A. Pomes et al., NOVEL ALLERGEN STRUCTURES WITH TANDEM AMINO-ACID REPEATS DERIVED FROMGERMAN AND AMERICAN COCKROACH, The Journal of biological chemistry, 273(46), 1998, pp. 30801-30807
Cockroaches produce potent allergens that are an important cause of as
thma. The two principal domiciliary cockroach species, Blattella germa
nica and Periplaneta americana, secrete major allergens, Bla g 1 and P
er a 1. Here, we report the molecular cloning of three Bla g 1 cDNA cl
ones, which showed 70% amino acid sequence identity with Per a 1. Plaq
ue immunoassays with human IgE antibodies or murine monoclonal antibod
ies showed that these allergens were antigenically cross-reactive. The
Bla gl sequences also showed homology to five previously undefined co
ckroach allergen sequences. An unusual feature of all these sequences
was that they contained multiple tandem amino acid repeats of similar
to 100 amino acid residues. Between one and seven repeat units were id
entified by dot-plot matrix analysis. The sequences also showed homolo
gy to a mosquito protein involved in digestion (ANG12 precursor) and t
o mitochondrial energy transfer proteins. High levels of Bla g 1 were
found in cockroach hindgut and proventriculus. Amino acid sequencing o
f natural Ela g 1 and Per a 1 suggested that these allergens are cleav
ed by trypsin-like enzymes following secretion into the digestive trac
t. The repeat sequences appear to have evolved by duplication of an an
cestral amino acid domain, which may have arisen from the mitochondria
l energy transfer proteins.