Characterization of the Duffy-Binding-Like Domain of Plasmodium falciparum Blood-Stage Antigen 332
Author(s) -
Sandra Nilsson,
Kirsten Moll,
Davide Angeletti,
Letusa Albrecht,
Inari Kursula,
Ning Jiang,
Xiaodong Sun,
Klavs Berzins,
Mats Wahlgren,
Qijun Chen
Publication year - 2011
Publication title -
malaria research and treatment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.726
H-Index - 15
eISSN - 2090-8075
pISSN - 2044-4362
DOI - 10.4061/2011/671439
Subject(s) - plasmodium falciparum , antibody , antigen , biology , malaria , immunofluorescence , cross reactivity , homology (biology) , microbiology and biotechnology , blot , virology , genetics , immunology , amino acid , gene , cross reactions
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
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