1. Cockroach allergens and asthma in Brazil: Identification of tropomyosin as a major allergen with potential cross-reactivity with mite and shrimp allergens 
Ana Beatriz R. Santos, BSca, Martin D. Chapman, PhDf, Rob C. Aalberse, PhDe, Lisa D. Vailes, MSf, Virginia P.L. Ferriani, MDb, Constance Oliver, PhDc, M.Candida Rizzo, MDd, Charles K. Naspitz, MDd, L.Karla Arruda, MDa 
Journal of Allergy and Clinical Immunology 
Volume 104, Issue 2, Pages (August 1999)
DOI: /S (99)
Copyright © 1999 Mosby, Inc. Terms and Conditions

2. Fig. 1
Skin test reactivity to inhalant allergens among patients with asthma, rhinitis, or both living in Ribeirão Preto (A ) and São Paulo (B ). Patients were skin tested with extracts from D pteronyssinus (Dpt), D farinae (Df), Blomia tropicalis (Bt), B germanica (Bg), P americana (Pa), cat, dog, Alternaria species (Alt), Cladosporium species (Cla), Helminthosporium species (Hel), Aspergillus species (Asp), Penicillium species (Pen), and mold mix (ie, Curvularia, Fusarium, Mucor, Pullularia, and Rhizopus species). Forty-nine patients from Ribeirão Preto with negative skin prick test responses underwent intradermal skin testing. Positive reactions were defined as a wheal diameter of 4 × 4 mm or greater than that induced by the negative saline control accompanied by erythema and a wheal diameter of 6 × 6 mm or greater with erythema for prick and intradermal testing, respectively. The prevalence of positive skin prick test responses to B tropicalis, Aspergillus species, and mold mix was significantly higher in São Paulo compared with Ribeirão Preto, as indicated by asterisk (P < .01, P < .001, and P < .001, respectively).
Journal of Allergy and Clinical Immunology  , DOI: ( /S (99) )
Copyright © 1999 Mosby, Inc. Terms and Conditions

3. Fig. 2
Human IgE antibody binding to P americana allergen. Five clones were obtained after screening a P americana cDNA library with pooled IgE antibodies, and each clone was screened again by using individual sera from 53 patients and 4 nonallergic control individuals by plaque immunoassay. Sequence analysis revealed that the nucleotide sequences of the 5 clones were identical. Representative results in 5 patients allergic to cockroaches (RP 26, RP 29, RP 31, SP 29, and SP 34) and 1 nonallergic control subject (PRJ) tested against 4 of the 5 clones (clones pa 3, pa 8, pa 10 and pa 12) are shown.
Journal of Allergy and Clinical Immunology  , DOI: ( /S (99) )
Copyright © 1999 Mosby, Inc. Terms and Conditions

4. Fig. 3
Nucleotide and deduced amino acid sequence of P americana cDNA clone pa 12, encoding P americana tropomyosin allergen. The estimated molecular mass of P americana tropomyosin is 32,794 d. The initiation codon ATG is in bold, and the stop codon TAA is indicated with an asterisk (*). No potential N-linked glycosylation sites were identified.
Journal of Allergy and Clinical Immunology  , DOI: ( /S (99) )
Copyright © 1999 Mosby, Inc. Terms and Conditions

5. Fig. 4
Sequence alignment of cockroach tropomyosin and tropomyosins from mites and shrimp. Amino acid sequences of D pteronyssinus (GenBank Y14906), D farinae (D17682), and shrimp (Metapenaeus ensis, U08008) tropomyosins showed 80%, 81%, and 82% identity to cockroach (P americana, AF ) tropomyosin, respectively. The signature pattern for tropomyosins L-K-E-A-E-x-R-A-E, indicated in bold, is conserved in the C-terminal section of cockroach tropomyosin, and the highly conserved N-terminal motif DAIKKK (EAIKKK), which contributes to binding to actin, is underlined.
Journal of Allergy and Clinical Immunology  , DOI: ( /S (99) )
Copyright © 1999 Mosby, Inc. Terms and Conditions

6. Fig. 5
Unfixed frozen sections of cockroach. A, Section immunostained with mAb 1A6, anti-D pteronyssinus tropomyosin, is shown. The muscle fibers are positive for tropomyosin. The striations in the leg muscle (arrow) are apparent (magnification, ×150). B, Section immunostained with mAb 1A6 is shown. At a higher magnification, the banding pattern typical of striated skeletal muscle is apparent (magnification, ×300). C, Section stained with mAb 1D8, anti-Der p 2, is shown. The exoskeleton (arrow) is autofluorescent (magnification, × 50). Control sections stained with unrelated antibodies or stained without the primary antibody did not show fluorescence, except for cockroach exoskeleton autofluorescence.
Journal of Allergy and Clinical Immunology  , DOI: ( /S (99) )
Copyright © 1999 Mosby, Inc. Terms and Conditions