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The structural basis of Ebola viral pathogenesis / Erica Ollmann Saphire.

Title: The structural basis of Ebola viral pathogenesis / Erica Ollmann Saphire.
Author(s)/Relationship(s): Saphire, Erica Ollmann, author.
Publisher: [Bethesda, Md.] : [National Institutes of Health], [2013]
Related Names: National Institutes of Health (U.S.), issuing body.
Series: NIH Wednesday afternoon lecture
Description: 1 online resource (1 streaming video file (55 min.) : color, sound).
Content Type: two-dimensional moving image
Media Type: computer
Carrier Type: online resource
Language: eng
Electronic Links: http://videocast.nih.gov/launch.asp?18151
MeSH Subjects: Ebolavirus --pathogenicity
Ebolavirus --genetics
Glycoproteins --genetics
Lecture
Webcast
Summary: (CIT): The Wednesday Afternoon Lecture Series presents the NIH Director’s Lecture Dr. Saphire’s lab studies viruses with compact genomes that encode just four to seven genes each. Viruses with limited genomes offer a defined landscape of possible protein-protein interactions. Each protein is critical-many are obligated to perform multiple functions and some rearrange their structures to achieve those new functions. As a result, these few polypeptides accomplish a surprisingly complex set of biological functions including immune evasion, receptor recognition, cell entry, transcription, translation, assembly and exit. Dr. Saphire systematically analyzes the structures and functions of each protein encodes by the virus to gain fundamental insights into the biology of entry, immune evasion, and assembly, and to decipher the collaborative roles of these proteins in pathogenesis. In this lecture, Dr. Saphire will illustrate the molecular function throughout the viral life cycle: how the Ebola virus glycoprotein remodels itself during viral entry and how this remodeling affects the antibody response; how the Ebola and Lassa viruses suppress host innate immune signaling; and how the Ebola matrix protein assembles into one structure to bud new virions and into a different conformation to bind RNA and control transcription inside infected cells.
Notes: Title from title screen.
NLM Unique ID: 101622747
Other ID Numbers: (DNLM)CIT:18151
(OCoLC)868259593

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