Computational Insights into the Interaction of the Conserved Cysteine-Noose Domain of the Human Respiratory Syncytial Virus G Protein with the Canonical Fractalkine Binding site of Transmembrane Receptor CX3CR1 Isoforms

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorFederal University of Rio de Janeiro-
Autor(es): dc.creatorPiloto, João Victor-
Autor(es): dc.creatorDias, Raphael Vinicius Rodrigues-
Autor(es): dc.creatorMazucato, Wan Suk Augusto-
Autor(es): dc.creatorFossey, Marcelo Andres-
Autor(es): dc.creatorde Melo, Fernando Alves-
Autor(es): dc.creatorAlmeida, Fabio Ceneviva Lacerda-
Autor(es): dc.creatorde Souza, Fatima Pereira-
Autor(es): dc.creatorCaruso, Icaro Putinhon-
Data de aceite: dc.date.accessioned2025-08-21T17:36:49Z-
Data de disponibilização: dc.date.available2025-08-21T17:36:49Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-04-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/membranes14040084-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/307889-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/307889-
Descrição: dc.descriptionThe human Respiratory Syncytial Virus (hRSV) stands as one of the most common causes of acute respiratory diseases. The infectivity of this virus is intricately linked to its membrane proteins, notably the attachment glycoprotein (G protein). The latter plays a key role in facilitating the attachment of hRSV to respiratory tract epithelial cells, thereby initiating the infection process. The present study aimed to characterize the interaction of the conserved cysteine-noose domain of hRSV G protein (cndG) with the transmembrane CX3C motif chemokine receptor 1 (CX3CR1) isoforms using computational tools of molecular modeling, docking, molecular dynamics simulations, and binding free energy calculations. From MD simulations of the molecular system embedded in the POPC lipid bilayer, we showed a stable interaction of cndG with the canonical fractalkine binding site in the N-terminal cavity of the CX3CR1 isoforms and identified that residues in the extracellular loop 2 (ECL2) region and Glu279 of this receptor are pivotal for the stabilization of CX3CR1/cndG binding, corroborating what was reported for the interaction of the chemokine fractalkine with CX3CR1 and its structure homolog US28. Therefore, the results presented here contribute by revealing key structural points for the CX3CR1/G interaction, allowing us to better understand the biology of hRSV from its attachment process and to develop new strategies to combat it.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics São Paulo State University (UNESP)-
Descrição: dc.descriptionInstitute of Medical Biochemistry (IBqM) National Center of Nuclear Magnetic Resonance Jiri Jonas Federal University of Rio de Janeiro-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics São Paulo State University (UNESP)-
Descrição: dc.descriptionFAPESP: 2022/13050-5-
Descrição: dc.descriptionFAPESP: 2023/01632-2-
Descrição: dc.descriptionFAPESP: 2023/09642-7-
Descrição: dc.descriptionCNPq: 317157/2023-0-
Descrição: dc.descriptionCAPES: 88887.502565/2020-00-
Idioma: dc.languageen-
Relação: dc.relationMembranes-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectcomputational tools-
Palavras-chave: dc.subjectCX3CR1-
Palavras-chave: dc.subjectfractalkine binding site-
Palavras-chave: dc.subjecthRSV G protein-
Título: dc.titleComputational Insights into the Interaction of the Conserved Cysteine-Noose Domain of the Human Respiratory Syncytial Virus G Protein with the Canonical Fractalkine Binding site of Transmembrane Receptor CX3CR1 Isoforms-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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