<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Vaknin A</submitter><funding>United States-Israel Binational Science Foundation</funding><funding>European Research Council</funding><funding>NIAID NIH HHS</funding><funding>Israel Science Foundation</funding><funding>NIGMS NIH HHS</funding><funding>National Science Foundation</funding><pagination>1590-1601</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11091876</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(5)</volume><pubmed_abstract>Ebola virus (EBOV) is an enveloped virus that must fuse with the host cell membrane in order to release its genome and initiate infection. This process requires the action of the EBOV envelope glycoprotein (GP), encoded by the virus, which resides in the viral envelope and consists of a receptor binding subunit, GP1, and a membrane fusion subunit, GP2. Despite extensive research, a mechanistic understanding of the viral fusion process is incomplete. To investigate GP-membrane association, a key step in the fusion process, we used two approaches: high-throughput measurements of single-particle diffusion and single-molecule measurements with optical tweezers. Using these methods, we show that the presence of the endosomal Niemann-Pick C1 (NPC1) receptor is not required for primed GP-membrane</pubmed_abstract><journal>ACS infectious diseases</journal><pubmed_title>Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.</pubmed_title><pmcid>PMC11091876</pmcid><funding_grant_id>2021793</funding_grant_id><funding_grant_id>101077502</funding_grant_id><funding_grant_id>1289/20</funding_grant_id><funding_grant_id>R01 AI174645</funding_grant_id><funding_grant_id>R01 GM143773</funding_grant_id><funding_grant_id>R01 AI148784</funding_grant_id><pubmed_authors>Vaknin A</pubmed_authors><pubmed_authors>Golani G</pubmed_authors><pubmed_authors>Grossman A</pubmed_authors><pubmed_authors>Munro JB</pubmed_authors><pubmed_authors>Goren S</pubmed_authors><pubmed_authors>Durham ND</pubmed_authors><pubmed_authors>Roichman Y</pubmed_authors><pubmed_authors>Sorkin R</pubmed_authors><pubmed_authors>Lupovitz I</pubmed_authors></additional><is_claimable>false</is_claimable><name>Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.</name><description>Ebola virus (EBOV) is an enveloped virus that must fuse with the host cell membrane in order to release its genome and initiate infection. This process requires the action of the EBOV envelope glycoprotein (GP), encoded by the virus, which resides in the viral envelope and consists of a receptor binding subunit, GP1, and a membrane fusion subunit, GP2. Despite extensive research, a mechanistic understanding of the viral fusion process is incomplete. To investigate GP-membrane association, a key step in the fusion process, we used two approaches: high-throughput measurements of single-particle diffusion and single-molecule measurements with optical tweezers. Using these methods, we show that the presence of the endosomal Niemann-Pick C1 (NPC1) receptor is not required for primed GP-membrane</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 May</publication><modification>2026-06-02T06:06:12.129Z</modification><creation>2026-04-15T03:09:48.778Z</creation></dates><accession>S-EPMC11091876</accession><cross_references><pubmed>38684073</pubmed><doi>10.1021/acsinfecdis.3c00622</doi></cross_references></HashMap>