{"doi":"10.1016/j.jsb.2016.06.017","title":"Native structure of a retroviral envelope protein and its conformational change upon interaction with the target cell","abstract":null,"journal":"Journal of Structural Biology","year":2017,"id":647245,"datarank":0.5456379239589579,"base_score":3.6375861597263857,"endowment":3.6375861597263857,"self_citation_contribution":0.5456379239589579,"citation_network_contribution":0.0,"self_endowment_contribution":0.5456379239589579,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":37,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1686192,"name":"Daven Vasishtan","orcid":null,"position":1,"is_corresponding":false},{"id":616286,"name":"C. Alistair Siebert","orcid":"0000-0002-8126-1979","position":2,"is_corresponding":false},{"id":1686193,"name":"Cathy Whittle","orcid":null,"position":3,"is_corresponding":false},{"id":1686194,"name":"Maik J. Lehmann","orcid":null,"position":4,"is_corresponding":false},{"id":241931,"name":"Walther Mothes","orcid":"0000-0002-3367-7240","position":5,"is_corresponding":false},{"id":225883,"name":"Kay Grünewald","orcid":"0000-0002-4788-2691","position":6,"is_corresponding":false},{"id":1686191,"name":"Christiane Riedel","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Native structure of a retroviral envelope protein and its conformational change upon interaction with the target cell","abstract":"Enveloped viruses enter their host cells by membrane fusion. The process of attachment and fusion in retroviruses is mediated by a single viral envelope glycoprotein (Env). Conformational changes of Env in the course of fusion are a focus of intense studies. Here we provide further insight into the changes occurring in retroviral Env during its initial interaction with the cell, employing murine leukemia virus (MLV) as model system. We first determined the structure of both natively membrane anchored MLV Env and MLV Env tagged with YFP in the proline rich region (PRR) by electron cryo tomography (cET) and sub-volume averaging. At a resolution of ∼20Å, native MLV Env presents as a hollow trimer (height ∼85Å, diameter ∼120Å) composed of step-shaped protomers. The major difference to the YFP-tagged protein was in regions outside of the central trimer. Next, we focused on elucidating the changes in MLV Env upon interaction with a host cell. Virus interaction with the plasma membrane occurred over a large surface and Env clustering on the binding site was observed. Sub-volume averaging did yield a low-resolution structure of Env interacting with the cell, which had lost its threefold symmetry and was elongated by ∼35Å in comparison to the unbound protein. This indicates a major rearrangement of Env upon host cell binding. At the site of virus interaction, the otherwise clearly defined bilayer structure of the host cell plasma membrane was much less evident, indicative of integral membrane protein accumulation and/or a change in membrane lipid composition.","is_dataset_classified":null,"base_score":3.6375861597263857,"endowment":3.6375861597263857,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"27345930","pmcid":"PMC5182179","openalex_id":"https://openalex.org/W2464889995","authors":[],"funders":[{"funder_name":"Wellcome Trust","grant_id":"107806/Z/15/Z","title":null},{"funder_name":"NCATS NIH HHS","grant_id":"UL1 TR001863","title":null},{"funder_name":"NCI NIH HHS","grant_id":"R01 CA098727","title":null},{"funder_name":"Wellcome Trust","grant_id":"060208/Z/00/Z","title":null},{"funder_name":"Wellcome Trust","grant_id":"090895/Z/09/Z","title":null},{"funder_name":"Wellcome Trust","grant_id":"090532/Z/09/Z","title":null},{"funder_name":"Wellcome Trust","grant_id":"093305/Z/10/Z","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01CA098727-13","title":"Retrovirus cell-to-cell transmission"},{"funder_name":"Wellcome Trust","grant_id":"090532","title":"Understanding the genetic basis of common human diseases: core funding for the Wellcome Trust Centre for Human Genetics."},{"funder_name":"Wellcome Trust","grant_id":"090895","title":"Membrane remodelling by viral and cellular proteins: Elucidating structure and dynamics of protein complexes in their native environment by cryo electron tomography and complementary approaches."},{"funder_name":"Wellcome Trust","grant_id":"107806","title":"Membrane modulation in crucial virus-host interactions."},{"funder_name":"Wellcome Trust","grant_id":"093305","title":"Purchase of electron microscopic infrastructure to establish a multi-user facility for cryo electron microscopy, in particular cryo electron tomography."},{"funder_name":"German National Academy of Science","grant_id":"","title":null},{"funder_name":"Wellcome Trust","grant_id":"","title":null},{"funder_name":"Wellcome Trust Senior Research Fellowship","grant_id":"","title":null},{"funder_name":"Wellcome Trust","grant_id":"","title":null}],"total_grants":16,"fwci":3.0572,"citation_percentile":0.91908714,"influential_citations":0,"citation_trend":[{"year":2017,"count":3},{"year":2018,"count":7},{"year":2019,"count":7},{"year":2020,"count":4},{"year":2021,"count":5},{"year":2023,"count":2},{"year":2024,"count":2},{"year":2025,"count":6},{"year":2026,"count":1}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://www.sciencedirect.com/science/article/pii/S104784771630123X/pdf","host_type":"journal"},{"url":"https://www.sciencedirect.com/science/article/pii/S104784771630123X/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S104784771630123X?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S104784771630123X?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.jsb.2016.06.017","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/27345930","host_type":"repository"},{"url":"https://ora.ox.ac.uk/objects/uuid:92768995-4789-4b6c-ba17-4da43c4a6597","host_type":"repository"},{"url":"https://ora.ox.ac.uk/objects/uuid:f4ec2282-42f5-4bda-9a8e-41a6443b1466","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5182179","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC5182179","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC5182179?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1016/j.jsb.2016.06.017","host_type":""},{"url":"https://dx.doi.org/10.1016/j.jsb.2016.06.017","host_type":""}],"fields_of_study":["HIV Research and Treatment","Virus-based gene therapy research","Herpesvirus Infections and Treatments","0301 basic medicine","0303 health sciences","03 medical and health sciences","Binding Sites","Cryoelectron Microscopy","Leukemia Virus, Murine","Protein Conformation","Viral Envelope Proteins"],"mesh_terms":["Binding Sites","Leukemia Virus, Murine","Protein Conformation","Viral Envelope Proteins","Cryoelectron Microscopy"],"keywords":["Viral envelope","Lipid bilayer fusion","Murine leukemia virus","Viral protein","Conformational change","Trimer","Biophysics","Lipid bilayer","Cell biology","Chemistry","Protein structure","Glycoprotein","Cell membrane","Membrane","Virus","Biology","Virology","Biochemistry","Retroviridae","env","virus entry","Electron Cryo Tomography","Sub-volume Averaging","Binding Sites","Protein Conformation","Cryoelectron Microscopy","Article","Leukemia Virus, Murine","Viral Envelope Proteins","Structural Biology"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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