<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Beirag N</submitter><funding>Wellcome Trust</funding><pagination>960733</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9367475</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13</volume><pubmed_abstract>Lung surfactant protein D (SP-D) and Dendritic cell-specific intercellular adhesion molecules-3 grabbing non-integrin (DC-SIGN) are pathogen recognising C-type lectin receptors. SP-D has a crucial immune function in detecting and clearing pulmonary pathogens; DC-SIGN is involved in facilitating dendritic cell interaction with naïve T cells to mount an anti-viral immune response. SP-D and DC-SIGN have been shown to interact with various viruses, including SARS-CoV-2, an enveloped RNA virus that causes COVID-19. A recombinant fragment of human SP-D (rfhSP-D) comprising of α-helical neck region, carbohydrate recognition domain, and eight N-terminal Gly-X-Y repeats has been shown to bind SARS-CoV-2 Spike protein and inhibit SARS-CoV-2 replication by preventing viral entry in Vero cells and HEK</pubmed_abstract><journal>Frontiers in immunology</journal><pubmed_title>Human surfactant protein D facilitates SARS-CoV-2 pseudotype binding and entry in DC-SIGN expressing cells, and downregulates spike protein induced inflammation.</pubmed_title><pmcid>PMC9367475</pmcid><funding_grant_id>210183</funding_grant_id><pubmed_authors>Varghese PM</pubmed_authors><pubmed_authors>Beirag N</pubmed_authors><pubmed_authors>Madan T</pubmed_authors><pubmed_authors>Idicula-Thomas S</pubmed_authors><pubmed_authors>Bulla R</pubmed_authors><pubmed_authors>Shamji MH</pubmed_authors><pubmed_authors>Kishore U</pubmed_authors><pubmed_authors>Murugaiah V</pubmed_authors><pubmed_authors>Neto MM</pubmed_authors><pubmed_authors>Kumar C</pubmed_authors><pubmed_authors>Mitchell D</pubmed_authors><pubmed_authors>Temperton N</pubmed_authors></additional><is_claimable>false</is_claimable><name>Human surfactant protein D facilitates SARS-CoV-2 pseudotype binding and entry in DC-SIGN expressing cells, and downregulates spike protein induced inflammation.</name><description>Lung surfactant protein D (SP-D) and Dendritic cell-specific intercellular adhesion molecules-3 grabbing non-integrin (DC-SIGN) are pathogen recognising C-type lectin receptors. SP-D has a crucial immune function in detecting and clearing pulmonary pathogens; DC-SIGN is involved in facilitating dendritic cell interaction with naïve T cells to mount an anti-viral immune response. SP-D and DC-SIGN have been shown to interact with various viruses, including SARS-CoV-2, an enveloped RNA virus that causes COVID-19. A recombinant fragment of human SP-D (rfhSP-D) comprising of α-helical neck region, carbohydrate recognition domain, and eight N-terminal Gly-X-Y repeats has been shown to bind SARS-CoV-2 Spike protein and inhibit SARS-CoV-2 replication by preventing viral entry in Vero cells and HEK</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-04T08:01:36.567Z</modification><creation>2025-04-04T08:01:36.567Z</creation></dates><accession>S-EPMC9367475</accession><cross_references><pubmed>35967323</pubmed><doi>10.3389/fimmu.2022.960733</doi></cross_references></HashMap>