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DTSTART;TZID="Pacific Time (US & Canada)":20240425T153000
DTEND;TZID="Pacific Time (US & Canada)":20240425T163000
SUMMARY:Advances in Immunology and Microbiology Seminar Series: Colleen Lynch
LOCATION:Bustad Hall
DESCRIPTION:Featuring research in the areas of:\n\nEpidemiology | Infectious Disease | Disease Ecology | Drug Discovery | Virology |\n\nGlobal Health | Vector-Borne Disease | Pathology\n\nThe Advances in Immunology & Microbiology seminar series is a weekly forum that brings together scientists from diverse fields and disciplines across the College of Veterinary Medicine to discuss research advances in the broad areas of immunology, microbiology, infectious diseases, and global health. Seminars feature student speakers from the Immunology & Infectious Disease (IID) doctoral program, IID-affiliated postdoctoral researchers and faculty, intramural speakers from across the university, and extramural speakers.\n\n\n\nPRESENTER: Colleen Lynch, PhD Candidate/Anatomic Pathology Resident; Nicola Lab; Department of Veterinary Microbiology & Pathology/Washington Animal Disease Diagnostic Laboratory\n\nTITLE: Cell Surface Expression of Ovine Herpesvirus 2 Glycoprotein B and Membrane Fusion\n\nABSTRACT: Ovine herpesvirus 2 (OvHV-2) is an important causative agent of malignant catarrhal fever, a typically fatal disease of ungulates, with no available vaccine or treatment. Membrane fusion, mediated by viral glycoproteins and host cell receptors is an essential step in herpesvirus entry and spread and is an excellent target for interventions. As OvHV-2 cannot be propagated in vitro, we use a cell-cell membrane fusion assay to experimentally evaluate the fusion mechanism. OvHV-2 glycoproteins gB, gH, and gL are necessary and sufficient for cell-cell fusion, but fusion is weak and variable. Cell surface expression of these proteins is a key determinant of cell-cell fusion. We constructed three truncated gB cytoplasmic tail mutants that eliminate putative endocytosis motifs. We aim to reduce the rate of gB endocytosis and increase surface expression and fusion, resulting in a more robust assay to further investigate the fusion mechanism, including required receptors and their viral ligands.
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