The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro
Identifieur interne : 000725 ( Main/Exploration ); précédent : 000724; suivant : 000726The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro
Auteurs : Sonja B. Lauterbach [Afrique du Sud] ; Theresa L. Coetzer [Afrique du Sud]Source :
- Malaria Journal [ 1475-2875 ] ; 2008.
Abstract
During erythrocytic schizogony,
r
r
Studies characterizing r
Url:
DOI: 10.1186/1475-2875-7-161
PubMed: 18721457
PubMed Central: 2543045
Affiliations:
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Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The M18 aspartyl aminopeptidase of <italic>Plasmodium falciparum </italic>
binds to human erythrocyte spectrin <italic>in vitro</italic>
</title>
<author><name sortKey="Lauterbach, Sonja B" sort="Lauterbach, Sonja B" uniqKey="Lauterbach S" first="Sonja B" last="Lauterbach">Sonja B. Lauterbach</name>
<affiliation wicri:level="4"><nlm:aff id="I1">Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193, Republic of South Africa</nlm:aff>
<country xml:lang="fr">Afrique du Sud</country>
<wicri:regionArea>Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193</wicri:regionArea>
<orgName type="university">Université du Witwatersrand</orgName>
<placeName><settlement type="city">Johannesbourg</settlement>
<region type="region" nuts="2">Gauteng</region>
</placeName>
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<author><name sortKey="Coetzer, Theresa L" sort="Coetzer, Theresa L" uniqKey="Coetzer T" first="Theresa L" last="Coetzer">Theresa L. Coetzer</name>
<affiliation wicri:level="4"><nlm:aff id="I1">Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193, Republic of South Africa</nlm:aff>
<country xml:lang="fr">Afrique du Sud</country>
<wicri:regionArea>Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193</wicri:regionArea>
<orgName type="university">Université du Witwatersrand</orgName>
<placeName><settlement type="city">Johannesbourg</settlement>
<region type="region" nuts="2">Gauteng</region>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The M18 aspartyl aminopeptidase of <italic>Plasmodium falciparum </italic>
binds to human erythrocyte spectrin <italic>in vitro</italic>
</title>
<author><name sortKey="Lauterbach, Sonja B" sort="Lauterbach, Sonja B" uniqKey="Lauterbach S" first="Sonja B" last="Lauterbach">Sonja B. Lauterbach</name>
<affiliation wicri:level="4"><nlm:aff id="I1">Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193, Republic of South Africa</nlm:aff>
<country xml:lang="fr">Afrique du Sud</country>
<wicri:regionArea>Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193</wicri:regionArea>
<orgName type="university">Université du Witwatersrand</orgName>
<placeName><settlement type="city">Johannesbourg</settlement>
<region type="region" nuts="2">Gauteng</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Coetzer, Theresa L" sort="Coetzer, Theresa L" uniqKey="Coetzer T" first="Theresa L" last="Coetzer">Theresa L. Coetzer</name>
<affiliation wicri:level="4"><nlm:aff id="I1">Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193, Republic of South Africa</nlm:aff>
<country xml:lang="fr">Afrique du Sud</country>
<wicri:regionArea>Department of Molecular Medicine and Haematology, National Health Laboratory Service, School of Pathology, University of the Witwatersrand, Parktown, Johannesburg 2193</wicri:regionArea>
<orgName type="university">Université du Witwatersrand</orgName>
<placeName><settlement type="city">Johannesbourg</settlement>
<region type="region" nuts="2">Gauteng</region>
</placeName>
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<series><title level="j">Malaria Journal</title>
<idno type="eISSN">1475-2875</idno>
<imprint><date when="2008">2008</date>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>During erythrocytic schizogony, <italic>Plasmodium falciparum </italic>
interacts with the human erythrocyte membrane when it enters into, grows within and escapes from the erythrocyte. An interaction between the <italic>P. falciparum </italic>
M18 aspartyl aminopeptidase (<italic>Pf</italic>
M18AAP) and the human erythrocyte membrane protein spectrin was recently identified using phage display technology. In this study, recombinant (r) <italic>Pf</italic>
M18AAP was characterized and the interaction between the enzyme and spectrin, as well as other erythrocyte membrane proteins, analyzed.</p>
</sec>
<sec sec-type="methods"><title>Methods</title>
<p>r<italic>Pf</italic>
M18AAP was produced as a hexahistidine-fusion protein in <italic>Escherichia coli </italic>
and purified using magnetic bead technology. The pI of the enzyme was determined by two-dimensional gel electrophoresis and the number of subunits in the native enzyme was estimated from Ferguson plots. The enzymatic activity over a pH and temperature range was tested by a coupled enzyme assay. Blot overlays were performed to validate the spectrin-<italic>Pf</italic>
M18AAP interaction, as well as identify additional interactions between the enzyme and other erythrocyte membrane proteins. Sequence analysis identified conserved amino acids that are expected to be involved in cofactor binding, substrate cleavage and quaternary structure stabilization.</p>
</sec>
<sec><title>Results</title>
<p>r<italic>Pf</italic>
M18AAP has a molecular weight of ~67 kDa and the enzyme separated as three entities with pI 6.6, 6.7 and 6.9. Non-denaturing gel electrophoresis indicated that r<italic>Pf</italic>
M18AAP aggregated into oligomers. An <italic>in vitro </italic>
coupled enzyme assay showed that r<italic>Pf</italic>
M18AAP cleaved an N-terminal aspartate from a tripeptide substrate with maximum enzymatic activity at pH 7.5 and 37°C. The spectrin-binding region of <italic>Pf</italic>
M18AAP is not found in <italic>Homo sapiens, Saccharomyces cerevisiae </italic>
and other<italic>Plasmodium </italic>
species homologues. Amino acids expected to be involved in cofactor binding, substrate cleavage and quaternary structure stabilization, are conserved. Blot overlays with r<italic>Pf</italic>
M18AAP against spectrin and erythrocyte membrane proteins indicated that r<italic>Pf</italic>
M18AAP binds to spectrin, as well as to protein 4.1, protein 4.2, actin and glyceraldehyde 3-phosphate dehydrogenase.</p>
</sec>
<sec><title>Conclusion</title>
<p>Studies characterizing r<italic>Pf</italic>
M18AAP showed that this enzyme interacts with erythrocyte spectrin and other membrane proteins. This suggests that, in addition to its proposed role in hemoglobin digestion, <italic>Pf</italic>
M18AAP performs other functions in the erythrocyte host and can utilize several substrates, which highlights the multifunctional role of malaria enzymes.</p>
</sec>
</div>
</front>
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<settlement><li>Johannesbourg</li>
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