IgE cross-reactivity between house dust mite allergens and Ascaris lumbricoides antigens
10.5415/apallergy.2012.2.1.35
- Author:
Gardette R VALMONTE
1
;
Gil A CAUYAN
;
John Donnie A RAMOS
Author Information
1. Department of Biological Sciences, College of Science, University of Santo Tomas, Manila 1015, Philippines. gvalmonte@mnl.ust.edu.ph
- Publication Type:Original Article
- Keywords:
Atopy;
Immunity;
Infection;
Paramyosin;
Parasitism
- MeSH:
Allergens;
Ascariasis;
Ascaris lumbricoides;
Ascaris;
Dermatophagoides farinae;
Dermatophagoides pteronyssinus;
Dust;
Enzyme-Linked Immunosorbent Assay;
Helminths;
Humans;
Immunoglobulin E;
Mites;
Parasites;
Pyroglyphidae;
Tropomyosin
- From:
Asia Pacific Allergy
2012;2(1):35-44
- CountryRepublic of Korea
- Language:English
-
Abstract:
BACKGROUND: Common antigens between intestinal parasites and environmental allergens may play a role in the modulation of allergic immune responses. There is a growing interest in investigating cross-reactivity between common helminths and dust mites affecting humans, particularly in the tropics. OBJECTIVE: This study examined the cross-reactivity between the human roundworm Ascaris lumbricoides (Al) and three house dust mite (HDM) species. METHODS: Specific serum IgE levels to HDM species Blomia tropicalis (Bt), Dermatophagoides pteronyssinus (Dp), and Dermatophagoides farinae (Df ); and Al extracts among allergic (n=100) and ascariasis (n=60) subjects were measured through enzyme-linked immunosorbent assay (ELISA). IgE-reactive components of HDM and Al extracts were detected through Western-Blot Analysis. Cross-reactivity between HDMs and Al was determined by ELISA inhibition using HDM and Al-specific sera from allergic (n=15) and ascariasis (n=15) subjects. The IgE-binding capacity of a recombinant paramyosin peptide (Blo t 11-fD) to allergic (n=50) and ascariasis (n=50) subjects' sera were likewise determined. RESULTS: Among allergic subjects, 70% exhibited Al-specific positive IgE-reactivity, while 20-28% of ascariasis subjects demonstrated HDM-specific positive IgE-reactivity. Multiple IgE-reactive components of HDM allergens (14-240 kDa) and Al antigens (15-250 kDa) were detected, indicating multi-allergen sensitization among the subjects tested. Al antigens can inhibit up to 92% of HDM-specific IgE-reactivity among allergic subjects, while up to 54% of Al-specific IgE-reactivity among ascariasis subjects was inhibited by HDM allergens. Positive rBlo t 11-fD-specific IgE reactivity was observed in 80% of the allergic subjects and 46% of the ascariasis subjects. CONCLUSIONS: This study showed the presence of multiple cross-reactive antigens in HDM and Al extracts. Identification of these molecules may provide basis for designing novel diagnostic and therapeutic strategies. The potential role of paramyosin as a specific cross-reactive allergen present in HDMs and Al has been shown.
