Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?

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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 journalJournal articleResearchpeer-review

Harvard

Dahlbäck, M, Nielsen, MA & Salanti, A 2010, 'Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?', Trends in Parasitology, vol. 26, no. 5, pp. 230-5. https://doi.org/10.1016/j.pt.2010.02.002

APA

Dahlbäck, M., Nielsen, M. A., & Salanti, A. (2010). Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains? Trends in Parasitology, 26(5), 230-5. https://doi.org/10.1016/j.pt.2010.02.002

Vancouver

Dahlbäck M, Nielsen MA, Salanti A. Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains? Trends in Parasitology. 2010;26(5):230-5. https://doi.org/10.1016/j.pt.2010.02.002

Author

Dahlbäck, Madeleine ; Nielsen, Morten A ; Salanti, Ali. / Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?. In: Trends in Parasitology. 2010 ; Vol. 26, No. 5. pp. 230-5.

Bibtex

@article{f3b98f105b8011df928f000ea68e967b,
title = "Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?",
abstract = "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.",
author = "Madeleine Dahlb{\"a}ck and Nielsen, {Morten A} and Ali Salanti",
year = "2010",
doi = "10.1016/j.pt.2010.02.002",
language = "English",
volume = "26",
pages = "230--5",
journal = "Trends in Parasitology",
issn = "1471-4922",
publisher = "Elsevier Ltd. * Trends Journals",
number = "5",

}

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