Abstract
The cDNA coding for group 1 allergen of adult Dermatophagoides farinae (Hughes) (Acari: Pyroglyphidae) from China was cloned, sequenced and expressed successfully. Sequence analysis showed the presence of an open reading frame containing 966 bp that encodes a protein of 321 amino acids. Through bioinformatics analyses, the hydrophobic protein was demonstrated to be likely extracellular, with a cleavage site between positions 18 and 19. Interestingly, homology analysis showed that the Der f 1 shared greater than 88% identity in amino acid sequence with Eur m 1 but only 77% with Der p 1. Phylogenetic analyses suggested that D. farinae was evolutionarily closer to Euroglyphus maynei (Cooreman) than to Dermatophagoides pteronyssinus (Trouessart), even though D. pteronyssinus and D. farinae belong to the same genus Dermatophagoides. A total of three cysteine peptidase active sites were found in the predicted amino acid sequence, including 127–138 (QGGCGSCWAFSG), 267–277 (NYHAVNIV GYG) and 284–303 (YWIVRNSWDTTWGDSGYGYF). Moreover, secondary structure analysis revealed that Der f 1 from China contained an alpha helix (34%), an extended strand (17%), a beta turn (6%), and a random coil (43%). A simple three-dimensional model of this protein was constructed using SWISS- MODEL server.
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