About: Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation

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About: Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation
Creator	Fijten, H Harmsen, M Van Solt, C
Source	PMC
abstract	Single-domain antibody fragments (VHHs) have several beneficial properties as compared to conventional antibody fragments. However, their small size complicates their toxin- and virus-neutralizing capacity. We isolated 27 VHHs binding Escherichia coli heat-labile toxin and expressed these in Saccharomyces cerevisiae. The most potent neutralizing VHH (LT109) was N-glycosylated, resulting in a large increase in molecular mass. This suggests that N-glycosylation of LT109 improves its neutralizing capacity. Indeed, deglycosylation of LT109 decreased its neutralizing capacity three- to fivefold. We also studied the effect of glycosylation of two previously isolated VHHs on their ability to neutralize foot-and-mouth disease virus. For this purpose, these VHHs that lacked potential N-glycosylation sites were genetically fused to another VHH that was known to be glycosylated. The resulting fusion proteins were also N-glycosylated. They neutralized the virus at at least fourfold-lower VHH concentrations as compared to the single, non-glycosylated VHHs and at at least 50-fold-lower VHH concentrations as compared to their deglycosylated counterparts. Thus, we have shown that N-glycosylation of VHHs contributes to toxin- and virus-neutralizing capacity.
has issue date	2009-05-12(xsd:dateTime)
bibo:doi	10.1007/s00253-009-2029-1
bibo:pmid	19455325
has license	no-cc
sha1sum (hex)	05ce56760c5dbdfc362b4f6a8c261ebd453b4893
schema:url	https://doi.org/10.1007/s00253-009-2029-1
resource representing a document's title	Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation
has PubMed Central identifier	PMC2755796
has PubMed identifier	19455325
schema:publication	Appl Microbiol Biotechnol
resource representing a document's body	covid:05ce56760c5dbdfc362b4f6a8c261ebd453b4893#body_text
is schema:about of	named entity 'genetically' named entity 'capacity' named entity 'foot-and-mouth disease virus' named entity 'fusion proteins' named entity 'N-glycosylated' named entity 'However' named entity 'PURPOSE' named entity 'PROTEINS' named entity 'LARGE' named entity 'NON-' named entity 'CONVENTIONAL' named entity 'FOOT-AND-MOUTH DISEASE VIRUS' named entity 'IMPROVES' named entity 'COMPARED' named entity 'ANTIBODY' named entity 'GLYCOSYLATION' named entity 'DEGLYCOSYLATION' named entity 'fused' named entity 'sites' named entity 'concentrations' named entity 'N-glycosylated' named entity 'glycosylated' named entity 'toxin' named entity 'VHH' named entity 'virus' named entity 'N-glycosylation' named entity 'virus' named entity 'The' named entity 'neutralizing' named entity 'glycosylated' named entity 'antibodies' named entity 'llama' named entity 'CDR2' named entity 'amino acid' named entity 'standard deviation' named entity 'porcine' named entity 'N-glycosylation' named entity 'vector' named entity 'glycosylation' named entity 'oligosaccharide' named entity 'virus' named entity 'VHH' named entity 'biotin' named entity 'therapeutic antibody' named entity 'endoglycosidase' named entity 'antigen-binding site' named entity 'carbonate' named entity 'llama' named entity 'toxin' named entity 'N-glycosylated' named entity 'Stratagene' named entity 'C-terminal' named entity 'Parenteral' named entity 'CDR3' named entity 'consensus sequence' named entity 'receptor' named entity 'glycosylation' named entity 'swine' named entity 'diarrheal diseases' named entity 'VHH' named entity 'recombinant' named entity 'protein stability' named entity 'antigen' named entity 'glycosylated' named entity 'San Diego' named entity 'protein' named entity 'Stratagene' named entity 'ovalbumin' named entity 'endoglycosidase' named entity 'glycosylation' named entity 'N-glycosylated' named entity 'microorganisms' named entity 'skimmed milk' named entity 'GM1' named entity 'PstI' named entity 'biotinylated' named entity 'Neutralizing antibodies' named entity 'steric hindrance' named entity 'VHH'

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