An antibody reactive to the Gly63-Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding
Experimental & Molecular Medicine
;
: e114-2014.
Article
Dans Anglais
| WPRIM
| ID: wpr-50917
ABSTRACT
The N-terminal fragment of prohormone brain natriuretic peptide (NT-proBNP) is a commonly used biomarker for the diagnosis of congestive heart failure, although its biological function is not well known. NT-proBNP exhibits heavy O-linked glycosylation, and it is quite difficult to develop an antibody that exhibits glycosylation-independent binding. We developed an antibody that binds to the recombinant NT-proBNP protein and its deglycosylated form with similar affinities in an enzyme immunoassay. The epitope was defined as Gly63-Lys68 based on mimetic peptide screening, site-directed mutagenesis and a competition assay with a peptide mimotope. The nearest O-glycosylation residues are Thr58 and Thr71; therefore, four amino acid residues intervene between the epitope and those residues in both directions. In conclusion, we report that an antibody reactive to Gly63-Lys68 of NT-proBNP exhibits O-glycosylation-independent binding.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Fragments peptidiques
/
Glycosylation
/
Protéines de fusion recombinantes
/
Données de séquences moléculaires
/
Mutagenèse dirigée
/
Séquence d'acides aminés
/
Cartographie épitopique
/
Peptide natriurétique cérébral
/
Cellules HEK293
/
Défaillance cardiaque
Limites du sujet:
Animaux
/
Humains
langue:
Anglais
Texte intégral:
Experimental & Molecular Medicine
Année:
2014
Type:
Article
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