CpG oligodeoxynucleotide enhances immunity against blood-stage malaria infection in mice parenterally immunized with a yeast-expressed 19 kDa carboxyl-terminal fragment of Plasmodium yoelii merozoite surface protein-1 (MSP119) formulated in oil-based Montanides

Vaccine ◽  
2003 ◽  
Vol 21 (21-22) ◽  
pp. 2923-2932 ◽  
Author(s):  
C. Hirunpetcharat ◽  
J. Wipasa ◽  
S. Sakkhachornphop ◽  
T. Nitkumhan ◽  
Y.Z. Zheng ◽  
...  
Keyword(s):  
Malaria Infection ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Plasmodium Yoelii ◽  
Blood Stage ◽  
Merozoite Surface Protein 1 ◽  
Terminal Fragment ◽  
Cpg Oligodeoxynucleotide ◽  
Carboxyl Terminal ◽  
Blood Stage Malaria

scholarly journals Oral Immunization with a Combination of Plasmodium yoelii Merozoite Surface Proteins 1 and 4/5 Enhances Protection against Lethal Malaria Challenge

2004 ◽  
Vol 72 (10) ◽  
pp. 6172-6175 ◽  
Author(s):  
Lina Wang ◽  
Matthew W. Goschnick ◽  
Ross L. Coppel
Keyword(s):  
Escherichia Coli ◽  
Malaria Infection ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Oral Immunization ◽  
Plasmodium Yoelii ◽  
Antibody Responses ◽  
Surface Proteins ◽  
Merozoite Surface Protein 1

ABSTRACT Oral immunization of mice with Escherichia coli-expressed Plasmodium yoelii merozoite surface protein 4/5 or the C-terminal 19-kDa fragment of merozoite surface protein 1 induced systemic antibody responses and protected mice against lethal malaria infection. A combination of these two proteins administered orally conferred improved protection compared to that conferred by either protein administered alone.

scholarly journals Immunoglobulin G3 Antibodies Specific for the 19-Kilodalton Carboxyl-Terminal Fragment of Plasmodium yoelii Merozoite Surface Protein 1 Transfer Protection to Mice Deficient in Fc-γRI Receptors

2000 ◽  
Vol 68 (5) ◽  
pp. 3019-3022 ◽  
Author(s):  
Peter Vukovic ◽  
P. Mark Hogarth ◽  
Nadine Barnes ◽  
David C. Kaslow ◽  
Michael F. Good
Keyword(s):  
Malaria Vaccine ◽  
Vaccine Candidate ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Plasmodium Yoelii ◽  
Merozoite Surface Protein 1 ◽  
Specific Immunoglobulin ◽  
Malaria Vaccine Candidate ◽  
Main Action ◽  
Carboxyl Terminal

ABSTRACT Merozoite surface protein 1 (MSP-119) is a leading malaria vaccine candidate. Specific antibodies contribute to immunity; binding to macrophages is believed to represent the main action of malaria antibodies. We show that an MSP-119-specific immunoglobulin G3 (IgG3) monoclonal antibody can passively transfer protection to mice deficient in the α chain of Fc-γRI whose macrophages cannot bind IgG3.

scholarly journals A Chimeric Plasmodium falciparum Merozoite Surface Protein Vaccine Induces High Titers of Parasite Growth Inhibitory Antibodies

2013 ◽  
Vol 81 (10) ◽  
pp. 3843-3854 ◽  
Author(s):  
James R. Alaro ◽  
Andrea Partridge ◽  
Kazutoyo Miura ◽  
Ababacar Diouf ◽  
Ana M. Lopez ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
T Cell ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Plasmodium Yoelii ◽  
T Cell Response ◽  
Blood Stage ◽  
Fusion Partner ◽  
Content Type ◽  
Cpg Oligodeoxynucleotide

ABSTRACTThe C-terminal 19-kDa domain ofPlasmodium falciparummerozoite surface protein 1 (PfMSP119) is an established target of protective antibodies. However, clinical trials ofPfMSP142, a leading blood-stage vaccine candidate which contains the protective epitopes ofPfMSP119, revealed suboptimal immunogenicity and efficacy. Based on proof-of-concept studies in thePlasmodium yoeliimurine model, we produced a chimeric vaccine antigen containing recombinantPfMSP119(rPfMSP119) fused to the N terminus ofP. falciparummerozoite surface protein 8 that lacked its low-complexity Asn/Asp-rich domain, rPfMSP8 (ΔAsn/Asp). Immunization of mice with the chimeric rPfMSP1/8 vaccine elicited strong T cell responses to conserved epitopes associated with the rPfMSP8 (ΔAsn/Asp) fusion partner. While specific forPfMSP8, this T cell response was adequate to provide help for the production of high titers of antibodies to bothPfMSP119and rPfMSP8 (ΔAsn/Asp) components. This occurred with formulations adjuvanted with either Quil A or with Montanide ISA 720 plus CpG oligodeoxynucleotide (ODN) and was observed in both inbred and outbred strains of mice.PfMSP1/8-induced antibodies were highly reactive with two major alleles ofPfMSP119(FVO and 3D7). Of particular interest, immunization withPfMSP1/8 elicited higher titers ofPfMSP119-specific antibodies than a combined formulation of rPfMSP142and rPfMSP8 (ΔAsn/Asp). As a measure of functionality,PfMSP1/8-specific rabbit IgG was shown to potently inhibit thein vitrogrowth of blood-stage parasites of the FVO and 3D7 strains ofP. falciparum. These data support the further testing and evaluation of this chimericPfMSP1/8 antigen as a component of a multivalent vaccine forP. falciparummalaria.

scholarly journals Passive Immunization with Antibodies against Three Distinct Epitopes on Plasmodium yoelii Merozoite Surface Protein 1 Suppresses Parasitemia

1998 ◽  
Vol 66 (8) ◽  
pp. 3925-3930 ◽  
Author(s):  
Lilian M. Spencer Valero ◽  
Solabomi A. Ogun ◽  
Suzanne L. Fleck ◽  
Irene T. Ling ◽  
Terry J. Scott-Finnigan ◽  
...  
Keyword(s):  
Passive Immunization ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Plasmodium Yoelii ◽  
Blood Stage ◽  
Merozoite Surface Protein 1 ◽  
C Terminus ◽  
Epidermal Growth ◽  
Lethal Blood

ABSTRACT We have produced monoclonal antibodies against Plasmodium yoelii merozoite surface protein 1 (MSP-1) and have assessed their ability to suppress blood stage parasitemia by passive immunization. Six immunoglobulin G antibodies were characterized in detail: three (B6, D3, and F5) were effective in suppressing a lethal blood stage challenge infection, two (B10 and G3) were partially effective, and one (B4) was ineffective. MSP-1 is the precursor to a complex of polypeptides on the merozoite surface; all of the antibodies bound to this precursor and to an ∼42-kDa fragment (MSP-142) that is derived from the C terminus of MSP-1. MSP-142 is further cleaved to an N-terminal ∼33-kDa polypeptide (MSP-133) and a C-terminal ∼19-kDa polypeptide (MSP-119) comprised of two epidermal growth factor (EGF)-like modules. D3 reacted with MSP-142 but not with either of the constituents MSP-133 and MSP-119, B4 recognized an epitope within the N terminus of MSP-133, and B6, B10, F5, and G3 bound to MSP-119. B10 and G3 bound to epitopes that required both C-terminal EGF-like modules for their formation, whereas B6 and F5 bound to epitopes in the first EGF-like module. These results indicate that at least three distinct epitopes on P. yoelii MSP-1 are recognized by antibodies that suppress parasitemia in vivo.

scholarly journals Enhanced Protection against Malaria by a Chimeric Merozoite Surface Protein Vaccine

2006 ◽  
Vol 75 (3) ◽  
pp. 1349-1358 ◽  
Author(s):  
Qifang Shi ◽  
Michelle M. Lynch ◽  
Margarita Romero ◽  
James M. Burns
Keyword(s):  
Antibody Response ◽  
Malaria Vaccine ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Plasmodium Yoelii ◽  
Protein Vaccine ◽  
Specific Antibody Response ◽  
Merozoite Surface Protein 1 ◽  
Epidermal Growth ◽  
Blood Stage Malaria

ABSTRACTThe 42-kDa processed fragment ofPlasmodium falciparummerozoite surface protein 1 (MSP-142) is a prime candidate for a blood-stage malaria vaccine. Merozoite surface protein 8 contains two C-terminal epidermal growth factor (EGF)-like domains that may function similarly to those of MSP-142. Immunization with either MSP-1 or MSP-8 induces protection that is mediated primarily by antibodies against conformation-dependent epitopes. In a series of comparative immunogenicity and efficacy studies using thePlasmodium yoeliirodent model, we tested the ability of recombinantP. yoeliiMSP-8 (rPyMSP-8) to complement rPyMSP-1-based vaccines. Unlike MSP-1, PyMSP-8-dependent protection required immunization with the full-length protein and was not induced with recombinant antigens that contained only the C-terminal EGF-like domains. Unlike PyMSP-8, the immunogenicity of the PyMSP-1 EGF-like domains was low when present as part of the rPyMSP-142antigen. Immunization with a mixture of rPyMSP-142and rPyMSP-8 further inhibited the antibody response to protective epitopes of rPyMSP-142and did not improve vaccine efficacy. To improve PyMSP-1 immunogenicity, we produced a chimeric antigen containing the EGF-like domains of PyMSP-1 fused to the N terminus of PyMSP-8. Immunization with the chimeric rPyMSP-1/8 antigen induced high and comparable antibody responses against the EGF-like domains of both PyMSP-1 and PyMSP-8. This enhanced MSP-1-specific antibody response and the concurrent targeting of MSP-1 and MSP-8 resulted in improved, nearly complete protection against lethalP. yoelii17XL malaria. Unexpectedly, immunization with rPyMSP-1/8 failed to protect against challenge infection with reticulocyte-restrictedP. yoelii17X parasites. Overall, these data establish an effective strategy to improve the efficacy ofP. falciparumMSP-based vaccines.

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