Please use this identifier to cite or link to this item: https://zone.biblio.laurentian.ca/handle/10219/2690
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dc.contributor.authorEchánove Juan, José Arquímides-
dc.date.accessioned2016-12-23T19:57:30Z-
dc.date.available2016-12-23T19:57:30Z-
dc.date.issued2016-12-19-
dc.identifier.urihttps://zone.biblio.laurentian.ca/handle/10219/2690-
dc.description.abstractThe Influenza virus is a significant global health problem whose worldwide circulation constantly triggers new pandemic strains often linked to genetic re-assortment and new mutations. Virus variability threatens and challenges the health of millions of citizens. Vaccination against influenza prior to infection offers the standard alternative to antiviral treatment in infected patients. Vaccine production must be available in sufficient volume for human and animal vaccination on a large scale. In this study I designed a novel recombinant influenza protein composed of three chimeric Hemagglutinin (HA) influenza receptor-binding domains (RBD) expressed in tandem. This construct was expressed as a single molecule in Pichia pastoris and characterized by gene sequencing, polyacrylamide gel electrophoresis, immuno-detection, and carbohydrate composition. The goal of this project is to develop a reagent for use in immunological response assays in a mouse model that will provide information regarding the potential use of these multisubunit gene-expressing constructs as vaccine candidates.en_CA
dc.language.isoenen_CA
dc.subjectPichia pastorisen_CA
dc.subjectInfluenza virusen_CA
dc.subjectHemagglutininen_CA
dc.subjectAntigenen_CA
dc.subjectProtein Expressionen_CA
dc.subjectGene Designen_CA
dc.subjectReceptor Binding Domainen_CA
dc.subjectVaccinationen_CA
dc.titleHemagglutinin-based antigen designs expressed in the methylotrophic yeast Pichia pastorisen_CA
dc.typeThesisen_CA
dc.description.degreeMaster of Science (MSc) in Chemical Sciencesen_CA
dc.publisher.grantorLaurentian University of Sudburyen_CA
Appears in Collections:Chemical Sciences - Master's Theses
Master's Theses

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