Angiostrongyliasis is a food-borne parasitic disease caused by the nematode that can lead to eosinophilic meningitis (EM) or meningoencephalitis in humans. is prevalent in the Pacific Islands. In recent years, a large number of outbreaks and severe cases have occurred. Several species of mollusk, such as snails and slugs, act as intermediate and paratenic hosts of . In this study, two cases of EM were found to have been caused by infection with due to consumption of raw centipedes. To survey the infections acquired through centipedes that the patients had bought at a vegetable market, we performed etiological examinations and polymerase chain reaction amplification of genes. Third-instar larvae of were detected in the centipedes, and specific genes from were detected in all the specimens. This indicates that the centipede may act as a competent host for the transmission of . To our knowledge, this is the first report of infection through the consumption of centipedes.
This study suggested a critical role of miRNAs in the host defense during A. cantonensis infection, providing new insights into the molecular mechanisms underlying the interaction between mmu-miR-146a-5p and TNF-α in angiostrongyliasis in nonpermissive hosts.
Angiostrongylus cantonensis infection can lead to severe neuropathological damage caused by the development of these nematodes in the central nervous system after penetrating the blood-brain barrier. They commonly cause eosinophilic meningitis or meningoencephalitis in non-permissive hosts (e.g., mice). It has been shown that differences exist in the brains of permissive and non-permissive hosts during the larval development of A. cantonensis; however, the mechanism underlying the difference is not completely understood. This study analyzed and characterized the differentially expressed proteins in the intracranial A. cantonensis larvae in rat (ILR) and mouse (ILM) brains by using proteomics. We found that 29 proteins were differentially expressed: 12 of these proteins were highly expressed in ILR, whereas the remaining 17 proteins were highly expressed in ILM. Three protein spots were homologous to the actin-2, actin-1, and disorganized muscle protein 1 (dim-1) of Caenorhabditis elegans. In addition, proteomic analyses revealed that act-1 and act-2 were up-regulated in ILM compared to ILR, whereas dim-1 was down-regulated in ILM. Annotation using gene ontology revealed that act-1, act-2, and dim-1 were mainly associated with adenosine triphosphate (ATP) catabolic processes and ATP binding. Quantitative real-time polymerase chain reaction analyses of act-1 and dim-1 using the first internal transcribed spacers of A. cantonensis 18S ribosomal RNA (rRNA) was consistent with 2-dimensional gel electrophoresis (2-DE) and the sizes of these parasites; ILR was longer and wider than ILM. These results indicate that the differentially expressed proteins dim-1 and act-1 could be related to the development and pathogenicity of A. cantonensis in different hosts.
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