AustralieFrV1, PubMed, Checkpoint, bibRecord, 002835

Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.

Identifieur interne : 002835 ( PubMed/Checkpoint ); précédent : 002834; suivant : 002836

Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.

Auteurs : Wai-Hong Tham [Australie] ; Nicholas T Y. Lim [Australie] ; Greta E. Weiss [Australie] ; Sash Lopaticki [Australie] ; Brendan R E. Ansell [Australie] ; Megan Bird [Australie] ; Isabelle Lucet [Australie] ; Dominique Dorin-Semblat [France] ; Christian Doerig [Australie] ; Paul R. Gilson [Australie] ; Brendan S. Crabb [Australie] ; Alan F. Cowman [Australie]

Source :

PLoS pathogens [ 1553-7374 ] ; 2015.

RBID : pubmed:26694741

Descripteurs français

KwdFr :
- Données de séquences moléculaires, Humains, Mérozoïtes (métabolisme), Paludisme à Plasmodium falciparum (métabolisme), Phosphorylation, Phosphotransferases (métabolisme), Plasmodium falciparum (métabolisme), Plasmodium falciparum (pathogénicité), Protéines de protozoaire (métabolisme), Séquence d'acides aminés, Érythrocytes (microbiologie).
MESH :
- microbiologie : Érythrocytes.
- métabolisme : Mérozoïtes, Paludisme à Plasmodium falciparum, Phosphotransferases, Plasmodium falciparum, Protéines de protozoaire.
- pathogénicité : Plasmodium falciparum.
- Données de séquences moléculaires, Humains, Phosphorylation, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence, Erythrocytes (microbiology), Humans, Malaria, Falciparum (metabolism), Merozoites (metabolism), Molecular Sequence Data, Phosphorylation, Phosphotransferases (metabolism), Plasmodium falciparum (metabolism), Plasmodium falciparum (pathogenicity), Protozoan Proteins (metabolism).
MESH :
- chemical , metabolism : Phosphotransferases, Protozoan Proteins.
- metabolism : Malaria, Falciparum, Merozoites, Plasmodium falciparum.
- microbiology : Erythrocytes.
- pathogenicity : Plasmodium falciparum.
- Amino Acid Sequence, Humans, Molecular Sequence Data, Phosphorylation.

Abstract

The most severe form of malaria in humans is caused by the protozoan parasite Plasmodium falciparum. The invasive form of malaria parasites is termed a merozoite and it employs an array of parasite proteins that bind to the host cell to mediate invasion. In Plasmodium falciparum, the erythrocyte binding-like (EBL) and reticulocyte binding-like (Rh) protein families are responsible for binding to specific erythrocyte receptors for invasion and mediating signalling events that initiate active entry of the malaria parasite. Here we have addressed the role of the cytoplasmic tails of these proteins in activating merozoite invasion after receptor engagement. We show that the cytoplasmic domains of these type 1 membrane proteins are phosphorylated in vitro. Depletion of PfCK2, a kinase implicated to phosphorylate these cytoplasmic tails, blocks P. falciparum invasion of red blood cells. We identify the crucial residues within the PfRh4 cytoplasmic domain that are required for successful parasite invasion. Live cell imaging of merozoites from these transgenic mutants show they attach but do not penetrate erythrocytes implying the PfRh4 cytoplasmic tail conveys signals important for the successful completion of the invasion process.

DOI: 10.1371/journal.ppat.1005343
PubMed: 26694741

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The most severe form of malaria in humans is caused by the protozoan parasite Plasmodium falciparum. The invasive form of malaria parasites is termed a merozoite and it employs an array of parasite proteins that bind to the host cell to mediate invasion. In Plasmodium falciparum, the erythrocyte binding-like (EBL) and reticulocyte binding-like (Rh) protein families are responsible for binding to specific erythrocyte receptors for invasion and mediating signalling events that initiate active entry of the malaria parasite. Here we have addressed the role of the cytoplasmic tails of these proteins in activating merozoite invasion after receptor engagement. We show that the cytoplasmic domains of these type 1 membrane proteins are phosphorylated in vitro. Depletion of PfCK2, a kinase implicated to phosphorylate these cytoplasmic tails, blocks P. falciparum invasion of red blood cells. We identify the crucial residues within the PfRh4 cytoplasmic domain that are required for successful parasite invasion. Live cell imaging of merozoites from these transgenic mutants show they attach but do not penetrate erythrocytes implying the PfRh4 cytoplasmic tail conveys signals important for the successful completion of the invasion process.</div>
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<Abstract><AbstractText>The most severe form of malaria in humans is caused by the protozoan parasite Plasmodium falciparum. The invasive form of malaria parasites is termed a merozoite and it employs an array of parasite proteins that bind to the host cell to mediate invasion. In Plasmodium falciparum, the erythrocyte binding-like (EBL) and reticulocyte binding-like (Rh) protein families are responsible for binding to specific erythrocyte receptors for invasion and mediating signalling events that initiate active entry of the malaria parasite. Here we have addressed the role of the cytoplasmic tails of these proteins in activating merozoite invasion after receptor engagement. We show that the cytoplasmic domains of these type 1 membrane proteins are phosphorylated in vitro. Depletion of PfCK2, a kinase implicated to phosphorylate these cytoplasmic tails, blocks P. falciparum invasion of red blood cells. We identify the crucial residues within the PfRh4 cytoplasmic domain that are required for successful parasite invasion. Live cell imaging of merozoites from these transgenic mutants show they attach but do not penetrate erythrocytes implying the PfRh4 cytoplasmic tail conveys signals important for the successful completion of the invasion process.</AbstractText>
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<Initials>BS</Initials>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology, Monash University, Melbourne, Victoria, Australia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Microbiology & Immunology, The University of Melbourne, Parkville, Victoria, Australia.</Affiliation>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia.</Affiliation>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName>
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<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
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<MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName>
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<affiliations><list><country><li>Australie</li>
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<tree><country name="Australie"><noRegion><name sortKey="Tham, Wai Hong" sort="Tham, Wai Hong" uniqKey="Tham W" first="Wai-Hong" last="Tham">Wai-Hong Tham</name>
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	Serveur d'exploration sur les relations entre la France et l'Australie
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Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.

Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.

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