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2.8 resolution cryo-EM structure of human parechovirus 3 in complex with Fab from a neutralizing antibody
by
Flatt, Justin Wayne
, Domanska, Ausra
, Geraets, James Alexander
, Butcher, Sarah Jane
, Joonas Jouni Juhani Jukonen
in
Antiviral agents
/ Epitopes
/ Image processing
/ Immune response
/ Microbiology
/ Monoclonal antibodies
/ Neonates
/ Ribonucleic acid
/ RNA
/ Sepsis
/ Virions
2018
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2.8 resolution cryo-EM structure of human parechovirus 3 in complex with Fab from a neutralizing antibody
by
Flatt, Justin Wayne
, Domanska, Ausra
, Geraets, James Alexander
, Butcher, Sarah Jane
, Joonas Jouni Juhani Jukonen
in
Antiviral agents
/ Epitopes
/ Image processing
/ Immune response
/ Microbiology
/ Monoclonal antibodies
/ Neonates
/ Ribonucleic acid
/ RNA
/ Sepsis
/ Virions
2018
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While trying to remove the title from your shelf something went wrong :( Kindly try again later!
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2.8 resolution cryo-EM structure of human parechovirus 3 in complex with Fab from a neutralizing antibody
by
Flatt, Justin Wayne
, Domanska, Ausra
, Geraets, James Alexander
, Butcher, Sarah Jane
, Joonas Jouni Juhani Jukonen
in
Antiviral agents
/ Epitopes
/ Image processing
/ Immune response
/ Microbiology
/ Monoclonal antibodies
/ Neonates
/ Ribonucleic acid
/ RNA
/ Sepsis
/ Virions
2018
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2.8 resolution cryo-EM structure of human parechovirus 3 in complex with Fab from a neutralizing antibody
Paper
2.8 resolution cryo-EM structure of human parechovirus 3 in complex with Fab from a neutralizing antibody
2018
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Overview
Human parechovirus 3 (HPeV3) infection is associated with sepsis in neonates characterized by significant immune activation and subsequent tissue damage. Strategies to limit infection have been unsuccessful due to inadequate molecular diagnostic tools for early detection and lack of a vaccine or specific antiviral therapy. Towards the latter, we present a 2.8 -resolution structure of HPeV3 in complex with fragments from a neutralizing human monoclonal antibody AT12-015 using cryo-EM and image reconstruction. Modeling revealed that the epitope extends across neighboring asymmetric units with contributions from capsid proteins VP0, VP1, and VP3. Antibody decoration was found to block binding of HPeV3 to cultured cells. Additionally at high-resolution, it was possible to model a stretch of RNA inside the virion and from this identify the key features that drive and stabilize protein-RNA association during assembly.
Publisher
Cold Spring Harbor Laboratory Press,Cold Spring Harbor Laboratory
Subject
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