An exported kinase (FIKK4.2) that mediates virulence-associated changes in Plasmodium falciparum-infected red blood cells.
Identifieur interne : 003740 ( PubMed/Curation ); précédent : 003739; suivant : 003741An exported kinase (FIKK4.2) that mediates virulence-associated changes in Plasmodium falciparum-infected red blood cells.
Auteurs : Lev M. Kats [Australie] ; Kate M. Fernandez [Australie] ; Fiona K. Glenister [Australie] ; Susann Herrmann [Australie] ; Donna W. Buckingham [Australie] ; Ghizal Siddiqui [Australie] ; Laveena Sharma [Australie] ; Rebecca Bamert [Australie] ; Isabelle Lucet [Australie] ; Micheline Guillotte [France] ; Odile Mercereau-Puijalon [France] ; Brian M. Cooke [Australie]Source :
- International journal for parasitology [ 1879-0135 ] ; 2014.
Descripteurs français
- KwdFr :
- Facteurs de virulence (génétique), Facteurs de virulence (métabolisme), Humains, Phosphotransferases (génétique), Phosphotransferases (métabolisme), Plasmodium falciparum (enzymologie), Plasmodium falciparum (génétique), Techniques de knock-out de gènes, Transport de protéines, Érythrocytes (parasitologie).
- MESH :
- enzymologie : Plasmodium falciparum.
- génétique : Facteurs de virulence, Phosphotransferases, Plasmodium falciparum.
- métabolisme : Facteurs de virulence, Phosphotransferases.
- parasitologie : Érythrocytes.
- Humains, Techniques de knock-out de gènes, Transport de protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Phosphotransferases, Virulence Factors.
- chemical , metabolism : Phosphotransferases, Virulence Factors.
- enzymology : Plasmodium falciparum.
- genetics : Plasmodium falciparum.
- parasitology : Erythrocytes.
- Gene Knockout Techniques, Humans, Protein Transport.
Abstract
Alteration of the adhesive and mechanical properties of red blood cells caused by infection with the malaria parasite Plasmodium falciparum underpin both its survival and extreme pathogenicity. A unique family of parasite putative exported kinases, collectively called FIKK (Phenylalanine (F) - Isoleucine (I) - Lysine (K) - Lysine (K)), has recently been implicated in these pathophysiological processes, however, their precise function in P. falciparum-infected red blood cells or their likely role in malaria pathogenesis remain unknown. Here, for the first time, we demonstrate that one member of the FIKK family, FIKK4.2, can function as an active kinase and is localised in a novel and distinct compartment of the parasite-infected red blood cell which we have called K-dots. Notably, targeted disruption of the gene encoding FIKK4.2 (fikk4.2) dramatically alters the parasite's ability to modify and remodel the red blood cells in which it multiplies. Specifically, red blood cells infected with fikk4.2 knockout parasites were significantly less rigid and less adhesive when compared with red blood cells infected with normal parasites from which the transgenic clones had been derived, despite expressing similar levels of the major cytoadhesion ligand, PfEMP1, on the red blood cell surface. Notably, these changes were accompanied by dramatically altered knob-structures on infected red blood cells that play a key role in cytoadhesion which is responsible for much of the pathogenesis associated with falciparum malaria. Taken together, our data identifies FIKK4.2 as an important kinase in the pathogenesis of P. falciparum malaria and strengthens the attractiveness of FIKK kinases as targets for the development of novel next-generation anti-malaria drugs.
DOI: 10.1016/j.ijpara.2014.01.003
PubMed: 24530877
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Cooke</name><affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia. Electronic address: brian.cooke@monash.edu.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800</wicri:regionArea></affiliation></author></analytic><series><title level="j">International journal for parasitology</title><idno type="eISSN">1879-0135</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Erythrocytes (parasitology)</term><term>Gene Knockout Techniques</term><term>Humans</term><term>Phosphotransferases (genetics)</term><term>Phosphotransferases (metabolism)</term><term>Plasmodium falciparum (enzymology)</term><term>Plasmodium falciparum (genetics)</term><term>Protein Transport</term><term>Virulence Factors (genetics)</term><term>Virulence Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Facteurs de virulence (génétique)</term><term>Facteurs de virulence (métabolisme)</term><term>Humains</term><term>Phosphotransferases (génétique)</term><term>Phosphotransferases (métabolisme)</term><term>Plasmodium falciparum (enzymologie)</term><term>Plasmodium falciparum (génétique)</term><term>Techniques de knock-out de gènes</term><term>Transport de protéines</term><term>Érythrocytes (parasitologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Phosphotransferases</term><term>Virulence Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Phosphotransferases</term><term>Virulence Factors</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteurs de virulence</term><term>Phosphotransferases</term><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de virulence</term><term>Phosphotransferases</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Érythrocytes</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Erythrocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Knockout Techniques</term><term>Humans</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Techniques de knock-out de gènes</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Alteration of the adhesive and mechanical properties of red blood cells caused by infection with the malaria parasite Plasmodium falciparum underpin both its survival and extreme pathogenicity. A unique family of parasite putative exported kinases, collectively called FIKK (Phenylalanine (F) - Isoleucine (I) - Lysine (K) - Lysine (K)), has recently been implicated in these pathophysiological processes, however, their precise function in P. falciparum-infected red blood cells or their likely role in malaria pathogenesis remain unknown. Here, for the first time, we demonstrate that one member of the FIKK family, FIKK4.2, can function as an active kinase and is localised in a novel and distinct compartment of the parasite-infected red blood cell which we have called K-dots. Notably, targeted disruption of the gene encoding FIKK4.2 (fikk4.2) dramatically alters the parasite's ability to modify and remodel the red blood cells in which it multiplies. Specifically, red blood cells infected with fikk4.2 knockout parasites were significantly less rigid and less adhesive when compared with red blood cells infected with normal parasites from which the transgenic clones had been derived, despite expressing similar levels of the major cytoadhesion ligand, PfEMP1, on the red blood cell surface. Notably, these changes were accompanied by dramatically altered knob-structures on infected red blood cells that play a key role in cytoadhesion which is responsible for much of the pathogenesis associated with falciparum malaria. Taken together, our data identifies FIKK4.2 as an important kinase in the pathogenesis of P. falciparum malaria and strengthens the attractiveness of FIKK kinases as targets for the development of novel next-generation anti-malaria drugs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24530877</PMID><DateCreated><Year>2014</Year><Month>03</Month><Day>31</Day></DateCreated><DateCompleted><Year>2014</Year><Month>11</Month><Day>18</Day></DateCompleted><DateRevised><Year>2014</Year><Month>03</Month><Day>31</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0135</ISSN><JournalIssue CitedMedium="Internet"><Volume>44</Volume><Issue>5</Issue><PubDate><Year>2014</Year><Month>Apr</Month></PubDate></JournalIssue><Title>International journal for parasitology</Title><ISOAbbreviation>Int. J. Parasitol.</ISOAbbreviation></Journal><ArticleTitle>An exported kinase (FIKK4.2) that mediates virulence-associated changes in Plasmodium falciparum-infected red blood cells.</ArticleTitle><Pagination><MedlinePgn>319-28</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijpara.2014.01.003</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0020-7519(14)00028-9</ELocationID><Abstract><AbstractText>Alteration of the adhesive and mechanical properties of red blood cells caused by infection with the malaria parasite Plasmodium falciparum underpin both its survival and extreme pathogenicity. A unique family of parasite putative exported kinases, collectively called FIKK (Phenylalanine (F) - Isoleucine (I) - Lysine (K) - Lysine (K)), has recently been implicated in these pathophysiological processes, however, their precise function in P. falciparum-infected red blood cells or their likely role in malaria pathogenesis remain unknown. Here, for the first time, we demonstrate that one member of the FIKK family, FIKK4.2, can function as an active kinase and is localised in a novel and distinct compartment of the parasite-infected red blood cell which we have called K-dots. Notably, targeted disruption of the gene encoding FIKK4.2 (fikk4.2) dramatically alters the parasite's ability to modify and remodel the red blood cells in which it multiplies. Specifically, red blood cells infected with fikk4.2 knockout parasites were significantly less rigid and less adhesive when compared with red blood cells infected with normal parasites from which the transgenic clones had been derived, despite expressing similar levels of the major cytoadhesion ligand, PfEMP1, on the red blood cell surface. Notably, these changes were accompanied by dramatically altered knob-structures on infected red blood cells that play a key role in cytoadhesion which is responsible for much of the pathogenesis associated with falciparum malaria. Taken together, our data identifies FIKK4.2 as an important kinase in the pathogenesis of P. falciparum malaria and strengthens the attractiveness of FIKK kinases as targets for the development of novel next-generation anti-malaria drugs.</AbstractText><CopyrightInformation>Copyright © 2014 Australian Society for Parasitology Inc. Published by Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kats</LastName><ForeName>Lev M</ForeName><Initials>LM</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernandez</LastName><ForeName>Kate M</ForeName><Initials>KM</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Glenister</LastName><ForeName>Fiona K</ForeName><Initials>FK</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrmann</LastName><ForeName>Susann</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Buckingham</LastName><ForeName>Donna W</ForeName><Initials>DW</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Siddiqui</LastName><ForeName>Ghizal</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sharma</LastName><ForeName>Laveena</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bamert</LastName><ForeName>Rebecca</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lucet</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guillotte</LastName><ForeName>Micheline</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Unité d'Immunologie Moléculaire des Parasites, Paris, France; Centre National de la Recherche Scientifique, URA 2581, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mercereau-Puijalon</LastName><ForeName>Odile</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Unité d'Immunologie Moléculaire des Parasites, Paris, France; Centre National de la Recherche Scientifique, URA 2581, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cooke</LastName><ForeName>Brian M</ForeName><Initials>BM</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia. Electronic address: brian.cooke@monash.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>02</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Int J Parasitol</MedlineTA><NlmUniqueID>0314024</NlmUniqueID><ISSNLinking>0020-7519</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037521">Virulence Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D010770">Phosphotransferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000469" MajorTopicYN="Y">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055786" MajorTopicYN="N">Gene Knockout Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010770" MajorTopicYN="N">Phosphotransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037521" MajorTopicYN="N">Virulence Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cell adhesion</Keyword><Keyword MajorTopicYN="N">Cell mechanics</Keyword><Keyword MajorTopicYN="N">Exported proteins</Keyword><Keyword MajorTopicYN="N">Kinases</Keyword><Keyword MajorTopicYN="N">Malaria</Keyword><Keyword MajorTopicYN="N">Plasmodium falciparum</Keyword><Keyword MajorTopicYN="N">Red blood cell</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>01</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>01</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>01</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>11</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24530877</ArticleId><ArticleId IdType="pii">S0020-7519(14)00028-9</ArticleId><ArticleId IdType="doi">10.1016/j.ijpara.2014.01.003</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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