A survey of urinary schistosomiasis among school aged children of ten communities in South-South, Nigeria.

Background & Objectives: Schistosomiasis is one of the major neglected tropical parasitic diseases caused by a group of blood-feeding worms in the genus Schistosoma. Nigeria ranks highest among all countries worldwide, however, there is a paucity of information on the prevalence of the disease in some parts of the country. Therefore, the research aims to augment available data on the prevalence of Schistosoma haematobium infection among schoolaged children in ten communities in Edo state, Nigeria.

Author Correction: Antigenic cross-reactivity between Schistosoma mansoni and allergenic invertebrates putatively due to shared glycanic epitopes.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Antigenic cross-reactivity between Schistosoma mansoni and allergenic invertebrates putatively due to shared glycanic epitopes.

Previous studies have shown that rabbit IgG antibodies against Schistosoma mansoni egg antigens (SmSEA) cross-react with allergens in natural rubber latex, peanuts and grass and tree pollens. Here we describe antigenic molecules that cross-react with rabbit anti-S. mansoni IgG antibodies in extracts of the house dust mite (HDM) Dermatophagoides farinae, the Australian cockroach (ACR) Periplaneta australasiae and in the venom of the honey bee Apis mellifera (HBV).

Antigenic cross-reactivity between Schistosoma mansoni and pollen allergens from the birch tree (Betula verrucosa) and Timothy grass (Phleum pratense): involvement of shared glycan epitopes and implications for the hygiene hypothesis.

Previous studies have shown that schistosome infection can protect against allergic symptoms, but the underlying mechanisms are still not fully understood. Here we have shown that rabbit IgG antibodies raised against Schistosoma mansoni soluble egg antigens (SmSEA) are cross-reactive with a wide array of molecules in Timothy grass pollen (TGP) and birch tree pollen (BTP). Five of the cross-reactive pollen molecules (two from TGP and three from BTP) were selected randomly and identified by tandem mass spectrometric (TMS) analysis to be, respectively, the TGP allergens Phl p 1 and Phl p 5b, and BTP glutathione S-transferase (GST), and the BTP allergens Bet v 1 and Bet v 6.

Treatment of Schistosoma mansoni with miltefosine in vitro enhances serological recognition of defined worm surface antigens.

Background: Miltefosine, an anti-cancer drug that has been successfully repositioned for treatment of Leishmania infections, has recently also shown promising effects against Schistosoma spp targeting all life cycle stages of the parasite. The current study examined the effect of treating Schistosoma mansoni adult worms with miltefosine on exposure of worm surface antigens in vitro.

Methodology/principal Findings: In an indirect immunofluorescence assay, rabbit anti-S.

Antigenic cross-reactivity between Schistosoma mansoni and peanut: a role for cross-reactive carbohydrate determinants (CCDs) and implications for the hygiene hypothesis.

The antigenic reactivity of constituents of Schistosoma mansoni and peanut (Arachis hypogaea) was investigated to determine whether identical antigenic epitopes possessed by both organisms provided a possible explanation for the negative correlation between chronic schistosome infection and atopy to allergens. Aqueous extracts of peanuts were probed in Western immunoblots with rabbit IgG antibodies raised against the egg, cercarial and adult worm stages of S. mansoni.

Cross-Reactivity between Schistosoma mansoni Antigens and the Latex Allergen Hev b 7: Putative Implication of Cross-Reactive Carbohydrate Determinants (CCDs).

IgG antibodies produced by rabbits immunized against S. mansoni antigens cross-reacted with aqueous soluble constituents of a variety of allergens. The antibody cross-reactivity was largely sensitive to degradation by treatment of the target antigens with sodium meta-periodate, suggesting the cross-reactivity was due to carbohydrate determinants that were common to both the schistosome and the allergens (CCDs).

Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase.

A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl-ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S.