Cross–reactive antigenic determinants present on different <i>Plasmodium falciparum</i> blood–stage antigens

Mattei, Denise; Berzins, Klavs; Wahlgren, Mats; Udomsangpetch, Rachanee; Perlmann, Peter; Griesser, Hans Werner; Scherf, Artur; Müjller–Hill, Benno; Bonnefoy, Serge; Guillotte, Micheline; Langsley, Gordon; Silva, Luiz Pereira da; Mercereau‐Puijalon, Odile

doi:10.1111/j.1365-3024.1989.tb00645.x

Cited by 82 publications

(54 citation statements)

References 29 publications

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“…1. A small glutamic acid-rich region (aa 258 to 281; 54% glutamic acid) was excluded to avoid cross-reactivity exhibited by glutamate-rich epitopes present in several P. falciparum antigens (8). Enzyme-linked immunosorbent assays (ELISAs) were performed as described earlier (13) to determine the level of total IgG and the subclass distribution against each peptide in sera from 30 malaria-protected African adults from Ivory Coast.…”

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confidence: 99%

Plasmodium falciparum Merozoite Surface Protein 6 Displays Multiple Targets for Naturally Occurring Antibodies That Mediate Monocyte-Dependent Parasite Killing

et al. 2005

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Plasmodium falciparum MSP6 is a merozoite surface antigen that shows organization and sequence homologies similar to those of MSP3. Within its C-terminus conserved region, it presents some epitopes that are cross-reactive with MSP3 and others that are not, both being targets of naturally occurring antibodies that block the P. falciparum erythrocytic cycle in cooperation with monocytes.Plasmodium falciparum MSP6 has been described recently as a merozoite surface molecule, structurally related in its overall sequence organization to the previously described MSP3 (10, 17). The C-terminal part of the protein shows homology with MSP3 (ca. 50% identity and 85% similarity of amino acid residues) and an identity for an 11-amino-acid (aa) stretch (ILGWEFGGG[A/V]P) previously identified as a target of antibodies with strong antiparasite activity (9, 13). Moreover, the C-terminal part of MSP6 is highly conserved in MSP6, as in the case of MSP3, whereas the N-terminal part displays polymorphisms, is proteolytically cleaved, and is less antigenic than the C-terminal part (10, 18).MSP3 has been identified as a target of protective antibodies by assays involving antibody-dependent cellular inhibition (ADCI), a mechanism found to best reflect the protection that can be passively transferred by antibodies in P. falciparuminfected patients (9). MSP3 has been pursued for human vaccine trials based on the following series of findings suggesting that anti-MSP3 antibodies contribute to protection against malaria. (i) Immunoepidemiological studies showed a significant correlation of immunoglobulin G3 (IgG3) antibodies with protection acquired by natural exposure to the parasite (13,14).(ii) Either naturally occurring or artificially raised antibodies have a strong monocyte-dependent ADCI effect (9, 13). (iii) Immunity can be actively elicited in primates against a P. falciparum challenge and correlates with prechallenge anti-MSP3 antibody titers (7). (iv) Immunity can be passively transferred by anti-MSP3 antibodies in P. falciparum-infected SCID mice (1, 13) and Plasmodium reichnowi-infected chimpanzees (M. Dziegel et al., submitted for publication).Given the homologies of MSP6 with MSP3, we therefore performed a detailed study of the antigenicity of MSP6 and assessed the antiparasite role of the naturally occurring anti-MSP6 antibodies.Antigenicity in populations of areas of endemicity. The C-terminal part of MSP6 (aa 161 to 371 in clone 3D7) was cloned and expressed as a recombinant histidine-tagged protein (MSP6-Cterm), as described earlier (16). Six overlapping peptides

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Plasmodium falciparum Merozoite Surface Protein 6 Displays Multiple Targets for Naturally Occurring Antibodies That Mediate Monocyte-Dependent Parasite Killing

et al. 2005

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“…2,3 Its amino acid sequence is only partially deduced (1,400 residues) and comprises undecamer repeat sequences with regularly spaced pairs of glutamic acid. 2,4,5 Although these repeats share a common feature, they are highly degenerated and most motifs occur only once in the sequence of Pf332 so far deduced. 2 Structurally related repeats are found in a number of P. falciparum proteins including Pf155/ring-infected erythrocyte surface antigen (RESA), Pf11.1, and glutamate-rich protein.…”

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Human immune responses to the highly repetitive Plasmodium falciparum antigen Pf332.

Kulane

Siddique²,

Sarthou³

et al. 1999

The American Journal of Tropical Medicine and Hygiene

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Abstract. The B and T cell responses to EB200, a repetitive part of the Plasmodium falciparum antigen Pf332, were examined in malaria-exposed Senegalese adults. Most donors had high levels of antibodies to recombinant EB200 and 17 overlapping peptides spanning EB200. Taking proliferation and/or cytokine (interferon-␥ and interleukin-4) production as a measure of T cell activation, eight of the EB200-derived peptides induced responses in Ͼ 40% of the donors tested. There was no general association between the different types of T cell responses measured, emphasizing the importance of including multiple parameters when analyzing T cell responses and suggesting that EB200 induces functionally distinct T cell responses. The most efficient peptide for induction of proliferative responses was one previously shown to induce T cell responses in five different H-2 congenic mouse strains primed with EB200, suggesting that this is a universal T cell epitope. The presence of multiple B and T cell epitopes in EB200, widely recognized by humans, is important since EB200 has been shown to elicit protective antibody responses in monkeys and may be considered for inclusion in malaria subunit vaccines.The Plasmodium falciparum antigen Pf332 is of potential interest for inclusion in a subunit vaccine against the malaria parasite.

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“…Antibodies against glutamate-rich proteins from P. falciparum often crossreact with other antigens. For example, Mab-33G2 primarily recognizes Ag332, but cross-reacts with Pf11.1 and Pf155/RESA (Mattei et al 1989). The optimal epitope recognized by Mab-33G2 is VTEEI with the pair of glutamates followed by a hydrophobic residue being particularly important (Ahlborg et al 1991).…”

Section: Resultsmentioning

confidence: 99%

“…These proteins are highly antigenic, but little is known about their biological functions or their roles in anti-malarial immunity. Furthermore, many of these glutamate-rich proteins exhibit cross-reacting epitopes (Mattei et al 1989;Ahlborg et al 1991;Wahlin et al 1992). Although several glutamate-rich proteins have been described in P. falciparum, little work has been done on similar proteins in rodent malaria species.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Plasmodium chabaudi gene encoding a protein with glutamate-rich tandem repeats

Giraldo¹,

Jennings²,

Deleersnijder

et al. 1999

Parasitology Research

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Several highly antigenic proteins containing tandem repeats rich in glutamic acid residues have been described in Plasmodium falciparum. However, relatively little information is available about analogous genes in rodent parasites. This report describes a 4.2-kb genomic DNA fragment from P. chabaudi with a deduced amino acid sequence that is predominantly glutamate-rich tandem repeats. Several dierent monoclonal antibodies raised against a 93-kDa P. chabaudi protein, which does not correspond to the cloned DNA fragment, recognize a recombinant protein expressed from the 4.2-kb DNA fragment. The only sequence similarities between these two genes are tandem repeats with a predominance of glutamate pairs followed by a hydrophobic residue. This repetitious-sequence motif may be the basis for the observed cross-reactivity. A similar motif has been demonstrated to be the basis for antibody cross-reactivity between glutamate-rich proteins of P. falciparum. The expression of multiple glutamate-rich proteins with cross-reacting epitopes may be a general phenomenon in Plasmodium species.

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Cross–reactive antigenic determinants present on different Plasmodium falciparum blood–stage antigens

Cited by 82 publications

References 29 publications

Plasmodium falciparum Merozoite Surface Protein 6 Displays Multiple Targets for Naturally Occurring Antibodies That Mediate Monocyte-Dependent Parasite Killing

Plasmodium falciparum Merozoite Surface Protein 6 Displays Multiple Targets for Naturally Occurring Antibodies That Mediate Monocyte-Dependent Parasite Killing

Human immune responses to the highly repetitive Plasmodium falciparum antigen Pf332.

Characterization of a Plasmodium chabaudi gene encoding a protein with glutamate-rich tandem repeats

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