A common glycan structure on immunoglobulin G for enhancement of effector functions.
Proc Natl Acad Sci U S A
; 112(34): 10611-6, 2015 Aug 25.
Article
en En
| MEDLINE
| ID: mdl-26253764
ABSTRACT
Antibodies have been developed as therapeutic agents for the treatment of cancer, infection, and inflammation. In addition to binding activity toward the target, antibodies also exhibit effector-mediated activities through the interaction of the Fc glycan and the Fc receptors on immune cells. To identify the optimal glycan structures for individual antibodies with desired activity, we have developed an effective method to modify the Fc-glycan structures to a homogeneous glycoform. In this study, it was found that the biantennary N-glycan structure with two terminal alpha-2,6-linked sialic acids is a common and optimized structure for the enhancement of antibody-dependent cell-mediated cytotoxicity, complement-dependent cytotoxicity, and antiinflammatory activities.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Polisacáridos
/
Inmunoglobulina G
/
Fragmentos Fc de Inmunoglobulinas
/
Rituximab
Límite:
Animals
/
Female
/
Humans
Idioma:
En
Año:
2015
Tipo del documento:
Article