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Infection and Immunity, February 2006, p. 1412-1415, Vol. 74, No. 2
0019-9567/06/$08.00+0 doi:10.1128/IAI.74.2.1412-1415.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Gowdahalli Krishnegowda,1,2
Christian F. Ockenhouse,3 and
D. Channe Gowda1,2*
Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, D.C. 20007,1 Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033,2 Department of Immunology, Walter Reed Army Institute of Research, Silver Spring, Maryland 209103
Received 29 September 2005/ Returned for modification 1 November 2005/ Accepted 10 November 2005
Immunization with a synthetic glycan corresponding to Plasmodium falciparum glycosylphosphatidylinositols (GPIs) has been proposed as a vaccination strategy against malaria. We investigated the structural requirements for binding of naturally elicited anti-GPI antibodies to parasite GPIs. The data show that anti-GPI antibody binding requires intact GPI structures and that the antibodies are directed predominantly against GPIs with a conserved glycan structure with three mannoses and marginally against the terminal fourth mannose. The results provide valuable insight for exploiting GPIs for the development of malaria vaccines.
Present address: Department of Molecular Pharmacology, Division of Biochemistry, Walter Reed Army Institute of Research, Silver Spring, MD 20910.
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