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Tyrophagus putrescentiae group 4 allergen allergenicity and epitope prediction.
Teng, F-X; Huang, H-F; Ge, D-Z; Yu, L-L; Xu, C; Cui, Y-B.
Afiliación
  • Teng FX; Department of Basic Medicine, Jiangsu Vocational College of Medicine, Yancheng, Jiangsu 224005, China.
  • Huang HF; Department of Dermatology, Wuxi People's Hospital Affiliated to Nanjing Medical University, Wuxi, Jiangsu 214023, China.
  • Ge DZ; Department of Internal Medicine, The University of Iowa, Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA 52246, United States.
  • Yu LL; Department of Basic Medicine, Jiangsu Vocational College of Medicine, Yancheng, Jiangsu 224005, China.
  • Xu C; Department of Internal Medicine, The University of Iowa, Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA 52246, United States.
  • Cui YB; Department of Clinical Laboratory, Wuxi People's Hospital Affiliated to Nanjing Medical University, Wuxi, Jiangsu 214023, China. Electronic address: ybcui1975@hotmail.com.
Allergol Immunopathol (Madr) ; 48(6): 619-625, 2020.
Article en En | MEDLINE | ID: mdl-32418775
INTRODUCTION AND OBJECTIVES: Allergen-specific immunotherapy (ASIT) is the only allergic disease-modifying therapy available for children and adults, and recombinant allergens are an interesting approach to improve allergy diagnosis and ASIT. Tyrophagus putrescentiae is a common storage mite that produces potent allergens. The aim of this study was to express and characterize recombinant group 4 allergen protein of T. putrescentiae (Tyr p 4), and to further investigate allergenicity and potential epitopes of Tyr p 4. MATERIALS AND METHODS: The cDNA encoding Tyr p 4 was generated by RT-PCR and subcloned into pET-28a(+) plasmid. The plasmid was then transformed into E. coli cells for expression. After purification by nickel affinity chromatography and identification by SDS-PAGE, recombinant Tyr p 4 protein was used for a skin prick test and an ELISA to determine the allergic response. RESULTS: Study participants' allergic response rate to Tyr p 4 protein was 13.3% (16/120). Eight B-cell epitopes and three T-cell epitopes of Tyr p 4 were predicted. CONCLUSIONS: Similar to group 4 allergens of other species of mite, allergenicity of Tyr p 4 is weak. The expression, characterization and epitope prediction of recombinant Tyr p 4 protein provide a foundation for further study of this allergen in the diagnosis and ASIT of storage mite allergy.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos / Desensibilización Inmunológica / Acaridae / Proteínas de Artrópodos / Hipersensibilidad Límite: Adult / Animals / Female / Humans / Male / Middle aged Idioma: En Revista: Allergol Immunopathol (Madr) Año: 2020 Tipo del documento: Article País de afiliación: China Pais de publicación: Singapur

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos / Desensibilización Inmunológica / Acaridae / Proteínas de Artrópodos / Hipersensibilidad Límite: Adult / Animals / Female / Humans / Male / Middle aged Idioma: En Revista: Allergol Immunopathol (Madr) Año: 2020 Tipo del documento: Article País de afiliación: China Pais de publicación: Singapur