Malaria parasites and erythrocyte invasion

Holder, Anthony A.; Blackman, Michael J.; Borre, Martin B.; Burghaus, Petra A.; Chappel, Jonathan A.; Keen, Jane K.; Ling, Irene T.; Ogun, Solabomi A.; Owen, Carolyn A.; Sinha, Katharine A.

doi:10.1042/bst0220291

Cited by 40 publications

(20 citation statements)

References 9 publications

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“…surface of merozoites and has been shown to play an important role in the invasion of erythrocytes by merozoites (2). During merozoite maturation, MSP-1 is proteolytically cleaved into four fragments of sizes 83, 30, 38 and 42 kDa, which are held together by noncovalent interactions.…”

Section: Introductionmentioning

confidence: 99%

Effect of GPI anchor moiety on the immunogenicity of DNA plasmids encoding the 19‐kDa C‐terminal portion of Plasmodium falciparum MSP‐1

Basagoudanavar

Gowda

2008

Parasite Immunology

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SUMMARY The glycosylphosphatidylinositol (GPI)‐anchored Plasmodium falciparum merozoite surface protein 1 (MSP‐1) is a widely studied malaria vaccine candidate. The C‐terminal 19‐kDa portion of MSP‐1 (MSP‐119) is of particular interest because this polypeptide moiety remains bound to the parasite even after erythrocyte invasion, while the remainder of MSP‐1 is shed during invasion. Studies have shown that antibodies against MSP‐119 inhibit merozoite invasion of erythrocytes efficiently, and that MSP‐119 produces protective immunity in mice and monkeys. To investigate the efficacy of MSP‐119 DNA vaccine and role of GPI anchor moiety in the immunogenicity of MSP‐119, we constructed expression vectors that produce MSP‐119 as either secretory or GPI‐anchored polypeptide. Both constructs efficiently expressed MSP‐119 in transfected HEK‐293 cells. While the recombinant plasmid lacking GPI anchor signal sequence expressed MSP‐119 mainly as secreted polypeptide, that containing GPI anchor signal sequence produced GPI‐anchored MSP‐119 on cell surface. In immunized mice, both constructs produced substantial levels of MSP‐119‐specific IgG1, IgG2a, IgG2b, IgG3, IgA and IgM antibodies. In both cases, the IgG1 level was significantly higher than other isotypes. Interestingly, the plasmid containing GPI anchor signal sequence produced significantly higher levels of IgG2a and IgG2b than the plasmid that lacks GPI signal sequence.

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Section: Introductionmentioning

confidence: 99%

Effect of GPI anchor moiety on the immunogenicity of DNA plasmids encoding the 19‐kDa C‐terminal portion of Plasmodium falciparum MSP‐1

Basagoudanavar

Gowda

2008

Parasite Immunology

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“…5 The EGF domains in PfMSP1-19 are thought to be required in interactions with the erythrocytes. 6 The use of allelic replacement to derive a transfected P. falciparum line that expresses a distinct MSP1-19 EGF domain from a rodent malaria parasite (P. chabaudi) showed that antibodies specific for this domain are a major component of the inhibitory response in immune humans.…”

Section: Introductionmentioning

confidence: 99%

Association of the IgG response to Plasmodium falciparum merozoite protein (C-terminal 19 kD) with clinical immunity to malaria in the Brazilian Amazon region.

Braga

Barros²,

Reis³

et al. 2002

The American Journal of Tropical Medicine and Hygiene

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Abstract. The antibody response to the C-terminal 19-kD fragment of Plasmodium falciparum merozoite surface protein-1 (PfMSP1-19) was investigated in groups of subjects living in areas of Brazil with different levels of malaria transmission. The prevalence and the levels of IgG to PfMSP1-19 increased with the time of exposure and were positively correlated with the absence of clinical symptoms in parasitemic patients. The frequency of positive response and the mean level of IgG were higher in areas where malaria prevalence was more intense, especially among asymptomatic patients. The serum absorbance values of the IgG1 isotype were significantly higher among subjects with long-term exposure and in asymptomatic infections. These data suggest a protective role of IgG1 in naturally acquired immunity in spite of the unstable transmission levels in the Brazilian Amazon.

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“…After repeated exposures to the infection for several years, people living in areas of endemicity acquire clinical protection against the disease. Several proteins on the merozoite surface have been shown to play a role in the initial recognition, binding, and invasion of parasites into the red blood cells (10,13). Antibody (Ab) responses to merozoite surface proteins have been shown to be associated with protective immunity against malaria (4).…”

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confidence: 99%

Comparative Immunogenicities of Full-Length Plasmodium falciparum Merozoite Surface Protein 3 and a 24-Kilodalton N-Terminal Fragment

Imam¹,

Devi²,

Verma³

et al. 2011

Clin. Vaccine Immunol.

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Recombinant Plasmodium falciparum merozoite surface protein 3 (PfMSP3F) and a 24-kDa fragment from its N terminus (MSP3N) that includes the essential conserved domain, which elicits the maximum antibody (Ab)-dependent cellular inhibition (ADCI), were expressed as soluble proteins in Escherichia coli. Both proteins were found to be stable in both soluble and lyophilized forms. Immunization with MSP3F and MSP3N formulated separately with two human-compatible adjuvants, aluminum hydroxide (Alhydrogel) and Montanide ISA 720, produced significant antibody responses in mice and rabbits. Polyclonal Abs against both antigens recognized native MSP3 in the parasite lysate. These two Abs also recognized two synthetic peptides, previously characterized to possess B cell epitopes from the N-terminal region. Antibody depletion assay showed that most of the IgG response is directed toward the N-terminal region of the full protein. Anti-MSP3F and anti-MSP3N rabbit antibodies did not inhibit merozoite invasion or intraerythrocytic development but significantly reduced parasitemia in the presence of human monocytes. The ADCI demonstrated by anti-MSP3N antibodies was comparable to that exhibited by anti-MSP3F antibodies (both generated in rabbit). These results suggest that the N-terminal fragment of MSP3 can be considered a vaccine candidate that can form part of a multigenic vaccine against malaria.

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Malaria parasites and erythrocyte invasion

Cited by 40 publications

References 9 publications

Effect of GPI anchor moiety on the immunogenicity of DNA plasmids encoding the 19‐kDa C‐terminal portion of Plasmodium falciparum MSP‐1

Effect of GPI anchor moiety on the immunogenicity of DNA plasmids encoding the 19‐kDa C‐terminal portion of Plasmodium falciparum MSP‐1

Association of the IgG response to Plasmodium falciparum merozoite protein (C-terminal 19 kD) with clinical immunity to malaria in the Brazilian Amazon region.

Comparative Immunogenicities of Full-Length Plasmodium falciparum Merozoite Surface Protein 3 and a 24-Kilodalton N-Terminal Fragment

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