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dc.contributor.authorKalbermatter, David-
dc.contributor.authorJeckelmann, Jean-Marc-
dc.contributor.authorWyss, Marianne-
dc.contributor.authorShrestha, Neeta-
dc.contributor.authorPliatsika, Dimanthi-
dc.contributor.authorRiedl, Rainer-
dc.contributor.authorLemmin, Thomas-
dc.contributor.authorPlattet, Philippe-
dc.contributor.authorFotiadis, Dimitrios-
dc.date.accessioned2023-02-11T10:03:25Z-
dc.date.available2023-02-11T10:03:25Z-
dc.date.issued2023-02-07-
dc.identifier.issn0027-8424de_CH
dc.identifier.issn1091-6490de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/26904-
dc.description.abstractCanine distemper virus (CDV) is an enveloped RNA morbillivirus that triggers respiratory, enteric, and high incidence of severe neurological disorders. CDV induces devastating outbreaks in wild and endangered animals as well as in domestic dogs in countries associated with suboptimal vaccination programs. The receptor-binding tetrameric attachment (H)-protein is part of the morbilliviral cell entry machinery. Here, we present the cryo-electron microscopy (cryo-EM) structure and supramolecular organization of the tetrameric CDV H-protein ectodomain. The structure reveals that the morbilliviral H-protein is composed of three main domains: stalk, neck, and heads. The most unexpected feature was the inherent asymmetric architecture of the CDV H-tetramer being shaped by the neck, which folds into an almost 90° bent conformation with respect to the stalk. Consequently, two non-contacting receptor-binding H-head dimers, which are also tilted toward each other, are located on one side of an intertwined four helical bundle stalk domain. Positioning of the four protomer polypeptide chains within the neck domain is guided by a glycine residue (G158), which forms a hinge point exclusively in two protomer polypeptide chains. Molecular dynamics simulations validated the stability of the asymmetric structure under near physiological conditions and molecular docking showed that two receptor-binding sites are fully accessible. Thus, this spatial organization of the CDV H-tetramer would allow for concomitant protein interactions with the stalk and head domains without steric clashes. In summary, the structure of the CDV H-protein ectodomain provides new insights into the morbilliviral cell entry system and offers a blueprint for next-generation structure-based antiviral drug discovery.de_CH
dc.language.isoende_CH
dc.publisherNational Academy of Sciencesde_CH
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americade_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectH-protein ectodomainde_CH
dc.subjectCanine distemper virusde_CH
dc.subjectCryo-electron microscopyde_CH
dc.subjectMorbillivirus cell entryde_CH
dc.subjectStructurede_CH
dc.subject.ddc579: Mikrobiologiede_CH
dc.titleStructure and supramolecular organization of the canine distemper virus attachment glycoproteinde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.1073/pnas.2208866120de_CH
dc.identifier.pmid36716368de_CH
zhaw.funding.euNode_CH
zhaw.issue6de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.starte2208866120de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume120de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.funding.snf183481de_CH
zhaw.webfeedOrganische Chemiede_CH
zhaw.webfeedCC Drug Discoveryde_CH
zhaw.author.additionalNode_CH
zhaw.display.portraitYesde_CH
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Kalbermatter, D., Jeckelmann, J.-M., Wyss, M., Shrestha, N., Pliatsika, D., Riedl, R., Lemmin, T., Plattet, P., & Fotiadis, D. (2023). Structure and supramolecular organization of the canine distemper virus attachment glycoprotein. Proceedings of the National Academy of Sciences of the United States of America, 120(6), e2208866120. https://doi.org/10.1073/pnas.2208866120
Kalbermatter, D. et al. (2023) ‘Structure and supramolecular organization of the canine distemper virus attachment glycoprotein’, Proceedings of the National Academy of Sciences of the United States of America, 120(6), p. e2208866120. Available at: https://doi.org/10.1073/pnas.2208866120.
D. Kalbermatter et al., “Structure and supramolecular organization of the canine distemper virus attachment glycoprotein,” Proceedings of the National Academy of Sciences of the United States of America, vol. 120, no. 6, p. e2208866120, Feb. 2023, doi: 10.1073/pnas.2208866120.
KALBERMATTER, David, Jean-Marc JECKELMANN, Marianne WYSS, Neeta SHRESTHA, Dimanthi PLIATSIKA, Rainer RIEDL, Thomas LEMMIN, Philippe PLATTET und Dimitrios FOTIADIS, 2023. Structure and supramolecular organization of the canine distemper virus attachment glycoprotein. Proceedings of the National Academy of Sciences of the United States of America. 7 Februar 2023. Bd. 120, Nr. 6, S. e2208866120. DOI 10.1073/pnas.2208866120
Kalbermatter, David, Jean-Marc Jeckelmann, Marianne Wyss, Neeta Shrestha, Dimanthi Pliatsika, Rainer Riedl, Thomas Lemmin, Philippe Plattet, and Dimitrios Fotiadis. 2023. “Structure and Supramolecular Organization of the Canine Distemper Virus Attachment Glycoprotein.” Proceedings of the National Academy of Sciences of the United States of America 120 (6): e2208866120. https://doi.org/10.1073/pnas.2208866120.
Kalbermatter, David, et al. “Structure and Supramolecular Organization of the Canine Distemper Virus Attachment Glycoprotein.” Proceedings of the National Academy of Sciences of the United States of America, vol. 120, no. 6, Feb. 2023, p. e2208866120, https://doi.org/10.1073/pnas.2208866120.


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