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Evaluation of a di‐ O ‐methylated glycan as a potential antigenic target for the serodiagnosis of human toxocariasis
Author(s) -
Elefant G. R.,
Roldán W. H.,
Seeböck A.,
Kosma P.
Publication year - 2016
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/pim.12311
Subject(s) - toxocariasis , toxocara canis , antigen , glycan , biology , antibody , immunology , epitope , serology , cross reactivity , helminths , microbiology and biotechnology , glycoprotein , cross reactions
Summary Serodiagnosis of human toxocariasis is based on the detection of specific IgG antibodies by the enzyme‐linked immunosorbent assay ( ELISA ) using Toxocara larvae excretory–secretory ( TES ) antigens, but its production is a laborious and time‐consuming process being also limited by the availability of adult females of T. canis as source for ova to obtain larvae. Chemical synthesis of the di‐ O ‐methylated (DiM) glycan structure found in the TES antigens has provided material for studying the antibody reactivity in a range of mammalian hosts, showing reactivity with human IgM and IgG. In this study, we have evaluated the performance of the DiM glycan against a panel of sera including patients with toxocariasis ( n = 60), patients with other helminth infections ( n = 75) and healthy individuals ( n = 94), showing that DiM is able to detect IgG antibodies with a sensitivity and specificity of 91·7% and 94·7%, respectively, with a very good agreement with the TES antigens (kappa = 0·825). However, cross‐reactivity was observed in some sera from patients with ascariasis, hymenolepiasis and fascioliasis. These results show that the DiM glycan could be a promising antigenic tool for the serodiagnosis of human toxocariasis.