5 research outputs found

    Intestinal schistosomiasis in an apparently healthy rural population in Bayelsa State, Nigeria

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    Background: Schistosomiasis is endemic in Nigeria and three species; Schistosoma haematobium, Schistosoma mansoni, and Schistosoma intercalatum have been reported in Niger Delta, Nigeria. This study aimed to determine the prevalence of schistosomiasis in rural communities of Bayelsa State, Nigeria.Methodology: Four rural homogeneous communities; Otuegala, Immiringi, Otuesega, and Ibelebiri in Ogbia Local Government Area of Bayelsa State, Nigeria, were randomly selected for the study. A structured questionnaire was administered to each participant in their native language and used to collect participant’s biodata and swimming history. Stool samples collected from all participants were examined qualitatively by wet preparation and after formolethol concentration. Data were analyzed using SPSS version 20.0 software and results presented in proportion and tables.Results: A total of 829 participants (age range 1 - 80 years) were recruited for the study. Helminth ova were identified in the stool samples of 218 (26.3%) participants. Among 380 males examined, 82 (21.6%) were infected, while out of 449 females examined, 138 (30.3%) were infected. The ova of seven helminths identified and their frequency of occurrence were; S. intercalatum 86 (10.4%), Ascaris lumbricoides 53 (6.4%), S. mansoni 35 (4.2%), Trichuris trichiura 22 (2.6%), hookworm 20 (2.4%) and Taenia spp 2 (0.2%). Schistosoma haematobium was identified in non-urine contaminated stool sample of an eight-year old boy. A total of 11 (1.3%) participants had double infections, affecting 7 (63.6%) females and 4 (36.4%) males, with the commonest combination being S. intercalatum and A.lumbricoides 6 (0.7%), followed by S. intercalatum and hookworm 4 (0.5%), and S. mansoni and hookworm 1(0.1%).Conclusion: S. intercalatum was the most prevalent intestinal helminthic infection in this study, which is a rare finding in most epidemiological investigations. The affinity of Schistosoma species to establish double infections with hookworm and other intestinal helminths should be taken into account during chemoprophylaxis. Keywords: Schistosomiasis, Chemoprophylaxis, Prevalence, Rural Populatio

    The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein.

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    Members of the CAP superfamily (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins), also known as SCP superfamily (sperm-coating proteins), have been implicated in many physiological processes, including immune defenses, venom toxicity, and sperm maturation. Their mode of action, however, remains poorly understood. Three proteins of the CAP superfamily, Pry1, -2, and -3 (pathogen related in yeast), are encoded in the Saccharomyces cerevisiae genome. We have shown previously that Pry1 binds cholesterol in vitro and that Pry function is required for sterol secretion in yeast cells, indicating that members of this superfamily may generally bind sterols or related small hydrophobic compounds. On the other hand, tablysin-15, a CAP protein from the horsefly Tabanus yao, has been shown to bind leukotrienes and free fatty acids in vitro Therefore, here we assessed whether the yeast Pry1 protein binds fatty acids. Computational modeling and site-directed mutagenesis indicated that the mode of fatty acid binding is conserved between tablysin-15 and Pry1. Pry1 bound fatty acids with micromolar affinity in vitro, and its function was essential for fatty acid export in cells lacking the acyl-CoA synthetases Faa1 and Faa4. Fatty acid binding of Pry1 is independent of its capacity to bind sterols, and the two sterol- and fatty acid-binding sites are nonoverlapping. These results indicate that some CAP family members, such as Pry1, can bind different lipids, particularly sterols and fatty acids, at distinct binding sites, suggesting that the CAP domain may serve as a stable, secreted protein domain that can accommodate multiple ligand-binding sites
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