Soluble and glyco-lipid modified baculovirus Plasmodium falciparum C-terminal merozoite surface protein 1, two forms of a leading malaria vaccine candidate

被引：29
作者：
Bonnet, Sarah
Petres, Stephane
Holm, Inge
Fontaine, Thierry
Rosario, Sandrine
Roth, Charles
Longacre, Shirley
机构：
[1] Inst Pasteur, Lab Vaccinol Parasitaire, F-75724 Paris 15, France
[2] Inst Pasteur, Paris, France
[3] Inst Pasteur, Unite Aspergillus, Paris, France
[4] Inst Pasteur, Unite Biochim & Biol Mol Insectes, Paris, France
来源：
VACCINE | 2006年 / 24卷 / 33-34期
关键词：
malaria vaccine; Plasmodium falciparum; merozoite surface protein 1; glycosyl-phosphtidyl-inositol (GPI);
D O I：
10.1016/j.vaccine.2006.04.069
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
Recombinant homologues of the Plasmodium merozoite surface protein I C-terminus are leading blood stage malaria vaccine candidates. MSP1 is anchored to the merozoite plasma membrane in vivo by a glycosyl-phosphatidyl-inositol (GPI) moiety, implicated in malaria pathology. Two types of recombinant Plasinodium falciparum MSP1p19 (PfMSP1p19) expressed in baculovirus/insect cells are described here: (1) a soluble, secreted form (PfMSP1pI9S) and (2) detergent soluble cellular form(s) (PfN4SP1p19 + A), released from the infected cell surface by treatment with GPI specific phosphatidyl-inositol phospholipase C (PI-PLC). Soluble and cellular PfMSP1p19 were purified and characterized using SDS-PAGE, mass spectrometry (MS), N-terminal amino acid sequencing, gel filtration and glycan analyses. Quantitative inositol dosage suggested that surface GPI processed entities constituted only 14% of the purified cellular PfMSP1p19 + A, with GPI unprocessed forms likely recovered in the endoplasmic reticulum. Nevertheless, this preparation has dramatic immuno-stimulatory activity to be described elsewhere. The interest of these results for both malaria specific and generic vaccine development are discussed. (c) 2006 Elsevier Ltd. All rights reserved.
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页码：5997 / 6008
页数：12
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