scholarly journals Identification of B Cell Epitopes of Blo t 13 Allergen and Cross-Reactivity with Human Adipocytes and Heart Fatty Acid Binding Proteins

2019 ◽  
Vol 20 (24) ◽  
pp. 6107 ◽  
Author(s):  
Marlon Múnera ◽  
Dalgys Martínez ◽  
Alexis Labrada ◽  
Luis Caraballo ◽  
Leonardo Puerta

Cross-reactivity between allergens and human proteins could have a clinical impact in allergic diseases. Blo t 13 is an allergen from the mite Blomia tropicalis, which belongs to the fatty acid binding protein (FABP) family and has structural homology with human FABPs. This work aimed to map B cell epitopes on Blo t 13 and to identify epitopes involved in cross-reactivity with human heart FABP (FABP3) and adipocyte FABP (FABP4). Sera from 25 patients with house dust mite (HDM) allergy that were sensitized to Blo t 13 were used for testing the reactivity of immunoglobulin E (IgE) and IgG to FABP. The epitope mapping of Blo t 13 was performed using overlapping peptides, and cross-reactivity between Blo t 13 and human FABP was analyzed using human sera and anti-Blo t 13 monoclonal antibodies. IgE antibodies to all FABPs were detected in 14/25 serum samples, and IgG was detected in 25/25 serum samples. The cross-reactivity of Blo t 13 was 42% with FABP3 and 48% with FABP4. Two IgE-binding regions were identified in Blo t 13; one between residues 54 and 72 (the main cross-reacting region) and another between residues 111 to 129. Our results suggest that exposure to the Blo t 13 allergen could induce an auto-reactive response to endogenous FABP in allergic patients sensitized to Blo t 13.

Parasitology ◽  
2010 ◽  
Vol 137 (12) ◽  
pp. 1805-1817 ◽  
Author(s):  
SUPATRA CHUNCHOB ◽  
RUDI GRAMS ◽  
VITHOON VIYANANT ◽  
PETER M. SMOOKER ◽  
SUKSIRI VICHASRI-GRAMS

SUMMARYFatty acid binding proteins are considered to be promising vaccine candidates against trematodiasis. In order to provide additional information about their function inFasciola giganticawe performed a comparative analysis of FgFABP1 and FgFABP3, two isoforms with quite different isoelectric points of 4·9 and 9·9 and 67% sequence identity. Both are expressed in the juvenile and adult parasite but differ in their tissue-specific distribution. In addition, the sequence of FABP3 is identical inF. hepaticaandF. giganticaindicating the protein's functional importance in this genus. Immune sera produced against soluble recombinant FgFABPs reacted with 14 kDa antigens in crude worm, soluble egg, cirrus sac extracts, and excretion/secretion product. Both FgFABPs were located in the parenchyma of the parasite but in addition, FgFABP1 was abundant in testes and spermatozoa while FgFABP3 was abundant in vitelline cells, eggs, and caecal epithelium. Mass spectrometry identified FgFABP1 and FgFABP3 in the ES product whereas only FgFABP3 was identified in egg extract. Serum samples of an experimentally infected rabbit reacted from week 6 post-infection with FgFABP3 and from week 12 with FgFABP1 while sera of infected sheep were not reactive. The results suggest differences in the biological functions of these 2 isoforms and differences in the host/parasite interaction that should be considered for their potential as vaccines against fascioliasis.


2021 ◽  
Author(s):  
Shivani Verma

Abstract In contemporary research, biological computational tools have emerged to play a pivotal role in facilitating both cost and time-efficient research. One such domain is addressing the prevailing food allergy issues, where these computational tools have been proven of vital importance. The present study is done as part of an internship at Jozbiz technologies. In the present study, we discuss the identification of IgE(Immunoglobulin E) binding allergy-causing B-Cell epitopes of macadamia (Macadamia integrifolia) allergens, namely AMP23_MACIN, AMP1_MACIN, AMP21_MACIN, MATK_MACIN and 11S1_MACIN. Using seven web servers (ABCPred, ElliPro, BepiPred 1.0b, BcePred, BCPred, CBTOPE and Disco Tope 2.0) twenty-one epitopes and seventeen conformational epitopes were predicted in the present study. The predicted epitopes are analysed in terms of residues having hydrophilicity, polar nature and having exposed surfaces. The unavailable 3-d structure of proteins was developed by homology modelling. Cross-reactivity of Macadamia integrifolia with other food items has also been listed.


1984 ◽  
Vol 259 (21) ◽  
pp. 13395-13401 ◽  
Author(s):  
P Brecher ◽  
R Saouaf ◽  
J M Sugarman ◽  
D Eisenberg ◽  
K LaRosa

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