Site-specific characterization of envelope protein N-glycosylation on Sanofi Pasteur's tetravalent CYD dengue vaccine

Highlights • First report assessing the site-specific N-glycosylation of the E-protein from CYD. • Both Asn67 and Asn153 sites are glycosylated. • The most abundant glycoforms at each site of the E-protein are different. • The main glycoform detected at Asn67 is able to interact with DC-SIGN co-rece...

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Bibliographic Details
Published inVaccine Vol. 33; no. 11; pp. 1360 - 1368
Main Authors Dubayle, Jean, Vialle, Sandrine, Schneider, Diane, Pontvianne, Jérémy, Mantel, Nathalie, Adam, Olivier, Guy, Bruno, Talaga, Philippe
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier Ltd 10.03.2015
Elsevier Limited
Subjects
Allergy and Immunology
Animals
Asparagine - chemistry
Cercopithecus aethiops
Dengue fever
Dengue Vaccines - chemistry
Dengue Virus
Envelope protein
Glycoproteins
Glycosylation
Humans
Infections
Lectins, C-Type - metabolism
Mammals
Mannose - metabolism
Mass spectrometry
Mutation
N-glycosylation
Polysaccharides - chemistry
Proteins
Scientific imaging
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Studies
Vaccines
Vector-borne diseases
Vero Cells
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - isolation & purification
Viruses
Envelope protein
Dengue virus
Mass spectrometry
N-glycosylation
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Summary:Highlights • First report assessing the site-specific N-glycosylation of the E-protein from CYD. • Both Asn67 and Asn153 sites are glycosylated. • The most abundant glycoforms at each site of the E-protein are different. • The main glycoform detected at Asn67 is able to interact with DC-SIGN co-receptor.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0264-410X
1873-2518
DOI:10.1016/j.vaccine.2015.01.047