<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>14(2)</volume><submitter>Jarahian M</submitter><pubmed_abstract>Expression of the extensively glycosylated Ebolavirus glycoprotein (EBOV-GP) induces physical alterations of surface molecules and plays a crucial role in viral pathogenicity. Here we investigate the interactions of EBOV-GP with host surface molecules using purified EBOV-GP, EBOV-GP-transfected cell lines, and EBOV-GP-pseudotyped lentiviral particles. Subsequently, we wanted to examine which receptors are involved in this recognition by binding studies to cells transfected with the EBOV-GP as well as to recombinant soluble EBOV-GP. As the viral components can also bind to inhibitory receptors of immune cells (e.g., Siglecs, TIM-1), they can even suppress the activity of immune effector cells. Our data show that natural killer (NK) cell receptors NKp44 and NKp46, selectins (CD62E/P/L), the </pubmed_abstract><journal>Journal of innate immunity</journal><pagination>135-147</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9082198</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Activating Natural Killer Cell Receptors, Selectins, and Inhibitory Siglecs Recognize Ebolavirus Glycoprotein.</pubmed_title><pmcid>PMC9082198</pmcid><pubmed_authors>Marstaller K</pubmed_authors><pubmed_authors>Ahani R</pubmed_authors><pubmed_authors>Watzl C</pubmed_authors><pubmed_authors>Banna N</pubmed_authors><pubmed_authors>Boller LK</pubmed_authors><pubmed_authors>Cid-Arregui A</pubmed_authors><pubmed_authors>Berger MR</pubmed_authors><pubmed_authors>Jarahian M</pubmed_authors><pubmed_authors>Azadmanesh K</pubmed_authors><pubmed_authors>Momburg F</pubmed_authors><pubmed_authors>Khezri A</pubmed_authors><pubmed_authors>Etemadzadeh MH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Activating Natural Killer Cell Receptors, Selectins, and Inhibitory Siglecs Recognize Ebolavirus Glycoprotein.</name><description>Expression of the extensively glycosylated Ebolavirus glycoprotein (EBOV-GP) induces physical alterations of surface molecules and plays a crucial role in viral pathogenicity. Here we investigate the interactions of EBOV-GP with host surface molecules using purified EBOV-GP, EBOV-GP-transfected cell lines, and EBOV-GP-pseudotyped lentiviral particles. Subsequently, we wanted to examine which receptors are involved in this recognition by binding studies to cells transfected with the EBOV-GP as well as to recombinant soluble EBOV-GP. As the viral components can also bind to inhibitory receptors of immune cells (e.g., Siglecs, TIM-1), they can even suppress the activity of immune effector cells. Our data show that natural killer (NK) cell receptors NKp44 and NKp46, selectins (CD62E/P/L), the </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-26T03:54:50.005Z</modification><creation>2025-02-19T03:41:50.186Z</creation></dates><accession>S-EPMC9082198</accession><cross_references><pubmed>34425576</pubmed><doi>10.1159/000517628</doi></cross_references></HashMap>