AustralieFrV1, Main, Exploration, bibRecord, 003275

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

Identifieur interne : 003275 ( Main/Exploration ); précédent : 003274; suivant : 003276

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 [ 1553-7366 ] ; 2015.

RBID : PMC:4687929

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.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687929

DOI: 10.1371/journal.ppat.1005343
PubMed: 26694741
PubMed Central: 4687929

Affiliations:

Le document en format XML

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 Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main"><italic>Plasmodium falciparum</italic>
 Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes</title>
<author><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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</nlm:aff>
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<wicri:regionArea>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Victoria</wicri:regionArea>
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<author><name sortKey="Dorin Semblat, Dominique" sort="Dorin Semblat, Dominique" uniqKey="Dorin Semblat D" first="Dominique" last="Dorin-Semblat">Dominique Dorin-Semblat</name>
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</nlm:aff>
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</affiliation>
</author>
<author><name sortKey="Gilson, Paul R" sort="Gilson, Paul R" uniqKey="Gilson P" first="Paul R." last="Gilson">Paul R. Gilson</name>
<affiliation wicri:level="1"><nlm:aff id="aff003"><addr-line>Burnet Institute, Melbourne, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Burnet Institute, Melbourne, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff007"><addr-line>Department of Immunology, Monash University, Melbourne, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Department of Immunology, Monash University, Melbourne, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Crabb, Brendan S" sort="Crabb, Brendan S" uniqKey="Crabb B" first="Brendan S." last="Crabb">Brendan S. Crabb</name>
<affiliation wicri:level="1"><nlm:aff id="aff003"><addr-line>Burnet Institute, Melbourne, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Burnet Institute, Melbourne, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff007"><addr-line>Department of Immunology, Monash University, Melbourne, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Department of Immunology, Monash University, Melbourne, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
<affiliation wicri:level="4"><nlm:aff id="aff008"><addr-line>Department of Microbiology & Immunology, The University of Melbourne, Parkville, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Department of Microbiology & Immunology, The University of Melbourne, Parkville, Victoria</wicri:regionArea>
<orgName type="university">Université de Melbourne</orgName>
<placeName><settlement type="city">Melbourne</settlement>
<region type="état">Victoria (État)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Cowman, Alan F" sort="Cowman, Alan F" uniqKey="Cowman A" first="Alan F." last="Cowman">Alan F. Cowman</name>
<affiliation wicri:level="1"><nlm:aff id="aff001"><addr-line>The Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>The Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
<affiliation wicri:level="4"><nlm:aff id="aff002"><addr-line>Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia</addr-line>
</nlm:aff>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Department of Medical Biology, The University of Melbourne, Parkville, Victoria</wicri:regionArea>
<orgName type="university">Université de Melbourne</orgName>
<placeName><settlement type="city">Melbourne</settlement>
<region type="état">Victoria (État)</region>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j">PLoS Pathogens</title>
<idno type="ISSN">1553-7366</idno>
<idno type="eISSN">1553-7374</idno>
<imprint><date when="2015">2015</date>
</imprint>
</series>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Erythrocytes (microbiology)</term>
<term>Humans</term>
<term>Malaria, Falciparum (metabolism)</term>
<term>Merozoites (metabolism)</term>
<term>Molecular Sequence Data</term>
<term>Phosphorylation</term>
<term>Phosphotransferases (metabolism)</term>
<term>Plasmodium falciparum (metabolism)</term>
<term>Plasmodium falciparum (pathogenicity)</term>
<term>Protozoan Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Mérozoïtes (métabolisme)</term>
<term>Paludisme à Plasmodium falciparum (métabolisme)</term>
<term>Phosphorylation</term>
<term>Phosphotransferases (métabolisme)</term>
<term>Plasmodium falciparum (métabolisme)</term>
<term>Plasmodium falciparum (pathogénicité)</term>
<term>Protéines de protozoaire (métabolisme)</term>
<term>Séquence d'acides aminés</term>
<term>Érythrocytes (microbiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Phosphotransferases</term>
<term>Protozoan Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Malaria, Falciparum</term>
<term>Merozoites</term>
<term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Érythrocytes</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Erythrocytes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mérozoïtes</term>
<term>Paludisme à Plasmodium falciparum</term>
<term>Phosphotransferases</term>
<term>Plasmodium falciparum</term>
<term>Protéines de protozoaire</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Phosphorylation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Phosphorylation</term>
<term>Séquence d'acides aminés</term>
</keywords>
</textClass>
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</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The most severe form of malaria in humans is caused by the protozoan parasite <italic>Plasmodium falciparum</italic>
. 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 <italic>Plasmodium falciparum</italic>
, 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 <italic>in vitro</italic>
. Depletion of PfCK2, a kinase implicated to phosphorylate these cytoplasmic tails, blocks <italic>P</italic>
. <italic>falciparum</italic>
 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.</p>
</div>
</front>
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   |texte=   Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes
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Serveur d'exploration sur les relations entre la France et l'Australie

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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	Serveur d'exploration sur les relations entre la France et l'Australie
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