Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins


SARS-CoV-2 Proteins
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    Quantitative proteomics of hamster lung tissues infected with SARS-CoV-2 reveal host-factors having implication in the disease pathogenesis and severity

    Authors: Voddu Suresh; Varshasnata Mohanty; Kiran Avula; Arup Ghosh; Bharti Singh; R Rajendra Kumar Reddy; Amol Ratnakar Suryawanshi; Sunil Raghav; Soma Chattopadhyay; Punit Prasad; Rajeeb Kumar Swain; Rupesh Dash; Ajay Parida; Gulam Hussain Syed; Shantibhusan Senapati

    doi:10.1101/2021.03.09.434371 Date: 2021-03-09 Source: bioRxiv

    Syrian golden hamsters (Mesocricetus auratus) infected MESHD by severe acute respiratory syndrome coronavirus 2 MESHD (SARS-CoV-2) manifests lung pathology that resembles human COVID-19 MESHD patients. In this study, efforts were made to check the infectivity of a local SARS-CoV-2 isolate in hamster model and evaluate the differential expression of lung proteins during acute infection MESHD and convalescence. The findings of this study confirm the infectivity of this isolate in vivo. Analysis of clinical parameters and tissue samples shows a similar type of pathophysiological manifestation of SARS-CoV-2 infection MESHD as reported earlier in COVID-19 MESHD patients and hamsters infected with other isolates. The lung-associated pathological changes were very prominent on the 4th day post-infection (dpi), mostly resolved by 14dpi. Here, we carried out quantitative proteomic analysis of the lung tissues from SARS-CoV-2-infected MESHD hamsters at day 4 and day 14 post infection. This resulted in the identification of 1,585 differentially expressed proteins of which 68 proteins were significantly altered among both the infected groups. Pathway analysis revealed complement and coagulation cascade, platelet activation, ferroptosis and focal adhesion as the top enriched pathways. In addition, we also identified altered expression of two pulmonary surfactant-associated proteins ( Sftpd HGNC and Sftpb HGNC), known for their protective role in lung function. Together, these findings will aid in the identification of candidate biomarkers and understanding the mechanism(s) involved in SARS-CoV-2 pathogenesis.

    Human Surfactant Protein D Binds S1 and Receptor Binding Domain of Spike protein PROTEIN and acts as an entry inhibitor of SARS-CoV-2 Pseudotyped viral particles in vitro

    Authors: Miao-Hsi Hsieh; Nazar Beirag; Valarmathy Murugaiah; Yu-Chi Chou; Wen-Shuo Kuo; Hui-Fan Kao; Taruna Madan; Uday Kishore; Jiu-Yao Wang; Dinesh Tripathi; Savneet Kaur; Ekta Gupta; Sanjeev Gupta; Ne Hooi Will Loh; Mario Cannataro; Brett K Beaulieu-Jones; Riccardo Bellazzi; Giuseppe Agapito; Mario Alessiani; Bruce J Aronow; Douglas S Bell; Antonio Bellasi; Vincent Benoit; Michele Beraghi; Martin Boeker; John Booth; Silvano Bosari; Florence T Bourgeois; Nicholas W Brown; Luca Chiovato; Lorenzo Chiudinelli; Arianna Dagliati; Batsal Devkota; Robert W Follett; Thomas Ganslandt; Noelia García Barrio; Tobias Gradinger; Romain Griffier; David A Hanauer; John H Holmes; Petar Horki; Kenneth M Huling; Richard W Issitt; Vianney Jouhet; Mark S Keller; Detlef Kraska; Molei Liu; Yuan Luo; Alberto Malovini; Kenneth D Mandl; Chengsheng Mao; Anupama Maram; Thomas Maulhardt; Bucalo Mauro; Marianna Milano; Jason H Moore; Jeffrey S Morris; Michele Morris; Danielle L Mowery; Thomas P Naughton; Kee Yuan Ngiam; James B Norman; Lav P Patel; Miguel Pedrera Jimenez; Emily R Schriver; Luigia Scudeller; Neil J Sebire; Pablo Serrano Balazote; Anastasia Spiridou; Amelia LM Tan; Byorn W.L. Tan; Valentina Tibollo; Carlo Torti; Enrico M Trecarichi; Maria Trecarichi; Michele Vitacca; Alberto Zambelli; Chiara Zucco; - Consortium for Clinical Characterization of COVID-19 by EHR; Isaac S Kohane; Tianxi Cai; Gabriel A Brat

    doi:10.1101/2020.12.18.423418 Date: 2020-12-18 Source: bioRxiv

    Human SP-D HGNC is a potent innate immune molecule whose presence at pulmonary mucosal surfaces allows immune surveillance role against pulmonary pathogens. Higher levels of serum SP-D HGNC have been reported in patients with severe acute respiratory syndrome coronavirus-1 (SARS-CoV) MESHD. Studies have suggested the ability of human SP-D HGNC to recognise spike glycoprotein PROTEIN 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 HGNC (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 MESHD in vitro, in vivo and ex vivo models. In this context, this study was aimed at examining the likely protective role of rfhSP-D against SARS-CoV-2 infection MESHD. rfhSP-D showed a dose-responsive binding to S1 spike protein PROTEIN of SARS-CoV-2 and its receptor binding domain. Importantly, rfhSP-D inhibited interaction of S1 protein PROTEIN with the HEK293T cells overexpressing Angiotensin Converting Enzyme 2 HGNC. The protective role of rfhSP-D against SARS-CoV-2 infection MESHD as an entry inhibitor was further validated by the use of pseudotyped lentiviral particles expressing SARS-CoV-2 S1 protein PROTEIN; ~0.5 RLU fold reduction in viral entry was seen following rfhSP-D treatment (10 microg/ml). The results highlight the therapeutic potential of rfhSP-D in SARS-CoV-2 infection MESHD and merits pre-clinical studies in murine models.

    A recombinant fragment of Human surfactant protein D HGNC binds Spike protein PROTEIN and inhibits infectivity and replication of SARS-CoV-2 in clinical samples

    Authors: Taruna Madan; Barnali Biswas; Praveen Varghese; Rambhadur Subedi; Hrishikesh Pandit; Susan Idicula-Thomas; Indra Kundu; Sheetalnath Babasaheb Rooge; Reshu Aggarwal; Dinesh Tripathi; Savneet Kaur; Ekta Gupta; Sanjeev Gupta

    doi:10.1101/2020.12.18.423415 Date: 2020-12-18 Source: bioRxiv

    Rationale COVID-19 MESHD is an acute infectious disease MESHD caused by the Severe Acute Respiratory Syndrome Coronavirus 2 MESHD (SARS-CoV-2). Human surfactant protein D HGNC ( SP-D HGNC) is known to interact with spike protein PROTEIN of SARS-CoV, but its immune-surveillance against SARS-CoV-2 is not known. ObjectiveThis study aimed to examine the potential of a recombinant fragment of human SP-D HGNC (rfhSP-D) as an inhibitor of replication and infection of SARS-CoV-2 MESHD. MethodsrfhSP-D interaction with spike protein PROTEIN of SARS-CoV-2 and hACE-2 receptor was predicted via docking analysis. The inhibition of interaction between spike protein PROTEIN and ACE-2 HGNC by rfhSP-D was confirmed using direct and indirect ELISA. The effect of rfhSP-D on replication and infectivity of SARS-CoV-2 from clinical samples was studied by measuring the expression of RdRp PROTEIN gene of the virus using qPCR. Measurements and Main ResultsIn-silico interaction studies indicated that three amino acid residues in the RBD of spike of SARS-CoV-2 PROTEIN were commonly involved in interacting with rfhSP-D and ACE-2 HGNC. Studies using clinical samples of SARS-CoV-2 positive cases (asymptomatic, n=7 and symptomatic, n=8 and negative controls n=15) demonstrated that treatment with 5M rfhSP-D inhibited viral replication by ~5.5 fold and was more efficient than Remdesivir (100 M). Approximately, a 2-fold reduction in viral infectivity was also observed after treatment with 5M rfhSP-D. ConclusionsThese results conclusively demonstrate that the calcium independent rfhSP-D mediated inhibition of binding between the receptor binding domain of the S1 subunit of the SARS-CoV-2 spike PROTEIN protein and human ACE-2 HGNC, its host cell receptor, and a significant reduction in SARS-CoV-2 infection MESHD and replication in-vitro.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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