{"id":26793,"date":"2024-12-10T11:06:11","date_gmt":"2024-12-10T03:06:11","guid":{"rendered":"https:\/\/tbenews.com\/tbe\/?p=26793"},"modified":"2024-12-10T11:07:37","modified_gmt":"2024-12-10T03:07:37","slug":"snapshot-week-51-2024-n-and-o-linked-glycans-of-the-envelope-protein-e-of-tbe-virus","status":"publish","type":"post","link":"https:\/\/tbenews.com\/tbe\/snapshot-week-51-2024-n-and-o-linked-glycans-of-the-envelope-protein-e-of-tbe-virus\/","title":{"rendered":"Snapshot week 51\/2024<br>N-and O-linked glycans of the envelope protein E of TBE virus"},"content":{"rendered":"<span class=\"cb-itemprop\" itemprop=\"reviewBody\">\n<p class=\"wp-block-paragraph\">K\u00f6nighofer et al.<br>Identification of three novel O-linked glycans in the envelope protein of tick-borne encephalitis virus<em>. Preprints<\/em>. 2024, doi:10.20944\/preprints202410.0914.v1<\/p>\n\n\n\n<p class=\"wp-block-paragraph\">Glycoprotein E (gE) of the TBE virus contains a single N-glycan linked at N154, and this glycan has been connected to important functions in viral entry, infectivity, and pathogenesis of TBE virus. In addition to the N-linked glycan, gE contains 67 potential O-linked glycosylation sites, but there are so far no reported data showing O-linked glycosylation of gE.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\">However, three O-linked glycans have recently been identified in the gE of a clinical TBE virus isolate (designated F7203), which was obtained from a Swedish patient and propagated in the human adenocarcinomic cell line A549. Analysis of 762 TBE virus strains from the European, Siberian, and Far Eastern subtypes revealed a high degree of conservation in the amino acid sequences surrounding the potential carriers of these O-linked structures. Notably, one O-linked glycan is located near the highly conserved N-linked glycan at N154, suggesting a potential role in viral maturation.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\">In addition, the N-linked glycan at position N154 was structurally analyzed.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\">The predominant structure identified was the oligomannose form, Man6GlcNac2, though a substantial fraction carried 8 to 9 mannose residues. Complex N-linked glycan structures were also detected, primarily with the composition HexNac4Hex5Fuc1. Only 5% of the N-linked glycans contained one or more sialic acid residues.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\">Glycosylation can influence antigen processing and presentation of antigen-presenting cells. Inactivated TBE vaccines produced on chick embryo fibroblasts (e.g. FSME Immun and Encepur) exhibit the glycosylation profile specific to these cells. Newly developed recombinant TBE vaccines may possess a modified glycosylation pattern dependent on the host cell used for virus production and may have an altered immunogenicity.<\/p>\n<\/span>","protected":false},"excerpt":{"rendered":"<p>K\u00f6nighofer et al.Identification of three novel O-linked glycans in the envelope protein of tick-borne encephalitis virus. Preprints. 2024, doi:10.20944\/preprints202410.0914.v1 Glycoprotein E (gE) of the TBE virus contains a single N-glycan linked at N154, and this glycan has been connected to important functions in viral entry, infectivity, and pathogenesis of TBE virus. In addition to the N-linked glycan, gE contains 67 potential O-linked glycosylation sites, but there are so far no reported data showing O-linked glycosylation of gE. However, three O-linked glycans have recently been identified in the gE of a clinical TBE virus isolate (designated F7203), which was obtained from a Swedish patient and propagated in the human adenocarcinomic cell line A549. Analysis of 762 TBE virus strains from the European, Siberian, and Far Eastern subtypes revealed a high degree of conservation in the amino acid sequences surrounding the potential carriers of these O-linked structures. Notably, one O-linked glycan is located near the highly conserved N-linked glycan at N154, suggesting a potential role in viral maturation. In addition, the N-linked glycan at position N154 was structurally analyzed. The predominant structure identified was the oligomannose form, Man6GlcNac2, though a substantial fraction carried 8 to 9 mannose residues. Complex N-linked glycan structures were also detected, primarily with the composition HexNac4Hex5Fuc1. Only 5% of the N-linked glycans contained one or more sialic acid residues. Glycosylation can influence antigen processing and presentation of antigen-presenting cells. Inactivated TBE vaccines produced on chick embryo fibroblasts (e.g. FSME Immun and Encepur) exhibit the glycosylation profile specific to these cells. Newly developed recombinant TBE vaccines may possess a modified glycosylation pattern dependent on the host cell used for virus production and may have an altered immunogenicity.<\/p>\n","protected":false},"author":94681,"featured_media":12864,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_monsterinsights_skip_tracking":false,"footnotes":""},"categories":[18],"tags":[264,1045,1201],"coauthors":[1108],"class_list":["post-26793","post","type-post","status-publish","format-standard","has-post-thumbnail","category-snapshot","tag-glycoprotein-e","tag-glycosylation","tag-n-linked-glycan"],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v28.1 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Snapshot week 51\/2024N-and O-linked glycans of the envelope protein E of TBE virus - TBE Book<\/title>\n<meta name=\"description\" content=\"K\u00f6nighofer et al.Identification of three novel O-linked glycans in the envelope protein of tick-borne encephalitis virus. 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