Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana

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Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana

The American cockroach, Periplaneta americana, is a vector of many pathogenic organisms associated with human diseases. Olfaction plays a crucial role in guiding cockroach behaviors and contributes to their ability to transmit pathogens. Odorant binding proteins (OBPs), abundant in the insect olfactory sensilla, are important for insect olfaction. In this study, three OBP genes, PameOBP1, 2 and...

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Characterization of recombinant per a 10 from Periplaneta americana.

Cockroach allergen is a major risk factor for IgE-mediated allergic response and asthma in sensitized individuals. Serine proteases have been identified from various sources and characterized as major allergens. The present study was aimed to express and characterize recombinant allergen Per a 10 (rPer a 10) from Periplaneta americana. rPer a 10 was expressed in Escherichia coli and purified in...

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Aedes albopictus is a major vector of dengue and Chikungunya viruses. Olfaction plays a vital role in guiding mosquito behaviors and contributes to their ability to transmit pathogens. Odorant-binding proteins (OBPs) are abundant in insect olfactory tissues and involved in the first step of odorant reception. While comprehensive descriptions are available of OBPs from Aedes aegypti, Culex quinq...

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isolation and purification of an antibacterial protein from immune induced haemolymph of american cockroach, periplaneta americana

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Molecular characterization of American cockroach tropomyosin (Periplaneta americana allergen 7), a cross-reactive allergen.

Inhalation of allergens produced by the American cockroach (Periplaneta americana) induces IgE Ab production and the development of asthma in genetically predisposed individuals. The cloning and expression in Escherichia coli of P. americana tropomyosin allergen have been achieved. The protein shares high homology with other arthropod tropomyosins (80% identity) but less homology with vertebrat...

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ژورنال

عنوان ژورنال: PLOS ONE

سال: 2017

ISSN: 1932-6203

DOI: 10.1371/journal.pone.0170072