Examinando por Autor "Valenzuela, Pablo D.T."

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    Complete sequence of the genome of the human isolate of Andes virus CHI-7913: comparative sequence and protein structure analysis
    (Sociedad de Biología de Chile, 2003) Tischler, Nicole D.; Fernández, Jorge; Müller, Ilse; Martínez, Rodrigo; Galeno, Héctor; Villagra, Eliecer; Mora, Judith; Ramírez, Eugenio; Rosemblatt, Mario; Valenzuela, Pablo D.T.
    We report here the complete genomic sequence of the Chilean human isolate of Andes virus CHI-7913. The S, M, and L genome segment sequences of this isolate are 1,802, 3,641 and 6,466 bases in length, with an overall GC content of 38.7%. These genome segments code for a nucleocapsid protein of 428 amino acids, a glycoprotein precursor protein of 1,138 amino acids and a RNA-dependent RNA polymerase of 2,152 amino acids. In addition, the genome also has other ORFs coding for putative proteins of 34 to 103 amino acids. The encoded proteins have greater than 98% overall similarity with the proteins of Andes virus isolates AH-1 and Chile R123. Among other sequenced Hantavirus, CHI-7913 is more closely related to Sin Nombre virus, with an overall protein similarity of 92%. The characteristics of the encoded proteins of this isolate, such as hydrophobic domains, glycosylation sites, and conserved amino acid motifs shared with other Hantavirus and other members of the Bunyaviridae family, are identified and discussed.
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    Generation and analysis of an Eucalyptus globulus cDNA library constructed from seedlings subjected to low temperature conditions
    (Pontificia Universidad Católica de Valparaíso, 2008) Rasmussen-Poblete, Susana; Valdes, Jorge; Gamboa, Maria Cecilia; Valenzuela, Pablo D.T.; Krauskopf, Erwin
    Eucalyptus globulus is the most important commercial temperate hardwood in the world because of its wood properties and due to its characteristics for biofuel production. However, only a very low number of expressed sequence tags (ESTs) are publicly available for this tree species. We constructed a cDNA from E. globulus seedlings subjected to low temperature and sequenced 9,913 randomly selected clones, generating 8,737 curated ESTs. The assembly produced 1,062 contigs and 3,879 singletons forming a Eucalyptus unigene set. Based on BLASTX analysis, 89.3% of the contigs and 88.5% of the singletons had significant similarity to known genes in the non-redundant database of GenBank. The Eucalyptus unigene set generated is a valuable public resource that provides an initial model for genes and regulatory pathways involved in cell wall biosynthesis at low temperature.
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    Hantavirus Gc glycoprotein: Evidence for a class ll fusion protein
    (Microbiology Society, 2005-11) Tischler, Nicole D.; Gonzales, Angel; Perez-Acle, Tomas; Rosemblatt, Mario; Valenzuela, Pablo D.T.
    Hantavirus cell entry is promoted by its envelope glycoproteins, Gn and Gc, through cell attachment and by fusion between viral and endosomal membranes at low pH. However, the role of Gn and Gc in receptor binding and cell fusion has not yet been defined. In this work, a sequence presenting characteristics similar to those of class II fusion peptides (FPs) of alphavirus E1 and flavivirus E proteins is identified within the hantavirus Gc glycoprotein. A three-dimensional comparative molecular model based on crystallographic data of tick-borne encephalitis virus E protein is proposed for the Andes virus (ANDV) Gc ectodomain, which supports a feasible class II fusion-protein fold. In vitro experimental evidence is provided for the binding activity of the ANDV FP candidate to artificial membranes, as demonstrated by fluorescence anisotropy assays. Taken together, these results support the hypothesis that the Gc glycoprotein of hantaviruses and of other members of the family Bunyaviridae directs the viral fusion activity and that it may be classified as a class II viral fusion protein. © 2005 SGM.
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    Production and immune response of recombinant Hsp60 and Hsp70 from the salmon pathogen Piscirickettsia salmonis
    (Sociedad de Biología de Chile, 2005) Wilhelm, Vivian; Soza, Cristian; Martinez, Rodrigo; Rosemblatt, Mario; Burzio, Luis; Valenzuela, Pablo D.T.
    We have isolated and sequenced the genes encoding the heat shock proteins 60 (Hsp60) and 70 (Hsp70) of the salmon pathogen Piscirickettsia salmonis. The sequence analysis revealed the expected two open reading frames that encode proteins with calculated molecular weights of 60,060 and 70,400. The proteins exhibit a 70-80% homology with other known prokaryotic Hsp60 and Hsp70 sequences. The coding regions have been expressed in E. coli as thioredoxin fusion proteins. Both recombinant proteins were shown to elicit a humoral response when injected intraperitoneally in Atlantic salmon and also conferred protection to fish challenged with P. salmonis. The present data will facilitate further studies on the involvement of heat shock proteins in protective immunity of fish to infection by P. salmonis and their potential use in recombinants vaccines against this intracellular pathogen.