2flg: Difference between revisions

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==Overview==

The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment, (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal, growth factor), each stabilized by three disulfide bonds. The native, conformation of this protein is important for eliciting P. falciparum, growth inhibitory antibodies. Here we show that the N-terminal EGF domain, alone can be chemically synthesized and efficiently refolded to a, native-like state, as shown by its solution structure as determined by NMR, spectroscopy. In order to study its immunogenicity, the domain was coupled, through its N terminus to a phospholipid and incorporated into, reconstituted influenza virus-like particles (virosomes). When used to, immunize mice, the peptide-loaded virosomes elicited potent humoral immune, responses that were shown by Western blots and immunofluorescence assays, to cross-react with native MSP-1 on the surfaces of P. falciparum blood, stage parasites. This opens the way for a medicinal chemistry-oriented, approach to the study and optimization of the antigenicity of the protein, as a potential malaria vaccine candidate, whilst exploiting the, immunopotentiating properties of influenza virosomes as a delivery, vehicle.

The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal growth factor), each stabilized by three disulfide bonds. The native conformation of this protein is important for eliciting P. falciparum growth inhibitory antibodies. Here we show that the N-terminal EGF domain alone can be chemically synthesized and efficiently refolded to a native-like state, as shown by its solution structure as determined by NMR spectroscopy. In order to study its immunogenicity, the domain was coupled through its N terminus to a phospholipid and incorporated into reconstituted influenza virus-like particles (virosomes). When used to immunize mice, the peptide-loaded virosomes elicited potent humoral immune responses that were shown by Western blots and immunofluorescence assays to cross-react with native MSP-1 on the surfaces of P. falciparum blood stage parasites. This opens the way for a medicinal chemistry-oriented approach to the study and optimization of the antigenicity of the protein as a potential malaria vaccine candidate, whilst exploiting the immunopotentiating properties of influenza virosomes as a delivery vehicle.

==About this Structure==

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[[Category: surface protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment, (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal, growth factor), each stabilized by three disulfide bonds. The native, conformation of this protein is important for eliciting P. falciparum, growth inhibitory antibodies. Here we show that the N-terminal EGF domain, alone can be chemically synthesized and efficiently refolded to a, native-like state, as shown by its solution structure as determined by NMR, spectroscopy. In order to study its immunogenicity, the domain was coupled, through its N terminus to a phospholipid and incorporated into, reconstituted influenza virus-like particles (virosomes). When used to, immunize mice, the peptide-loaded virosomes elicited potent humoral immune, responses that were shown by Western blots and immunofluorescence assays, to cross-react with native MSP-1 on the surfaces of P. falciparum blood, stage parasites. This opens the way for a medicinal chemistry-oriented, approach to the study and optimization of the antigenicity of the protein, as a potential malaria vaccine candidate, whilst exploiting the, immunopotentiating properties of influenza virosomes as a delivery, vehicle.
+The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal growth factor), each stabilized by three disulfide bonds. The native conformation of this protein is important for eliciting P. falciparum growth inhibitory antibodies. Here we show that the N-terminal EGF domain alone can be chemically synthesized and efficiently refolded to a native-like state, as shown by its solution structure as determined by NMR spectroscopy. In order to study its immunogenicity, the domain was coupled through its N terminus to a phospholipid and incorporated into reconstituted influenza virus-like particles (virosomes). When used to immunize mice, the peptide-loaded virosomes elicited potent humoral immune responses that were shown by Western blots and immunofluorescence assays to cross-react with native MSP-1 on the surfaces of P. falciparum blood stage parasites. This opens the way for a medicinal chemistry-oriented approach to the study and optimization of the antigenicity of the protein as a potential malaria vaccine candidate, whilst exploiting the immunopotentiating properties of influenza virosomes as a delivery vehicle.
 ==About this Structure==
@@ Line 24: / Line 24: @@
 [[Category: surface protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:30:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:38 2008''