Structural Insights into VLR Fine Specificity for Blood Group Carbohydrates.
Structure
; 25(11): 1667-1678.e4, 2017 11 07.
Article
em En
| MEDLINE
| ID: mdl-28988747
ABSTRACT
High-quality reagents to study and detect glycans with high specificity for research and clinical applications are severely lacking. Here, we structurally and functionally characterize several variable lymphocyte receptor (VLR)-based antibodies from lampreys immunized with O erythrocytes that specifically recognize the blood group H-trisaccharide type II antigen. Glycan microarray analysis and biophysical data reveal that these VLRs exhibit greater specificity for H-trisaccharide compared with the plant lectin UEA-1, which is widely used in blood typing. Among these antibodies, O13 exhibits superior specificity for H-trisaccharide, the basis for which is revealed by comparative analysis of high-resolution VLRglycan crystal structures. Using a structure-guided approach, we designed an O13 mutant with further enhanced specificity for H-trisaccharide. These insights into glycan recognition by VLRs suggest that lampreys can produce highly specific glycan antibodies, and are a valuable resource for the production of next-generation glycan reagents for biological and biomedical research and as diagnostics and therapeutics.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Contexto em Saúde:
2_ODS3
Base de dados:
MEDLINE
Assunto principal:
Polissacarídeos
/
Trissacarídeos
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Antígenos de Grupos Sanguíneos
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Receptores de Antígenos de Linfócitos T
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Lampreias
/
Anticorpos Monoclonais
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Structure
Ano de publicação:
2017
Tipo de documento:
Article