics. OBJECTIVES: The aim of this study was to investigate the allergenic composition from the house dust mite D. siboney. METHODS: The characterization of D. siboney extract was performed by SDS-gPAGE and immunoblotting. Purification of individual components was performed by affinity chromatography. RESULTS: At least 16 components between 13 and 98 kDa stained by Coomassie Blue were found. Using a panel of 35 sera from atopic mite sensitive patients 13 components reacted to different extent with patient IgE. Two components, 25 and 14 kDa, bound to specific IgE strongly and frequently, i.e. 80 and 91% of the patients, respectively. Affinity chromatography using crossreacting monoclonal antibodies to group 1 and 2 allergens resulted in purified preparations of 25 and 14 kDa proteins, which showed IgE-binding with the majority of the human sera when tested by immuno-dot. CONCLUSION: Based on the IgE binding profile of D. siboney and on the capacity to react with crossreacting monoclonal antibodies for groups 1 and 2, it is proposed to name these two allergens, 25 and 14 kDa, Der s 1 and Der s 2, respectively.