{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T20:38:34Z","timestamp":1772138314627,"version":"3.50.1"},"reference-count":56,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2025,1,12]],"date-time":"2025-01-12T00:00:00Z","timestamp":1736640000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"UK Research and Innovation Future Leaders Fellowship"},{"name":"University of Oxford\u2019s COVID-19 Research Response Fund"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,1,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Abdala is a COVID-19 vaccine produced in Pichia pastoris and is based on the receptor-binding domain (RBD) of the SARS-CoV-2 spike. Abdala is currently approved for use in multiple countries with clinical trials confirming its safety and efficacy in preventing severe illness and death. Although P. pastoris is used as an expression system for protein-based vaccines, yeast glycosylation remains largely uncharacterised across immunogens. Here, we characterise N-glycan structures and their site of attachment on Abdala and show how yeast-specific glycosylation decreases binding to the ACE2 receptor and a receptor-binding motif (RBM) targeting antibody compared to the equivalent mammalian-derived RBD. Reduced receptor and antibody binding is attributed to changes in conformational dynamics resulting from N-glycosylation. These data highlight the critical importance of glycosylation in vaccine design and demonstrate how individual glycans can influence host interactions and immune recognition via protein structural dynamics.<\/jats:p>","DOI":"10.1093\/glycob\/cwaf001","type":"journal-article","created":{"date-parts":[[2025,1,10]],"date-time":"2025-01-10T07:16:17Z","timestamp":1736493377000},"source":"Crossref","is-referenced-by-count":1,"title":["Structural and Functional Glycosylation of the Abdala COVID-19 Vaccine"],"prefix":"10.1093","volume":"35","author":[{"given":"Sean A","family":"Burnap","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford , South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]},{"name":"The Kavli Institute for Nanoscience Discovery , Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valeria","family":"Calvaresi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford , South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]},{"name":"The Kavli Institute for Nanoscience Discovery , Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gleysin","family":"Cabrera","sequence":"additional","affiliation":[{"name":"Center for Genetic Engineering and Biotechnology , Avenida 31 e\/ 158 y 190. Cubanac\u00e1n. Playa. Havana, 11600 ,","place":["Cuba"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Satomy","family":"Pousa","sequence":"additional","affiliation":[{"name":"Center for Genetic Engineering and Biotechnology , Avenida 31 e\/ 158 y 190. Cubanac\u00e1n. Playa. Havana, 11600 ,","place":["Cuba"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miladys","family":"Limonta","sequence":"additional","affiliation":[{"name":"Center for Genetic Engineering and Biotechnology , Avenida 31 e\/ 158 y 190. Cubanac\u00e1n. Playa. Havana, 11600 ,","place":["Cuba"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yassel","family":"Ramos","sequence":"additional","affiliation":[{"name":"Center for Genetic Engineering and Biotechnology , Avenida 31 e\/ 158 y 190. Cubanac\u00e1n. Playa. Havana, 11600 ,","place":["Cuba"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luis Javier","family":"Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Center for Genetic Engineering and Biotechnology , Avenida 31 e\/ 158 y 190. Cubanac\u00e1n. Playa. Havana, 11600 ,","place":["Cuba"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David J","family":"Harvey","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford , South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]},{"name":"The Kavli Institute for Nanoscience Discovery , Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0594-226X","authenticated-orcid":false,"given":"Weston B","family":"Struwe","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford , South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]},{"name":"The Kavli Institute for Nanoscience Discovery , Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, OX1 3QU ,","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2025,1,12]]},"reference":[{"key":"2025012412171557500_ref1","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1042\/BJ20070748","article-title":"Glucosylated free oligosaccharides are biomarkers of endoplasmic- reticulum alpha-glucosidase inhibition","volume":"409","author":"Alonzi","year":"2008","journal-title":"Biochem J"},{"key":"2025012412171557500_ref2","doi-asserted-by":"publisher","first-page":"3427","DOI":"10.1016\/j.cell.2023.06.005","article-title":"TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry","volume":"186","author":"Baggen","year":"2023","journal-title":"Cell"},{"key":"2025012412171557500_ref3","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1111\/j.1470-8744.1999.tb00770.x","article-title":"Glycosylation of Pichia pastoris -derived proteins","volume":"30","author":"Bretthauer","year":"1999","journal-title":"Biotechnol Appl Biochem"},{"key":"2025012412171557500_ref4","doi-asserted-by":"publisher","first-page":"586","DOI":"10.1021\/acscentsci.1c00058","article-title":"Assessing antigen structural integrity through glycosylation analysis of the SARS-CoV-2 viral spike","volume":"7","author":"Brun","year":"2021","journal-title":"ACS Cent Sci"},{"key":"2025012412171557500_ref5","doi-asserted-by":"publisher","first-page":"12939","DOI":"10.1039\/D2CC04711J","article-title":"Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics","volume":"58","author":"Burnap","year":"2022","journal-title":"Chem Commun"},{"key":"2025012412171557500_ref6","doi-asserted-by":"publisher","first-page":"14657","DOI":"10.1016\/S0021-9258(18)33332-5","article-title":"Glycoprotein synthesis in yeast. 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