MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion

Ocampo, Marisol; Curtidor, Hernando; Vera, Ricardo; Valbuena, John; Rodrı́guez, Luis E.; Puentes, Álvaro; López, Ramsés; Garcı́a, Javier; Tovar, Diana; Pacheco, Paola; Navarro, Miguel; Patarroyo, Manuel E.

doi:10.1016/j.bbrc.2004.01.050

Cited by 17 publications

(25 citation statements)

References 36 publications

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“…Peptide binding activity was defined as being the amount (in picomoles) of peptide that bound specifically to erythrocytes per added peptide (in picomoles). HABPs were defined as being those peptides showing activity ≥2%, according to previously established criteria (Urquiza et al 1996; Curtidor et al 2001; Rodriguez et al 2003; Ocampo et al 2004).…”

Section: Resultsmentioning

confidence: 99%

“…The peptides were 125 I‐labeled according to previously described methodology (Yamamura et al 1978; Urquiza et al 1996; Curtidor et al 2001; Rodriguez et al 2003; Ocampo et al 2004). Briefly, 3.2 μLNa 125 I (100mCi/mL) were oxidized with 12.5 μL chloramine‐T (2.25 μg/μL) and added to 5 μg peptide for 5 min at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…Human erythrocytes (2 × 10 8 cells/μL), obtained from healthy donors, were washed in HBS buffer until the buffy coat was removed and then incubated with different radiolabeled‐peptide concentrations (10–200 nM), in the absence (total binding)or the presence(nonspecific binding) of 40 μM unlabeled peptide. The sample reached 200 μL final volume with HBS and was incubated for 90 min at room temperature (Urquiza et al 1996; Curtidor et al 2001; Rodriguez et al 2003; Ocampo et al 2004). The cells were then washed five times with HBS and bound cell radiolabeled peptide was quantified in an automatic γ counter (4/200 plus ICN Biomedicals, Inc).…”

Section: Methodsmentioning

confidence: 99%

“…The unlabeled peptide concentration was 40 μM. Cells were washed with HBS and a × counter was used for measuring cell‐bound radiolabeled peptide (Yamamura et al 1978; Weiland and Molinoff 1981; Hulme 1993; Urquiza et al 1996; Curtidor et al 2001; Rodriguez et al 2003; Ocampo et al 2004).…”

Section: Methodsmentioning

confidence: 99%

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Identifying Plasmodium falciparum merozoite surface antigen 3 (MSP3) protein peptides that bind specifically to erythrocytes and inhibit merozoite invasion

et al. 2005

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Receptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine Plasmodium falciparum merozoite surface protein-3 (MSP-3) FC27 strain regions that specifically bind to membrane surface receptors on human erythrocytes. Three MSP-3 protein high activity binding peptides (HABPs) were identified; their binding to erythrocytes became saturable, had nanomolar affinity constants, and became sensitive on being treated with neuraminidase and trypsin but were resistant to chymotrypsin treatment. All of them specifically recognized 45-, 55-, and 72-kDa erythrocyte membrane proteins. They all presented a-helix structural elements. All HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by $55%-85%, suggesting that MSP-3 protein's role in the invasion process probably functions by using mechanisms similar to those described for other MSP family antigens.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Identifying Plasmodium falciparum merozoite surface antigen 3 (MSP3) protein peptides that bind specifically to erythrocytes and inhibit merozoite invasion

et al. 2005

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“…The LSA-1 plays an important role in hepatic cell invasion of sporozoites as well as erythrocyte invasion of merozoites (6,20). The MAEBL is an erythrocyte-binding protein located in the rhoptries and on the surface of mature merozoites; it is expressed at the beginning of schizogony (3,18). P200 was previously identified as a diagnostic antigen for the serological detection of B. bigemina infection and also has a glutamic acid-rich region, as does the Be158 protein (23).…”

Section: Resultsmentioning

confidence: 99%

Cloning of a Novel Babesia equi Gene Encoding a 158-Kilodalton Protein Useful for Serological Diagnosis

Hirata

Yokoyama

et al. 2005

Clin Vaccine Immunol

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In this study, we characterized a Babesia equi Be158 gene obtained by immunoscreening a B. equi cDNA expression phage library with B. equi-infected horse serum. The Be158 gene consists of an open reading frame of 3,510 nucleotides. The recombinant Be158 gene product was produced in Escherichia coli and used for the immunization of mice. In Western blot analysis, mouse immune serum against the Be158 gene product recognized 75-and 158-kDa proteins from the lysate of B. equi-infected erythrocytes. In an indirect fluorescentantibody test with the mouse immune serum, the Be158 antigen appeared in the cytoplasm of Maltese cross-forming parasites (which consist of four merozoites) and was located mainly in the extraerythrocytic merozoite body. When the recombinant Be158 gene product was used in an enzyme-linked immunosorbent assay as a serological antigen, it was found to react to B. equi-infected horse sera, indicating that the Be158 gene product is useful as a serologically diagnostic antigen for B. equi infection.

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MAAP: Malarial adhesins and adhesin‐like proteins predictor

et al. 2008

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Malaria caused by protozoan parasites belonging to the genus Plasmodium is a dreaded disease, second only to tuberculosis. The emergence of parasites resistant to commonly used drugs and the lack of availability of vaccines aggravates the problem. One of the preventive approaches targets adhesion of parasites to host cells and tissues. Adhesion of parasites is mediated by proteins called adhesins. Abrogation of adhesion by either immunizing the host with adhesins or inhibiting the interaction using structural analogs of host cell receptors holds the potential to develop novel preventive strategies. The availability of complete genome sequence offers new opportunities for identifying adhesin and adhesin-like proteins. Development of computational algorithms can simplify this task and accelerate experimental characterization of the predicted adhesins from complete genomes. A curated positive dataset of experimentally known adhesins from Plasmodium species was prepared by careful examination of literature reports. "Controversial" or "hypothetical" adhesins were excluded. The negative dataset consisted of proteins representing various intracellular functions including information processing, metabolism, and interface (transporters). We did not include proteins likely to be on the surface with unknown adhesin properties or which are linked even indirectly to the adhesion process in either of the training sets. A nonhomology-based approach using 420 compositional properties of amino acid dipeptide and multiplet frequencies was used to develop MAAP Web server with Support Vector Machine (SVM) model classifier as its engine for the prediction of malarial adhesins and adhesin-like proteins. The MAAP engine has six SVM classifier models identified through an exhaustive search from 728 kernel parameters set. These models displayed an efficiency (Mathews correlation coefficient) of 0.860-0.967. The final prediction P(maap) score is the maximum score attained by a given sequence in any of the six models. The results of MAAP runs on complete proteomes of Plasmodium species revealed that in Plasmodium falciparum at P(maap) scores above 0.0, we observed a sensitivity of 100% with two false positives. In P. vivax and P. yoelii an optimal threshold P(maap) score of 0.7 was optimal with very few false positives (upto 5). Several new predictions were obtained. This list includes hypothetical protein PF14_0040, interspersed repeat antigen, STEVOR, liver stage antigen, SURFIN, RIFIN, stevor (3D7-stevorT3-2), mature parasite-infected erythrocyte surface antigen or P. falciparum erythrocyte membrane protein 2, merozoite surface protein 6 in P. falciparum, circumsporozoite proteins, microneme protein-1, Vir18, Vir12-like, Vir12, Vir18-like, Vir18-related and Vir4 in P. vivax, circumsporozoite protein/thrombospondin related anonymous proteins, 28 kDa ookinete surface protein, yir1, and yir4 of P. yoelii. Among these, a few proteins identified by MAAP were matched with those identified by other groups using different experimental and theor...

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MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion

Cited by 17 publications

References 36 publications

Identifying Plasmodium falciparum merozoite surface antigen 3 (MSP3) protein peptides that bind specifically to erythrocytes and inhibit merozoite invasion

Identifying Plasmodium falciparum merozoite surface antigen 3 (MSP3) protein peptides that bind specifically to erythrocytes and inhibit merozoite invasion

Cloning of a Novel Babesia equi Gene Encoding a 158-Kilodalton Protein Useful for Serological Diagnosis

MAAP: Malarial adhesins and adhesin‐like proteins predictor

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