Structural basis for recognition of the malaria vaccine candidate Pfs48/45 by a transmission blocking antibody.
Nat Commun
; 9(1): 3822, 2018 09 20.
Article
de En
| MEDLINE
| ID: mdl-30237518
ABSTRACT
The quest to develop an effective malaria vaccine remains a major priority in the fight against global infectious disease. An approach with great potential is a transmission-blocking vaccine which induces antibodies that prevent establishment of a productive infection in mosquitos that feed on infected humans, thereby stopping the transmission cycle. One of the most promising targets for such a vaccine is the gamete surface protein, Pfs48/45. Here we establish a system for production of full-length Pfs48/45 and use this to raise a panel of monoclonal antibodies. We map the binding regions of these antibodies on Pfs48/45 and correlate the location of their epitopes with their transmission-blocking activity. Finally, we present the structure of the C-terminal domain of Pfs48/45 bound to the most potent transmission-blocking antibody, and provide key molecular information for future structure-guided immunogen design.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Glycoprotéines membranaires
/
Protéines de protozoaire
/
Vaccins contre le paludisme
/
Anticorps bloquants
/
Paludisme
Limites:
Animals
Langue:
En
Journal:
Nat Commun
Sujet du journal:
BIOLOGIA
/
CIENCIA
Année:
2018
Type de document:
Article
Pays d'affiliation:
Royaume-Uni