Probing the equatorial groove of the hookworm protein and vaccine candidate antigen, Na-ASP-2.
Identifieur interne : 003605 ( Main/Exploration ); précédent : 003604; suivant : 003606Probing the equatorial groove of the hookworm protein and vaccine candidate antigen, Na-ASP-2.
Auteurs : Lyndel Mason [Australie] ; Leon Tribolet [Australie] ; Anne Simon [France] ; Natascha Von Gnielinski [Australie] ; Lisa Nienaber [Australie] ; Paul Taylor [Royaume-Uni] ; Charlene Willis [Australie] ; Malcolm K. Jones [Australie] ; Paul W. Sternberg [États-Unis] ; Robin B. Gasser [Australie] ; Alex Loukas [Australie] ; Andreas Hofmann [Australie]Source :
- The international journal of biochemistry & cell biology [ 1878-5875 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Antigènes d'helminthe (), Antigènes d'helminthe (immunologie), Antigènes d'helminthe (métabolisme), Cristallographie aux rayons X, Modèles moléculaires, Necator americanus (), Necator americanus (isolement et purification), Necator americanus (métabolisme), Nécatorose (parasitologie), Phosphoric monoester hydrolases (), Phosphoric monoester hydrolases (métabolisme), Protéines d'helminthes (), Protéines d'helminthes (immunologie), Protéines d'helminthes (métabolisme), Sites de fixation, Structure tertiaire des protéines, Vaccins (), Vaccins (immunologie).
- MESH :
- immunologie : Antigènes d'helminthe, Protéines d'helminthes, Vaccins.
- isolement et purification : Necator americanus.
- métabolisme : Antigènes d'helminthe, Necator americanus, Phosphoric monoester hydrolases, Protéines d'helminthes.
- parasitologie : Nécatorose.
- Animaux, Antigènes d'helminthe, Cristallographie aux rayons X, Modèles moléculaires, Necator americanus, Phosphoric monoester hydrolases, Protéines d'helminthes, Sites de fixation, Structure tertiaire des protéines, Vaccins.
English descriptors
- KwdEn :
- Animals, Antigens, Helminth (chemistry), Antigens, Helminth (immunology), Antigens, Helminth (metabolism), Binding Sites, Crystallography, X-Ray, Helminth Proteins (chemistry), Helminth Proteins (immunology), Helminth Proteins (metabolism), Models, Molecular, Necator americanus (chemistry), Necator americanus (isolation & purification), Necator americanus (metabolism), Necatoriasis (parasitology), Phosphoric Monoester Hydrolases (chemistry), Phosphoric Monoester Hydrolases (metabolism), Protein Structure, Tertiary, Vaccines (chemistry), Vaccines (immunology).
- MESH :
- chemical , chemistry : Antigens, Helminth, Helminth Proteins, Phosphoric Monoester Hydrolases, Vaccines.
- chemical , immunology : Antigens, Helminth, Helminth Proteins, Vaccines.
- chemical , metabolism : Antigens, Helminth, Helminth Proteins, Phosphoric Monoester Hydrolases.
- chemistry : Necator americanus.
- isolation & purification : Necator americanus.
- metabolism : Necator americanus.
- parasitology : Necatoriasis.
- Animals, Binding Sites, Crystallography, X-Ray, Models, Molecular, Protein Structure, Tertiary.
Abstract
Hookworm activation-associated secreted proteins can be structurally classified into at least three different groups. The hallmark feature of Group 1 activation-associated secreted proteins is a prominent equatorial groove, which is inferred to form a ligand binding site. Furthermore, a conserved tandem histidine motif is located in the centre of the groove and believed to provide or support a yet to be determined catalytic activity. Here, we report three-dimensional crystal structures of Na-ASP-2, an L3-secreted activation-associated secreted protein from the human hookworm Necator americanus, which demonstrate transition metal binding ability of the conserved tandem histidine motif. We further identified moderate phosphohydrolase activity of recombinant Na-ASP-2, which relates to the tandem histidine motif. By panning a random 12-mer peptide phage library, we identified a peptide with high similarity to the human calcium-activated potassium channel SK3, and confirm binding of the synthetic peptide to recombinant Na-ASP-2 by differential scanning fluorimetry. Potential binding modes of the peptide to Na-ASP-2 were studied by molecular dynamics simulations which clearly identify a preferred topology of the Na-ASP-2:SK3 peptide complex.
DOI: 10.1016/j.biocel.2014.03.003
PubMed: 24631931
Affiliations:
- Australie, France, Royaume-Uni, États-Unis
- Californie, Victoria (État), Écosse
- Melbourne, Édimbourg
- Université d'Édimbourg, Université de Melbourne
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Le document en format XML
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Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Tribolet, Leon" sort="Tribolet, Leon" uniqKey="Tribolet L" first="Leon" last="Tribolet">Leon Tribolet</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Centre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Simon, Anne" sort="Simon, Anne" uniqKey="Simon A" first="Anne" last="Simon">Anne Simon</name><affiliation wicri:level="1"><nlm:affiliation>Université Lyon 1, Villeurbanne cedex, and Laboratoire Chimie et Biologie des Membranes et des Nanoobjets, Université Bordeaux, CBMN, UMR 5248, 33600 Pessac, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université Lyon 1, Villeurbanne cedex, and Laboratoire Chimie et Biologie des Membranes et des Nanoobjets, Université Bordeaux, CBMN, UMR 5248, 33600 Pessac</wicri:regionArea><wicri:noRegion>33600 Pessac</wicri:noRegion><wicri:noRegion>33600 Pessac</wicri:noRegion></affiliation></author><author><name sortKey="Von Gnielinski, Natascha" sort="Von Gnielinski, Natascha" uniqKey="Von Gnielinski N" first="Natascha" last="Von Gnielinski">Natascha Von Gnielinski</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Nienaber, Lisa" sort="Nienaber, Lisa" uniqKey="Nienaber L" first="Lisa" last="Nienaber">Lisa Nienaber</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Taylor, Paul" sort="Taylor, Paul" uniqKey="Taylor P" first="Paul" last="Taylor">Paul Taylor</name><affiliation wicri:level="4"><nlm:affiliation>Institute for Structural Biology, School of Biological Sciences, The University of Edinburgh, Scotland, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute for Structural Biology, School of Biological Sciences, The University of Edinburgh, Scotland</wicri:regionArea><orgName type="university">Université d'Édimbourg</orgName><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName></affiliation></author><author><name sortKey="Willis, Charlene" sort="Willis, Charlene" uniqKey="Willis C" first="Charlene" last="Willis">Charlene Willis</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia; School of Veterinary Science, The University of Queensland, Gatton, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia; School of Veterinary Science, The University of Queensland, Gatton, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Jones, Malcolm K" sort="Jones, Malcolm K" uniqKey="Jones M" first="Malcolm K" last="Jones">Malcolm K. Jones</name><affiliation wicri:level="1"><nlm:affiliation>School of Veterinary Science, The University of Queensland, Gatton, Queensland, Australia; Queensland Institute of Medical Research, Herston, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Veterinary Science, The University of Queensland, Gatton, Queensland, Australia; Queensland Institute of Medical Research, Herston, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Sternberg, Paul W" sort="Sternberg, Paul W" uniqKey="Sternberg P" first="Paul W" last="Sternberg">Paul W. Sternberg</name><affiliation wicri:level="2"><nlm:affiliation>Biology Division, California Institute of Technology, Pasadena, CA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biology Division, California Institute of Technology, Pasadena, CA</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Gasser, Robin B" sort="Gasser, Robin B" uniqKey="Gasser R" first="Robin B" last="Gasser">Robin B. Gasser</name><affiliation wicri:level="4"><nlm:affiliation>Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Veterinary Science, 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="Loukas, Alex" sort="Loukas, Alex" uniqKey="Loukas A" first="Alex" last="Loukas">Alex Loukas</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, Queensland, Australia. Electronic address: alex.loukas@jcu.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Centre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Hofmann, Andreas" sort="Hofmann, Andreas" uniqKey="Hofmann A" first="Andreas" last="Hofmann">Andreas Hofmann</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria, Australia. Electronic address: a.hofmann@griffith.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria</wicri:regionArea><wicri:noRegion>Victoria</wicri:noRegion></affiliation></author></analytic><series><title level="j">The international journal of biochemistry & cell biology</title><idno type="eISSN">1878-5875</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antigens, Helminth (chemistry)</term><term>Antigens, Helminth (immunology)</term><term>Antigens, Helminth (metabolism)</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Helminth Proteins (chemistry)</term><term>Helminth Proteins (immunology)</term><term>Helminth Proteins (metabolism)</term><term>Models, Molecular</term><term>Necator americanus (chemistry)</term><term>Necator americanus (isolation & purification)</term><term>Necator americanus (metabolism)</term><term>Necatoriasis (parasitology)</term><term>Phosphoric Monoester Hydrolases (chemistry)</term><term>Phosphoric Monoester Hydrolases (metabolism)</term><term>Protein Structure, Tertiary</term><term>Vaccines (chemistry)</term><term>Vaccines (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigènes d'helminthe ()</term><term>Antigènes d'helminthe (immunologie)</term><term>Antigènes d'helminthe (métabolisme)</term><term>Cristallographie aux rayons X</term><term>Modèles moléculaires</term><term>Necator americanus ()</term><term>Necator americanus (isolement et purification)</term><term>Necator americanus (métabolisme)</term><term>Nécatorose (parasitologie)</term><term>Phosphoric monoester hydrolases ()</term><term>Phosphoric monoester hydrolases (métabolisme)</term><term>Protéines d'helminthes ()</term><term>Protéines d'helminthes (immunologie)</term><term>Protéines d'helminthes (métabolisme)</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Vaccins ()</term><term>Vaccins (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term><term>Phosphoric Monoester Hydrolases</term><term>Vaccines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term><term>Vaccines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term><term>Phosphoric Monoester Hydrolases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Necator americanus</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes d'helminthe</term><term>Protéines d'helminthes</term><term>Vaccins</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Necator americanus</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Necator americanus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Necator americanus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antigènes d'helminthe</term><term>Necator americanus</term><term>Phosphoric monoester hydrolases</term><term>Protéines d'helminthes</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Nécatorose</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Necatoriasis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Models, Molecular</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antigènes d'helminthe</term><term>Cristallographie aux rayons X</term><term>Modèles moléculaires</term><term>Necator americanus</term><term>Phosphoric monoester hydrolases</term><term>Protéines d'helminthes</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Vaccins</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Hookworm activation-associated secreted proteins can be structurally classified into at least three different groups. The hallmark feature of Group 1 activation-associated secreted proteins is a prominent equatorial groove, which is inferred to form a ligand binding site. Furthermore, a conserved tandem histidine motif is located in the centre of the groove and believed to provide or support a yet to be determined catalytic activity. Here, we report three-dimensional crystal structures of Na-ASP-2, an L3-secreted activation-associated secreted protein from the human hookworm Necator americanus, which demonstrate transition metal binding ability of the conserved tandem histidine motif. We further identified moderate phosphohydrolase activity of recombinant Na-ASP-2, which relates to the tandem histidine motif. By panning a random 12-mer peptide phage library, we identified a peptide with high similarity to the human calcium-activated potassium channel SK3, and confirm binding of the synthetic peptide to recombinant Na-ASP-2 by differential scanning fluorimetry. Potential binding modes of the peptide to Na-ASP-2 were studied by molecular dynamics simulations which clearly identify a preferred topology of the Na-ASP-2:SK3 peptide complex.</div></front></TEI><affiliations><list><country><li>Australie</li><li>France</li><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Californie</li><li>Victoria (État)</li><li>Écosse</li></region><settlement><li>Melbourne</li><li>Édimbourg</li></settlement><orgName><li>Université d'Édimbourg</li><li>Université de Melbourne</li></orgName></list><tree><country name="Australie"><noRegion><name sortKey="Mason, Lyndel" sort="Mason, Lyndel" uniqKey="Mason L" first="Lyndel" last="Mason">Lyndel Mason</name></noRegion><name sortKey="Gasser, Robin B" sort="Gasser, Robin B" uniqKey="Gasser R" first="Robin B" last="Gasser">Robin B. Gasser</name><name sortKey="Hofmann, Andreas" sort="Hofmann, Andreas" uniqKey="Hofmann A" first="Andreas" last="Hofmann">Andreas Hofmann</name><name sortKey="Jones, Malcolm K" sort="Jones, Malcolm K" uniqKey="Jones M" first="Malcolm K" last="Jones">Malcolm K. Jones</name><name sortKey="Loukas, Alex" sort="Loukas, Alex" uniqKey="Loukas A" first="Alex" last="Loukas">Alex Loukas</name><name sortKey="Nienaber, Lisa" sort="Nienaber, Lisa" uniqKey="Nienaber L" first="Lisa" last="Nienaber">Lisa Nienaber</name><name sortKey="Tribolet, Leon" sort="Tribolet, Leon" uniqKey="Tribolet L" first="Leon" last="Tribolet">Leon Tribolet</name><name sortKey="Von Gnielinski, Natascha" sort="Von Gnielinski, Natascha" uniqKey="Von Gnielinski N" first="Natascha" last="Von Gnielinski">Natascha Von Gnielinski</name><name sortKey="Willis, Charlene" sort="Willis, Charlene" uniqKey="Willis C" first="Charlene" last="Willis">Charlene Willis</name></country><country name="France"><noRegion><name sortKey="Simon, Anne" sort="Simon, Anne" uniqKey="Simon A" first="Anne" last="Simon">Anne Simon</name></noRegion></country><country name="Royaume-Uni"><region name="Écosse"><name sortKey="Taylor, Paul" sort="Taylor, Paul" uniqKey="Taylor P" first="Paul" last="Taylor">Paul Taylor</name></region></country><country name="États-Unis"><region name="Californie"><name sortKey="Sternberg, Paul W" sort="Sternberg, Paul W" uniqKey="Sternberg P" first="Paul W" last="Sternberg">Paul W. Sternberg</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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