Search: WFRF:(Olofsson Sigvard 1948) > (2010-2014) > Diverse IgG serum r...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 03618naa a2200541 4500 | |
001 | oai:gup.ub.gu.se/185062 | |
003 | SwePub | |
008 | 240528s2013 | |||||||||||000 ||eng| | |
024 | 7 | a https://gup.ub.gu.se/publication/1850622 URI |
024 | 7 | a https://doi.org/10.1007/s10719-012-9465-32 DOI |
040 | a (SwePub)gu | |
041 | a eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a D'Arrigo, I.4 aut |
245 | 1 0 | a Diverse IgG serum response to novel glycopeptide epitopes detected within immunodominant stretches of Epstein-Barr virus glycoprotein 350/220: diagnostic potential of O-glycopeptide microarrays |
264 | c 2013-01-08 | |
264 | 1 | b Springer Science and Business Media LLC,c 2013 |
520 | a The Epstein-Barr virus (EBV) envelope glycoprotein 350/220 (gp350/220) is the most abundant molecule on the viral surface and it is responsible for the initial viral attachment to cell surface of the host. As many other viral envelope proteins, it is highly glycosylated, not least with O-linked glycans, most of which essential for EBV life cycle. EBV gp350/220 is also a primary target for neutralizing antibodies in the human hosts and a promising candidate for an EBV vaccine. Here we showed that recombinant GalNAc transferases can glycosylate scan peptides of the EBV gp350/220 envelope protein immobilized on microarray glass slides. We also identified serum IgG antibodies to a selection of peptides and O-glycopeptides, whereas sera from EBV-IgG negative individuals remained negative. We here describe novel glycopeptide epitopes present within immunodominant stretches of EBV gp350/220 and demonstrate a remarkable variability between individual samples with respect to their reactivity patterns to peptides and glycopeptides. The study provides additional insights into the complex B-cell response towards the EBV gp350/220 envelope protein, which may have implications for diagnostic and vaccine developments. | |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologi0 (SwePub)3042 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Medical Biotechnology0 (SwePub)3042 hsv//eng |
653 | a Epstein-barr virus (EBV) | |
653 | a Microarray | |
653 | a Glycopeptide | |
653 | a Biomarker | |
653 | a Serology | |
653 | a Glycosyltransferase | |
653 | a GALNT | |
653 | a MONOCLONAL-ANTIBODIES | |
653 | a PEPTIDE SEQUENCE | |
653 | a GLYCOSYLATION | |
653 | a VACCINE | |
653 | a GP350 | |
653 | a CHAIN | |
653 | a PROTEINS | |
653 | a PORCINE | |
653 | a GALNAC | |
653 | a T1 | |
700 | 1 | a Clo, E.4 aut |
700 | 1 | a Bergström, Tomas,d 1950u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine4 aut0 (Swepub:gu)xberto |
700 | 1 | a Olofsson, Sigvard,d 1948u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine4 aut0 (Swepub:gu)xolosi |
700 | 1 | a Blixt, O.4 aut |
710 | 2 | a Göteborgs universitetb Institutionen för biomedicin, avdelningen för infektionssjukdomar4 org |
773 | 0 | t Glycoconjugate Journald : Springer Science and Business Media LLCg 30:7, s. 633-640q 30:7<633-640x 0282-0080x 1573-4986 |
856 | 4 | u https://link.springer.com/content/pdf/10.1007/s10719-012-9465-3.pdf |
856 | 4 8 | u https://gup.ub.gu.se/publication/185062 |
856 | 4 8 | u https://doi.org/10.1007/s10719-012-9465-3 |
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