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Immunobiological properties and structure analysis of group 13 allergen from Blomia tropicalis and its IgE-mediated cross-reactivity.
Zhou, Ying; Zhu, Keli; Li, Qingqing; Zhou, Dongmei; Ren, Yaning; Liao, Yuanfen; Cao, Peng; Gong, Yong; Cui, Yubao.
Afiliación
  • Zhou Y; Department of Pediatrics Laboratory, The Affiliated Wuxi Children's Hospital of Jiangnan University, Wuxi 214023, PR China.
  • Zhu K; Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, PR China.
  • Li Q; Clinical Research Center, The Affiliated Wuxi People's Hospital of Nanjing Medical University, Wuxi 214023, PR China.
  • Zhou D; Clinical Research Center, The Affiliated Wuxi People's Hospital of Nanjing Medical University, Wuxi 214023, PR China.
  • Ren Y; Clinical Research Center, The Affiliated Wuxi People's Hospital of Nanjing Medical University, Wuxi 214023, PR China.
  • Liao Y; Clinical Research Center, The Affiliated Wuxi People's Hospital of Nanjing Medical University, Wuxi 214023, PR China.
  • Cao P; Faculty of Environment and Life, Beijing University of Technology, Beijing, China.
  • Gong Y; Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, PR China. Electronic address: yonggong@ihep.ac.cn.
  • Cui Y; Clinical Research Center, The Affiliated Wuxi People's Hospital of Nanjing Medical University, Wuxi 214023, PR China. Electronic address: ybcui1975@hotmail.com.
Int J Biol Macromol ; 254(Pt 3): 127788, 2024 Jan.
Article en En | MEDLINE | ID: mdl-37926306
Blomia tropicalis is an important species of allergenic mite. Structurally related cross-reactive allergens are involved in pathogenesis of clinical symptoms. The present study focused on recombinant allergen rBlo t 13 from B. tropicalis, including investigation of its structure, immunological properties, IgE-mediated cross-reactivity. In this work, the prokaryotic expression plasmids pET-28(a)-Blo t 13, pET-28(a)-Der f 13, and pET-28(a)-Tyr p 13 were constructed, transformed into E. coli Rosetta (DE3) pLysS, and purified by nickel affinity chromatography, respectively. By using ELISA, the IgE-binding rates were detected for rBlo t 13 and its epitope peptides, as well as the cross-reactivity among rBlo t 13, rDer f 13, and rTyr p 13. The tertiary structure of rBlo t 13 was resolved using X-ray diffraction at 2.0 Å resolution. Using IgE-ELISA, the IgE binding rate of rBlo t 13 was 60 % with Blomia tropicalis-positive sera. In the experiments of ELISA for cross-reactivity with rBlo t 13 on solid phase, the inhibition rates were 65 %, 57 % and 63 % for rBlo t 13, rDer f 13, and rTyr p 13, respectively. The structure of Blo t 13 protein contains a ß-barrel structure which is composed of 10 ß strands and has 2 α helices at the end of the barrel. Comparison of the tertiary structures of rBlo t 13, rDer f 13, and rTyr p 13 revealed that the ß-barrel structure is highly conserved, consistent with the alignment of amino acid sequences. We obtained the recombinant protein rBlo t 13, demonstrated its cross-reactivity with Der f 13 and Tyr p 13 due to their structural similarity.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos / Ácaros Límite: Animals Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos / Ácaros Límite: Animals Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos