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Malaria Research and Treatment
Volume 2011 (2011), Article ID 671439, 14 pages
Research Article

Characterization of the Duffy-Binding-Like Domain of Plasmodium falciparum Blood-Stage Antigen 332

1Department of Microbiology, Tumor, and Cell Biology, Karolinska Institutet, 171 77 Stockholm, Sweden
2Department of Medical Biochemistry and Biophysics, Karolinska Institutet, 171 77 Stockholm, Sweden
3Centre for Structural Systems Biology, Helmholtz Centre for Infection Research and Deutsches Elektronen-Synchrotron, University of Hamburg, 22607 Hamburg, Germany
4Key Laboratory of Zoonosis, Ministry of Education, Jilin University, Changchun 130062, China
5Institute of Parasitic Disease Control, Puer City, Yunnan Province, China
6Department of Immunology, Wenner-Gren Institute, Stockholm University, 106 91 Stockholm, Sweden
7Laboratory of Parasitology, Institute of Pathogen Biology, Chinese Academy of Medical Sciences, Beijing 100730, China

Received 25 March 2011; Accepted 8 June 2011

Academic Editor: Neena Valecha

Copyright © 2011 Sandra Nilsson et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Studies on Pf332, a major Plasmodium falciparum blood-stage antigen, have largely been hampered by the cross-reactive nature of antibodies generated against the molecule due to its high content of repeats, which are present in other malaria antigens. We previously reported the identification of a conserved domain in Pf332 with a high degree of similarity to the Duffy-binding-like (DBL) domains of the erythrocyte-binding-like (EBL) family. We here describe that antibodies towards Pf332-DBL are induced after repeated exposure to P. falciparum and that they are acquired early in life in areas of intense malaria transmission. Furthermore, a homology model of Pf332-DBL was found to be similar to the structure of the EBL-DBLs. Despite their similarities, antibodies towards Pf332-DBL did not display any cross-reactivity with EBL-proteins as demonstrated by immunofluorescence microscopy, Western blotting, and peptide microarray. Thus the DBL domain is an attractive region to use in further studies on the giant Pf332 molecule.