{"id":10307,"date":"2018-03-09T12:48:18","date_gmt":"2018-03-09T04:48:18","guid":{"rendered":"https:\/\/id-ea.org\/tbe\/?p=10307"},"modified":"2019-05-15T12:07:50","modified_gmt":"2019-05-15T04:07:50","slug":"snapshot-week-10","status":"publish","type":"post","link":"https:\/\/tbenews.com\/tbe\/snapshot-week-10\/","title":{"rendered":"Snapshot – Week 10"},"content":{"rendered":"

F\u00fczik et al.
\nStructure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
\nNat. Commun.<\/em> 2018; 9:436, DOI: 10.1038\/s41467-018-02882-0<\/p>\n

The study by F\u00fczik et al. presents the cryo-EM structure of TBE virus virions in the presence and absence of the Fab fragment of the neutralizing antibody 19\/1786 (which neutralizes multiple strains and has minimal cross-reactivity with other flaviviruses). The authors present a mechanism of action of the neutralizing antibody based on the structural results and imaging at low pH. The epitope of the antibody is focused on the E domain III, but also interacts with domains I and II and various mutations were prepared to study the interaction with various sites of the E-protein.<\/p>\n<\/span>","protected":false},"excerpt":{"rendered":"

F\u00fczik et al. Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody. Nat. Commun. 2018; 9:436, DOI: 10.1038\/s41467-018-02882-0 The study by F\u00fczik et al. presents the cryo-EM structure of TBE virus virions in the presence and absence of the Fab fragment of the neutralizing antibody 19\/1786 (which neutralizes multiple strains and has minimal cross-reactivity with other flaviviruses). The authors present a mechanism of action of the neutralizing antibody based on the structural results and imaging at low pH. The epitope of the antibody is focused on the E domain III, but also interacts with domains I and II and various mutations were prepared to study the interaction with various sites of the E-protein.<\/p>\n","protected":false},"author":6,"featured_media":12864,"comment_status":"open","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_monsterinsights_skip_tracking":false,"footnotes":""},"categories":[18],"tags":[],"coauthors":[81],"class_list":["post-10307","post","type-post","status-publish","format-standard","has-post-thumbnail","category-snapshot"],"yoast_head":"\nSnapshot - Week 10 - TBE Book<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/tbenews.com\/tbe\/snapshot-week-10\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Snapshot - Week 10 - TBE Book\" \/>\n<meta property=\"og:description\" content=\"F\u00fczik et al. Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody. Nat. Commun. 2018; 9:436, DOI: 10.1038\/s41467-018-02882-0 The study by F\u00fczik et al. presents the cryo-EM structure of TBE virus virions in the presence and absence of the Fab fragment of the neutralizing antibody 19\/1786 (which neutralizes multiple strains and has minimal cross-reactivity with other flaviviruses). The authors present a mechanism of action of the neutralizing antibody based on the structural results and imaging at low pH. 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