| Yang Cheng | 3 Articles |
Members of genus Acanthamoeba are widely distributed in the environment. Some are pathogenic and cause keratitis and fatal granulomatous amoebic encephalitis. In this study, we isolated an Acanthamoeba CJW/W1 strain from tap water in Wuxi, Jiangsu Province, China. Its 18S rDNA was sequenced and a phylogenetic tree was constructed. The isolated cysts belonged to morphologic group II. Comparison of 18S rDNA sequences of CJW/W1 strain and other isolates showed high similarity (99.7%) to a clinical isolate Asp, KA/E28. A phylogeny analysis confirmed this isolate belonged to the pathogenic genotype T4, the most common strain associated with Acanthamoeba-related diseases. This is the first report of an Acanthamoeba strain isolated from tap water in Wuxi, China. Acanthamoeba could be a public health threat to the contact lens wearers and, therefore, its prevalence should be monitored.
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Plasmodium vivax produces numerous caveola-vesicle complex (CVC) structures beneath the membrane of infected erythrocytes. Recently, a member helical interspersed subtelomeric (PHIST) superfamily protein, PcyPHIST/CVC-8195, was identified as CVCs-associated protein in Plasmodium cynomolgi and essential for survival of this parasite. Very little information has been documented to date about PHIST/CVC-8195 protein in P. vivax. In this study, the recombinant PvPHIST/CVC-8195 N and C termini were expressed, and immunoreactivity was assessed using confirmed vivax malaria patients sera by protein microarray. The subcellular localization of PvPHIST/CVC-8195 N and C termini in blood stage parasites was also determined. The antigenicity of recombinant PvPHIST/CVC-8195 N and C terminal proteins were analyzed by using serum samples from the Republic of Korea. The results showed that immunoreactivities to these proteins had 61% and 43% sensitivity and 96.9% and 93.8% specificity, respectively. The N terminal of PvPHIST/CVC-8195 which contains transmembrane domain and export motif (PEXEL; RxLxE/Q/D) produced CVCs location throughout the erythrocytic-stage parasites. However, no fluorescence was detected with antibodies against C terminal fragment of PvPHIST/CVC-8195. These results suggest that the PvPHIST/CVC-8195 is localized on the CVCs and may be immunogenic in natural infection of P. vivax.
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Malaria, caused by Plasmodium species, remains a major global health burden. The spleen is the central organ for clearance of infected red blood cells and regulation of immunity, yet paradoxically also serves as a site of parasite sequestration. Splenic fibroblasts may contribute to this process through adhesion mechanisms, but their role remains poorly defined. This study investigated P. yoelii tryptophan-rich antigen 7 (PyTRAg7), a member of the TRAg protein family, in splenic parasite–host interactions. TRAgs constitute a conserved protein family present in multiple Plasmodium species, including human malaria parasites, suggesting the relevance of PyTRAg7-associated mechanisms to human infection. Using protein binding assays and gene-edited parasites, PyTRAg7 was shown to interact with vimentin on mouse splenic fibroblasts, activating NF-κB p65 signaling and increasing ICAM-1 and integrin β1 expression. Deletion of PyTRAg7 reduced infected red blood cells adhesion to mouse splenic fibroblasts, lowered splenic parasite burden, delayed parasitemia onset, and prolonged host survival. Histological analysis showed preserved splenic architecture and reduced hemozoin deposition in the absence of PyTRAg7. The murine P. yoelii model was used due to its genetic tractability and its suitability for dissecting spleen-dependent sequestration mechanisms not easily studied in human malaria parasites. These findings identify PyTRAg7 as a key mediator of fibroblast–parasite interactions that promote cytoadherence and splenic remodeling, offering a potential target for malaria intervention.
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