<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>46</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Unknown</omics_type><volume>12</volume><submitter>Hsieh MH</submitter><pubmed_abstract>Human SP-D is a potent innate immune molecule whose presence at pulmonary mucosal surfaces allows its role in immune surveillance against pathogens. Higher levels of serum SP-D have been reported in the patients with severe acute respiratory syndrome coronavirus (SARS-CoV). Studies have suggested the ability of human SP-D to recognise spike glycoprotein of SARS-CoV; its interaction with HCoV-229E strain leads to viral inhibition in human bronchial epithelial (16HBE) cells. Previous studies have reported that a recombinant fragment of human SP-D (rfhSP-D) composed of 8 Gly-X-Y repeats, neck and CRD region, can act against a range of viral pathogens including influenza A Virus and Respiratory Syncytial Virus &lt;i>in vitro&lt;/i>, &lt;i>in vivo&lt;/i> and &lt;i>ex vivo&lt;/i>. In this context, this study was aimed at examining the likely protective role of rfhSP-D against SARS-CoV-2 infection. rfhSP-D showed a dose-responsive binding to S1 spike protein of SARS-CoV-2 and its receptor binding domain. Importantly, rfhSP-D inhibited interaction of S1 protein with the HEK293T cells overexpressing human angiotensin converting enzyme 2 (hACE2). The protective role of rfhSP-D against SARS-CoV-2 infection as an entry inhibitor was further validated by the use of pseudotyped lentiviral particles expressing SARS-CoV-2 S1 protein; ~0.5 RLU fold reduction in viral entry was seen following treatment with rfhSP-D (10 µg/ml). These results highlight the therapeutic potential of rfhSP-D in SARS-CoV-2 infection and merit pre-clinical studies in animal models.</pubmed_abstract><journal>Frontiers in immunology</journal><pagination>641360</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8161545</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Human Surfactant Protein D Binds Spike Protein and Acts as an Entry Inhibitor of SARS-CoV-2 Pseudotyped Viral Particles.</pubmed_title><pmcid>PMC8161545</pmcid><pubmed_authors>Kao HF</pubmed_authors><pubmed_authors>Beirag N</pubmed_authors><pubmed_authors>Chou YC</pubmed_authors><pubmed_authors>Madan T</pubmed_authors><pubmed_authors>Hsieh MH</pubmed_authors><pubmed_authors>Kuo WS</pubmed_authors><pubmed_authors>Kishore U</pubmed_authors><pubmed_authors>Murugaiah V</pubmed_authors><pubmed_authors>Wang JY</pubmed_authors><view_count>46</view_count></additional><is_claimable>false</is_claimable><name>Human Surfactant Protein D Binds Spike Protein and Acts as an Entry Inhibitor of SARS-CoV-2 Pseudotyped Viral Particles.</name><description>Human SP-D is a potent innate immune molecule whose presence at pulmonary mucosal surfaces allows its role in immune surveillance against pathogens. Higher levels of serum SP-D have been reported in the patients with severe acute respiratory syndrome coronavirus (SARS-CoV). Studies have suggested the ability of human SP-D to recognise spike glycoprotein of SARS-CoV; its interaction with HCoV-229E strain leads to viral inhibition in human bronchial epithelial (16HBE) cells. Previous studies have reported that a recombinant fragment of human SP-D (rfhSP-D) composed of 8 Gly-X-Y repeats, neck and CRD region, can act against a range of viral pathogens including influenza A Virus and Respiratory Syncytial Virus &lt;i>in vitro&lt;/i>, &lt;i>in vivo&lt;/i> and &lt;i>ex vivo&lt;/i>. In this context, this study was aimed at examining the likely protective role of rfhSP-D against SARS-CoV-2 infection. rfhSP-D showed a dose-responsive binding to S1 spike protein of SARS-CoV-2 and its receptor binding domain. Importantly, rfhSP-D inhibited interaction of S1 protein with the HEK293T cells overexpressing human angiotensin converting enzyme 2 (hACE2). The protective role of rfhSP-D against SARS-CoV-2 infection as an entry inhibitor was further validated by the use of pseudotyped lentiviral particles expressing SARS-CoV-2 S1 protein; ~0.5 RLU fold reduction in viral entry was seen following treatment with rfhSP-D (10 µg/ml). These results highlight the therapeutic potential of rfhSP-D in SARS-CoV-2 infection and merit pre-clinical studies in animal models.</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021</publication><modification>2022-02-10T13:18:47.944Z</modification><creation>2022-02-10T13:18:47.944Z</creation></dates><accession>S-EPMC8161545</accession><cross_references><pubmed>34054808</pubmed><doi>10.3389/fimmu.2021.641360</doi></cross_references></HashMap>