Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains? / Dahlbäck, Madeleine; Nielsen, Morten A; Salanti, Ali.
In: Trends in Parasitology, Vol. 26, No. 5, 2010, p. 230-5.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?
AU - Dahlbäck, Madeleine
AU - Nielsen, Morten A
AU - Salanti, Ali
PY - 2010
Y1 - 2010
N2 - Pregnancy-associated malaria (PAM) is caused by Plasmodium falciparum-infected erythrocytes (IEs) accumulating in the placenta and has dire consequences for both mother and child. The multi-domain antigen VAR2CSA confers specific adhesion of IEs to chondroitin sulphate A (CSA) in the placenta, and is the leading PAM vaccine candidate. Recent data from different laboratories show that the binding properties of individual VAR2CSA domains do not reflect the native CSA-specific adhesion of IEs, which questions the relevance of the information obtained from single domain binding assays and co-crystallization experiments. Here, we discuss the implications of these findings for VAR2CSA vaccine development and highlight the need for studying the native structure of this protein.
AB - Pregnancy-associated malaria (PAM) is caused by Plasmodium falciparum-infected erythrocytes (IEs) accumulating in the placenta and has dire consequences for both mother and child. The multi-domain antigen VAR2CSA confers specific adhesion of IEs to chondroitin sulphate A (CSA) in the placenta, and is the leading PAM vaccine candidate. Recent data from different laboratories show that the binding properties of individual VAR2CSA domains do not reflect the native CSA-specific adhesion of IEs, which questions the relevance of the information obtained from single domain binding assays and co-crystallization experiments. Here, we discuss the implications of these findings for VAR2CSA vaccine development and highlight the need for studying the native structure of this protein.
U2 - 10.1016/j.pt.2010.02.002
DO - 10.1016/j.pt.2010.02.002
M3 - Journal article
C2 - 20189879
VL - 26
SP - 230
EP - 235
JO - Trends in Parasitology
JF - Trends in Parasitology
SN - 1471-4922
IS - 5
ER -
ID: 19641341