Heliomaster squamosus
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ABSTRACT:
PROVIDER: PRJNA959593 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Polyporus squamosus CCBS 676 transcriptome - Ps
| PRJNA440081 | ENA
Project description:Polyporus squamosus CCBS 676 Standard Draft genome sequencing
| PRJNA444340 | ENA
Project description:Despite dramatic reductions in malaria cases in the catchment area of Macha Hospital, Choma District, Southern Province in Zambia, prevalence has remained near 1-2% by RDT for the past several years. To investigate residual malaria transmission in the area, this study focuses on the relative abundance, foraging behavior, and phylogenetic relationships of Anopheles squamosus specimens. In 2011, higher than expected rates of anthropophily were observed among "zoophilic" An. squamosus, a species that had sporadically been found to contain Plasmodium falciparum sporozoites. The importance of An. squamosus in the region was reaffirmed in 2016 when P. falciparum sporozoites were detected in numerous An. squamosus specimens. This study analyzed Centers for Disease Control (CDC) light trap collections of adult mosquitoes from two collection schemes: one performed as part of a reactive-test-and-treat program and the second performed along a geographical transect. Morphological identification, molecular verification of anopheline species, and blood meal source were determined on individual samples. Data from these collections supported earlier studies demonstrating An. squamosus to be primarily exophagic and zoophilic, allowing them to evade current control measures. The phylogenetic relationships generated from the specimens in this study illustrate the existence of well supported clade structure among An. squamosus specimens, which further emphasizes the importance of molecular identification of vectors. The primarily exophagic behavior of An. squamosus in these collections also highlights that indoor vector control strategies will not be sufficient for elimination of malaria in southern Zambia.
| S-EPMC7915044 | biostudies-literature
Project description:Anopheles squamosus, genomic and transcriptomic data
| PRJEB83526 | ENA
Project description:With ongoing global efforts to eliminate malaria, several countries have entered a pre-elimination stage, in which populations of the primary mosquito vector are reduced and the rates of malaria transmission are low. Efforts to eliminate malaria have changed the dynamics of disease transmission, causing a shift in anopheline community composition in some regions. One of the most abundant species of Anopheles found in pre-elimination areas, such as southern Africa, is Anopheles squamosus (Theobald, 1901; Diptera: Culicidae). Although An. squamosus has been documented across the African continent, limited information is available about its biology. Knowing what, when, and where the malaria vector bites humans can help develop effective malaria control strategies. The aim of this review is to compile the information available on An. squamosus's biology, ecology, distribution, behavior, and potential role in disease transmission. The review of current literature suggested that An. squamosus is abundant throughout the African continent. Studies indicate that this species occupies the same range and exhibits similar behaviors to primary malaria vectors in southern and eastern African countries, like Zambia. In conclusion, An. squamosus continues to be an understudied species that has circumvented disease control measures and further studies are needed to develop effective control strategies.
| S-EPMC11855103 | biostudies-literature
Project description:Lectin from the mushroom Polyporus squamosus (PSL) has a unique carbohydrate-binding specificity for sialylated glycoconjugates containing Neu5Acalpha2,6Galbeta1,4Glc/GlcNAc trisaccharide sequences of asparagine-linked glycoproteins. In the present study, we elucidate the molecular basis for its binding specificity as well as establish a consistent source of this useful lectin using a bacterial expression system. cDNA cloning revealed that PSL contains a ricin B chain-like (QXW)(3) domain at its N-terminus that is composed of three homologous subdomains (alpha, beta and gamma). A recombinant lectin was expressed in Escherichia coli as a fully active, soluble form. It agglutinated rabbit erythrocytes and showed the highest affinity for Neu5Acalpha2,6Galbeta1,4GlcNAc, but not for the sialyl alpha2,3-linked isomer. We also investigated the structure-function relationship of PSL. A monomeric C-terminal deletion mutant lacking 40% of the lectin's molecular mass retained sugar-binding activity, indicating that the carbohydrate-binding sites are situated in the N-terminal portion of the lectin, whereas the C-terminal portion probably functions in oligomerization and structural stabilization. Mutant constructs that have single amino acid substitutions in the putative sugar-binding sites, based on sequence alignment with the ricin B-chain, indicate that the beta and gamma subdomains are most probably sugar-binding sites. The recombinantly expressed lectin will be a valuable reagent for the detection of the Neu5Acalpha2,6Galbeta1,4GlcNAc sequence of asparagine-linked glycans.
| S-EPMC1133824 | biostudies-literature