The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.

Fusarium species are among airborne fungi and recognized as causative agents of human atopic disorders. However, Fusarium allergens have not been well characterized and the lack of information limits clinical diagnosis and treatment of fungal allergy. The purpose of this study is to identify and cha...

Full description

Bibliographic Details
Main Authors: Hong Chou, Keh-Gong Wu, Chang-Ching Yeh, Hsiao-Yun Tai, Ming F Tam, Yu-Sen Chen, Horng-Der Shen
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4116196?pdf=render
_version_ 1818940848947068928
author Hong Chou
Keh-Gong Wu
Chang-Ching Yeh
Hsiao-Yun Tai
Ming F Tam
Yu-Sen Chen
Horng-Der Shen
author_facet Hong Chou
Keh-Gong Wu
Chang-Ching Yeh
Hsiao-Yun Tai
Ming F Tam
Yu-Sen Chen
Horng-Der Shen
author_sort Hong Chou
collection DOAJ
description Fusarium species are among airborne fungi and recognized as causative agents of human atopic disorders. However, Fusarium allergens have not been well characterized and the lack of information limits clinical diagnosis and treatment of fungal allergy. The purpose of this study is to identify and characterize important allergens of F. proliferatum. IgE-reacting F. proliferatum components were identified by immunoblot using serum samples from patients of respiratory atopic diseases. Characterization of allergens and determination of IgE cross-reactivity were performed by cDNA cloning, then homologous expression and immunoblot inhibition studies. We identified nine different F. proliferatum components that can be recognized by IgE antibodies in 17 (28%) of the 60 atopic sera tested. Components with molecular masses of about 43, 37.5 and 36.5 kDa with IgE-binding frequencies of about 88, 47 and 53%, respectively, were considered as important allergens of F. proliferatum. The 37.5 kDa IgE-binding component was putatively considered as a transaldolase protein of F. proliferatum. The full-length cDNA of F. proliferatum transaldolase was subsequently cloned. It encodes an open reading frame of 312 amino acids and has sequence identifies of 73 and 61%, respectively, with Cladosporium and human transaldolases. The purified recombinant F. proliferatum transaldolase can inhibit the IgE-binding against the 37.5 kDa component of F. proliferatum and the transaldolase allergen from Cladosporium cladosporioides. More importantly, the recombinant F. proliferatum transaldolase can inhibit IgE-binding against human transaldolase in a concentration-dependent manner. Thus, a novel and important F. proliferatum transaldolase allergen was identified. In addition to IgE cross-reactivity between the Fusarium and the Cladosporium transaldolase allergens, IgE cross-reactivity between the Fusarium and the human transaldolases also exists and might contribute to atopic manifestations in the absence of exogenous allergen exposure.
first_indexed 2024-12-20T06:46:10Z
format Article
id doaj.art-a013948734ff40048d303d40ebb693ba
institution Directory Open Access Journal
issn 1932-6203
language English
last_indexed 2024-12-20T06:46:10Z
publishDate 2014-01-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS ONE
spelling doaj.art-a013948734ff40048d303d40ebb693ba2022-12-21T19:49:41ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0197e10348810.1371/journal.pone.0103488The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.Hong ChouKeh-Gong WuChang-Ching YehHsiao-Yun TaiMing F TamYu-Sen ChenHorng-Der ShenFusarium species are among airborne fungi and recognized as causative agents of human atopic disorders. However, Fusarium allergens have not been well characterized and the lack of information limits clinical diagnosis and treatment of fungal allergy. The purpose of this study is to identify and characterize important allergens of F. proliferatum. IgE-reacting F. proliferatum components were identified by immunoblot using serum samples from patients of respiratory atopic diseases. Characterization of allergens and determination of IgE cross-reactivity were performed by cDNA cloning, then homologous expression and immunoblot inhibition studies. We identified nine different F. proliferatum components that can be recognized by IgE antibodies in 17 (28%) of the 60 atopic sera tested. Components with molecular masses of about 43, 37.5 and 36.5 kDa with IgE-binding frequencies of about 88, 47 and 53%, respectively, were considered as important allergens of F. proliferatum. The 37.5 kDa IgE-binding component was putatively considered as a transaldolase protein of F. proliferatum. The full-length cDNA of F. proliferatum transaldolase was subsequently cloned. It encodes an open reading frame of 312 amino acids and has sequence identifies of 73 and 61%, respectively, with Cladosporium and human transaldolases. The purified recombinant F. proliferatum transaldolase can inhibit the IgE-binding against the 37.5 kDa component of F. proliferatum and the transaldolase allergen from Cladosporium cladosporioides. More importantly, the recombinant F. proliferatum transaldolase can inhibit IgE-binding against human transaldolase in a concentration-dependent manner. Thus, a novel and important F. proliferatum transaldolase allergen was identified. In addition to IgE cross-reactivity between the Fusarium and the Cladosporium transaldolase allergens, IgE cross-reactivity between the Fusarium and the human transaldolases also exists and might contribute to atopic manifestations in the absence of exogenous allergen exposure.http://europepmc.org/articles/PMC4116196?pdf=render
spellingShingle Hong Chou
Keh-Gong Wu
Chang-Ching Yeh
Hsiao-Yun Tai
Ming F Tam
Yu-Sen Chen
Horng-Der Shen
The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.
PLoS ONE
title The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.
title_full The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.
title_fullStr The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.
title_full_unstemmed The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.
title_short The transaldolase, a novel allergen of Fusarium proliferatum, demonstrates IgE cross-reactivity with its human analogue.
title_sort transaldolase a novel allergen of fusarium proliferatum demonstrates ige cross reactivity with its human analogue
url http://europepmc.org/articles/PMC4116196?pdf=render
work_keys_str_mv AT hongchou thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT kehgongwu thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT changchingyeh thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT hsiaoyuntai thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT mingftam thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT yusenchen thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT horngdershen thetransaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT hongchou transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT kehgongwu transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT changchingyeh transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT hsiaoyuntai transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT mingftam transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT yusenchen transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue
AT horngdershen transaldolaseanovelallergenoffusariumproliferatumdemonstratesigecrossreactivitywithitshumananalogue