Browsing by MeSH term "Gene Library"
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Publication Identification of small molecules capable of enhancing viral membrane fusion(BioMed Central (BMC), 2023-05-24) García-Murria, Mª Jesús; Gadea-Salom, Laura; Moreno, Sandra; Rius-Salvador, Marina; Zaragoza, Oscar; Brun, Alejandro; Mingarro, Ismael; Martínez-Gil, Luis; Generalitat Valenciana (España); Ministerio de Ciencia e Innovación (España); Unión Europea. Comisión Europea. H2020; Agencia Estatal de Investigación (España)Several approaches have been developed to analyze the entry of highly pathogenic viruses. In this study, we report the implementation of a Bimolecular Multicellular Complementation (BiMuC) assay to safely and efficiently monitor SARS-CoV-2 S-mediated membrane fusion without the need for microscopy-based equipment. Using BiMuC, we screened a library of approved drugs and identified compounds that enhance S protein-mediated cell-cell membrane fusion. Among them, ethynylestradiol promotes the growth of SARS-CoV-2 and Influenza A virus in vitro. Our findings demonstrate the potential of BiMuC for identifying small molecules that modulate the life cycle of enveloped viruses, including SARS-CoV-2.Publication Initial characterization of Pf62, a novel protein of Plasmodium falciparum identified by immunoscreening(Deutsche Gesellschaft für Parasitologie (DGP), 2009-06) Moyano, Eva M; Gonzalez, Luis Miguel; Montero-Clemente, Estrella; Cuevas, Laureano; Perez-Pastrana, Esperanza; Santa-María, Ysmael; Benito, Agustin; Instituto de Salud Carlos IIIIn order to find new antigens from Plasmodium falciparum, a complementary DNA (cDNA) library was constructed and screened. The study of expression library of P. falciparum was performed in an attempt to identify new antigens that could have potential relevance for the falciparum-malaria diagnosis and/or protection. Between the positive clones detected (ring erythrocyte surface antigen, merozoite erythrocyte surface antigen, RHOP H3, CSP, LSA), a new gene that correspond to a new protein (Pf62) was isolated and characterized. This antigen was useful for the diagnosis of malaria in enzyme-linked immunosorbent assay tests. The cDNA corresponding to this antigen and structure of the gene were characterized. Pf62 is a single copy gene that contains one exon. The Pf62 cDNA has an open reading frame of 1,599 nucleotides that code for a putative protein of 532 amino acids with a predicted molecular mass of 62 kDa. The polypeptide contains in the central section two regions of repeats of 21 and 19 amino acids, respectively. The localization of the Pf62 protein was performed by immunoblot, indirect immunofluorescence assay and immunoelectron microscopy. Pf62 is localized in the cytoplasm of the parasite and also on the surface of the infected erythrocyte. Serologic assays by using synthetic peptides designed from different antigenic regions of the Pf62 protein resulted in acceptable data of sensitivity and specificity in symptomatic malaria patients.Publication Molecular and immunogenic properties of apyrase SP01B and D7-related SP04 recombinant salivary proteins of Phlebotomus perniciosus from Madrid, Spain(Hindawi, 2013) Martin-Martin, Ines; Molina, Ricardo; Jimenez, Maribel; Ministerio de Ciencia e Innovación (España); Unión EuropeaSand fly salivary proteins are on the spotlight to become vaccine candidates against leishmaniasis and to markers of exposure to sand fly bites due to the host immune responses they elicit. Working with the whole salivary homogenate entails serious drawbacks such as the need for maintaining sand fly colonies and the laborious task of glands dissection. In order to overcome these difficulties, producing recombinant proteins of different vectors has become a major task. In this study, a cDNA library was constructed with the salivary glands of Phlebotomus perniciosus from Madrid, Spain, the most widespread vector of Leishmania infantum in the Mediterranean basin. Analysis of the cDNA sequences showed several polymorphisms among the previously described salivary transcripts. The apyrase SP01B and the D7-related protein SP04 were successfully cloned, expressed in Escherichia coli, and purified. Besides, recombinant proteins were recognized by sera of hamsters and mice previously immunized with saliva through the exposure to uninfected sand fly bites. These results suggest that these two recombinant proteins conserved their immunogenic properties after expression in a prokaryote system. Therefore, this work contributes to expand the knowledge of P. perniciosus saliva that would be eventually used for the development of tools for vector control programs.