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MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinE (144)

ProteinS (39)

ProteinN (33)

ComplexRdRp (17)

ProteinM (17)


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SARS-CoV-2 Proteins
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    Gene Expression Meta-Analysis Identifies Molecular Changes Associated with SARS-CoV Infection in Lungs

    Authors: Amber Park; Laura Harris; Tanushka Doctor; Neda Nasheri; Hua Wang; Xuemei Feng; Gennadiy Zelinskyy; Mirko Trilling; Kathrin Sutter; Mengji Lu; Baoju Wang; Dongliang Yang; Xin Zheng; Jia Liu; Davey Smith; Daniela Weiskopf; Alessandro Sette; Shane Crotty; Jian Jin; Xian Chen; Andrew Pekosz; Sabra Klein; Irina Burd

    doi:10.1101/2020.11.14.382697 Date: 2020-11-16 Source: bioRxiv

    Background: Severe Acute Respiratory Syndrome MESHD (SARS) corona virus ( SARS-CoV) infections MESHD are a serious public health threat because of their pandemic-causing potential. This work uses mRNA expression data to predict genes associated with SARS-CoV infection MESHD through an innovative meta-analysis examining gene signatures (i. e., gene PROTEIN lists ranked by differential gene expression between SARS and mock infection MESHD). Methods: This work defines 29 gene signatures representing SARS infection MESHD across seven strains with established mutations that vary virulence (infectious clone SARS (icSARS), Urbani, MA15, {Delta} ORF6 PROTEIN, BAT-SRBD, {Delta} NSP16 PROTEIN, and ExoNI) and host (human lung cultures and/or mouse lung samples) and examines them through Gene Set Enrichment Analysis (GSEA). To do this, first positive and negative icSARS gene panels were defined from GSEA-identified leading-edge genes between 500 genes from positive or negative tails of the GSE47960-derived icSARSvsmock signature and the GSE47961-derived icSARSvsmock signature, both from human cultures. GSEA then was used to assess enrichment and identify leading-edge icSARS panel genes in the other 27 signatures. Genes associated with SARS-CoV infection MESHD are predicted by examining membership in GSEA-identified leading-edges across signatures. Results: Significant enrichment (GSEA p<0.001) was observed between GSE47960-derived and GSE47961-derived signatures, and those leading-edges defined the positive (233 genes) and negative (114 genes) icSARS panels. Non-random (null distribution p<0.001) significant enrichment (p<0.001) was observed between icSARS panels and all verification icSARSvsmock signatures derived from human cultures, from which 51 over- and 22 under-expressed genes were shared across leading-edges with 10 over-expressed genes already being associated with icSARS infection MESHD. For the icSARSvsmock mouse signature, significant, non-random enrichment (both p<0.001) held for only the positive icSARS panel, from which nine genes were shared with icSARS infection MESHD in human cultures. Considering other SARS strains, significant (p<0.01), non-random (p<0.002) enrichment was observed across signatures derived from other SARS strains for the positive icSARS panel. Five positive icSARS panel genes, CXCL10, OAS3, OASL, IFIT3, and XAF1, were found in mice and human signatures. Conclusion: The GSEA-based meta-analysis approach used here identified genes with and without reported associations with SARS-CoV infections MESHD, highlighting this approachs predictability and usefulness in identifying genes that have potential as therapeutic targets to preclude or overcome SARS infections MESHD.

    Sequence and Structural Analysis of COVID-19 MESHD E and M Protein PROTEIN With MERS Virus E and M Protein PROTEIN – A Comparative Study

    Authors: Ebtisam A. Aldaais; Subha Yegnaswamy; Fatimah Albahrani; Fatima Alsowaiket; Sarah Alramadan

    doi:10.21203/rs.3.rs-108454/v1 Date: 2020-11-14 Source: ResearchSquare

    The outbreak of SARS in 2003, MERS in 2012, and now COVID-19 MESHD in 2019 have demonstrated that Coronaviruses are capable of causing primary lethal infections in humans, and the pandemic is now a global concern. The COVID-19 MESHD belongs to the beta coronavirus family encoding 29 proteins, of which 4 are structural, the Spike, Membrane, Envelope, and Nucleocapsid proteins PROTEIN. Here we have analyzed and compared the Membrane (M) and Envelope (E) proteins PROTEIN of COVID-19 MESHD and MERS with SARS and Bat viruses. The sequence analysis of conserved regions of both E and M protein PROTEIN revealed that many regions of COVID-19 MESHD are similar to Bat and SARS viruses while the MERS virus showed variations. The essential binding motifs found in SARS-CoV MESHD appeared in COVID-19 MESHD. Besides, the M protein PROTEIN of COVID- 19 showed a distinct serine phosphorylation site in the C-terminal domain, which looked like a catalytic triad seen in serine proteases. A Dileucine motif occurred many times in the sequence of the M protein PROTEIN of all the four viruses compared. Concerning the structural part, the COVID-19 MESHD E protein PROTEIN showed more similarity to Bat while MERS shared similarity with the SARS virus. The M protein PROTEIN of both COVID-19 MESHD and MERS displayed variations in the structure. The interaction between M and E protein PROTEIN was also studied to know the additional binding regions. Our study highlights the critical motifs and structural regions to be considered for further research to design better inhibitors for the infection caused by these viruses.

    SARS-CoV-2 antibody signatures for predicting the outcome of COVID-19 MESHD

    Authors: Qing Lei; Caizheng Yu; Yang Li; Hongyan Hou; Zhaowei Xu; Meian He; Ziyong Sun; Feng Wang; Sheng-ce Tao; Xionglin Fan

    doi:10.1101/2020.11.10.20228890 Date: 2020-11-13 Source: medRxiv

    The COIVD-19 global pandemic is far from ending. There is an urgent need to identify applicable biomarkers for predicting the outcome of COVID-19 MESHD. Growing evidences have revealed that SARS-CoV-2 specific antibodies remain elevated with disease progression and severity in COIVD-19 patients. We assumed that antibodies may serve as biomarkers for predicting disease outcome. By taking advantage of a newly developed SARS-CoV-2 proteome microarray, we surveyed IgM/ IgG responses against 20 SARS-CoV-2 proteins in 1,034 hospitalized COVID-19 MESHD patients on admission, who were followed till 66 days. The microarray results were correlated with clinical information, laboratory test results and patient outcomes. Cox proportional hazards model was used to explore the association between SARS-CoV-2 specific antibodies and COVID-19 MESHD mortality. We found that high level of IgM against ORF7b PROTEIN at the time of hospitalization is an independent predictor of patient survival (p trend = 0.002), while levels of IgG responses to 6 non-structural proteins PROTEIN and 1 accessory protein, i. e PROTEIN., NSP4 HGNC NSP4 PROTEIN, NSP7 PROTEIN, NSP9 PROTEIN, NSP10 PROTEIN, RdRp PROTEIN ( NSP12 PROTEIN), NSP14 PROTEIN, and ORF3b PROTEIN, possess significant predictive power for patient death MESHD, even after further adjustments for demographics, comorbidities, and common laboratory markers for disease severity (all with p trend < 0.05). Spline regression analysis indicated that the correlation between ORF7b PROTEIN IgM, NSP9 PROTEIN IgG, and NSP10 PROTEIN IgG and risk of COVID-19 MESHD mortality is linear (p = 0.0013, 0.0073 and 0.0003, respectively). Their AUCs for predictions, determined by computational cross-validations (validation1), were 0.74 (cut-off = 7.59), 0.66 (cut-off = 9.13), and 0.68 (cut-off = 6.29), respectively. Further validations were conducted in the second and third serial samples of these cases (validation2A, n = 633, validation2B, n = 382), with high accuracy of prediction for outcome. These findings have important implications for improving clinical management, and especially for developing medical interventions and vaccines.

    In silico analyses on the comparative sensing of SARS-CoV-2 mRNA by intracellular TLRs of human

    Authors: Abhigyan Choudhury; Nabarun Chandra Das; Ritwik Patra; Manojit Bhattacharya; Suprabhat Mukherjee; Kianna M. Nguyen; Ming H. Ho; Jung-Eun Shin; Jared Feldman; Blake M. Hauser; Timothy M. Caradonna; Laura M. Wingler; Aaron G. Schmidt; Debora S. Marks; Jonathan Abraham; Andrew C. Kruse; Chang C. Liu

    doi:10.1101/2020.11.11.377713 Date: 2020-11-11 Source: bioRxiv

    The worldwide outbreak of COVID-19 MESHD COVID-19 MESHD pandemic caused by SARS-CoV-2 leads to loss of mankind and global economic stability. The continuous spreading of the disease and its pathogenesis takes millions of lives of peoples and the unavailability of appropriate therapeutic strategy makes it much more severe. Toll-like receptors (TLRs) are the crucial mediators and regulators of host immunity. The role of several TLRs in immunomodulation of host by SARS-CoV-2 is recently demonstrated. However, the functionality of human intracellular TLRs including TLR3 HGNC,7,8 and 9 is still being untested for sensing of viral RNA. This study is hoped to rationalize the comparative binding and sensing of SARS-CoV-2 mRNA towards the intracellular TLRs, considering the solvent-based force-fields operational in the cytosolic aqueous microenvironment that predominantly drive these reactions. Our in-silico study on the binding of all mRNAs with the intracellular TLRs shown that the mRNA of NSP10 PROTEIN, S2, and E proteins PROTEIN of SARS-CoV-2 are potent enough to bind with TLR3 HGNC, TLR9 HGNC, and TLR7 HGNC and trigger downstream cascade reactions, and may be used as an option for validation of therapeutic option and immunomodulation against COVID-19 MESHD.

    Exosome-Mediated mRNA Delivery For SARS-CoV-2 Vaccination

    Authors: Shang-Jui Tsai; Chenxu Guo; Nadia A Atai; Stephen J Gould; Emma S Child; Rhodri M L Morgan; Alan Armstrong; David J Mann; Sheng Cui; Paulo Souza-Fonseca Guimaraes; Lucia Noronha; Timothy McCulloch; Gustavo Rodrigues Rossi; Caroline Cooper; Benjamin Tang; Kirsty Short; Melissa J Davis; Fernando Souza-Fonseca Guimaraes; Gabrielle T Belz; Ken O'Byrne

    doi:10.1101/2020.11.06.371419 Date: 2020-11-06 Source: bioRxiv

    Background: In less than a year from its zoonotic entry into the human population, SARS-CoV-2 has infected more than 45 million people, caused 1.2 million deaths, and induced widespread societal disruption MESHD. Leading SARS-CoV-2 vaccine candidates immunize with the viral spike protein PROTEIN delivered on viral vectors, encoded by injected mRNAs, or as purified protein. Here we describe a different approach to SARS-CoV-2 vaccine development that uses exosomes to deliver mRNAs that encode antigens from multiple SARS-CoV-2 structural proteins. Approach: Exosomes were purified and loaded with mRNAs designed to express (i) an artificial fusion protein, LSNME, that contains portions of the viral spike, nucleocapsid, membrane, and envelope proteins PROTEIN, and (ii) a functional form of spike. The resulting combinatorial vaccine, LSNME/SW1, was injected into thirteen weeks-old, male C57BL/6J mice, followed by interrogation of humoral and cellular immune responses to the SARS-CoV-2 nucleocapsid and spike proteins PROTEIN, as well as hematological and histological analysis to interrogate animals for possible adverse effects. Results: Immunized mice developed CD4+, and CD8+ T-cell reactivities that respond to both the SARS-CoV-2 nucelocapsid protein and the SARS-CoV-2 spike PROTEIN protein. These responses were apparent nearly two months after the conclusion of vaccination, as expected for a durable response to vaccination. In addition, the spike-reactive CD4+ T-cells response was associated with elevated expression of interferon gamma, indicative of a Th1 response, and a lesser induction of interleukin 4, a Th2-associated cytokine. Vaccinated mice showed no sign of altered growth, injection-site hypersensitivity MESHD, change in white blood cell profiles, or alterations in organ morphology. Consistent with these results, we also detected moderate but sustained anti-nucleocapsid and anti-spike antibodies in the plasma of vaccinated animals. Conclusion: Taken together, these results validate the use of exosomes for delivering functional mRNAs into target cells in vitro and in vivo, and more specifically, establish that the LSNME/SW1 vaccine induced broad immunity to multiple SARS-CoV-2 proteins.

    Extracellular vesicle-based vaccine platform displaying native viral envelope proteins PROTEIN elicits a robust anti-SARS-CoV-2 response in mice.

    Authors: Katarzyna Polak; Noémie Greze; Maëlle Lachat; Delphine Merle; Steve Chiumento; Christelle Bertrand-Gaday; Bernadette Trentin; Robert Z. Mamoun; Gamze Tumentemur; Sevda Demir; Utku Seyis; Recai Kuzay; Muhammer Elek; Gurcan Ertop; Serap Arbak; Merve Acikel Elmas; Cansu Hemsinlioglu; Ozden Hatirnaz Ng; Sezer Akyoney; Ilayda Sahin; Cavit Kerem Kayhan; Fatma Tokat; Gurler Akpinar; Murat Kasap; Ayse Sesin Kocagoz; Ugur Ozbek; Dilek Telci; Fikrettin Sahin; Koray Yalcin; Siret Ratip; Umit Ince; Guldal Suyen; Ercument Ovali; Liam Fergusson; Marta Conti; Marius Rameil; Vanessa Nakonecnij; Jakob Vanhoefer; Leonard Schmiester; Muying Wang; Emily E Ackerman; Jason E Shoemaker; Jeremy Zucker; Kristie L Oxford; Jeremy Teuton; Ebru Kocakaya; Gokce Yagmur Summak; Kristina Hanspers; Martina Kutmon; Susan Coort; Lars Eijssen; Friederike Ehrhart; Rex D. A. B.; Denise Slenter; Marvin Martens; Robin Haw; Bijay Jassal; Lisa Matthews; Marija Orlic-Milacic; Andrea Senff-Ribeiro; Karen Rothfels; Veronica Shamovsky; Ralf Stephan; Cristoffer Sevilla; Thawfeek Mohamed Varusai; Jean-Marie Ravel; Vera Ortseifen; Silvia Marchesi; Piotr Gawron; Ewa Smula; Laurent Heirendt; Venkata Satagopam; Guanming Wu; Anders Riutta; Martin Golebiewski; Stuart Owen; Carole Goble; Xiaoming Hu; Rupert Overall; Dieter Maier; Angela Bauch; John A Bachman; Benjamin M Gyori; Carlos Vega; Valentin Groues; Miguel Vazquez; Pablo Porras; Luana Licata; Marta Iannuccelli; Francesca Sacco; Denes Turei; Augustin Luna; Ozgun Babur; Sylvain Soliman; Alberto Valdeolivas; Marina Esteban-Medina; Maria Pena-Chilet; Tomas Helikar; Bhanwar Lal Puniya; Anastasia Nesterova; Anton Yuryev; Anita de Waard; Dezso Modos; Agatha Treveil; Marton Laszlo Olbei; Bertrand De Meulder; Aurelien Naldi; Aurelien Dugourd; Laurence Calzone; Chris Sander; Emek Demir; Tamas Korcsmaros; Tom C Freeman; Franck Auge; Jacques S Beckmann; Jan Hasenauer; Olaf Wolkenhauer; Egon Willighagen; Alexander R Pico; Chris Evelo; Lincoln D Stein; Henning Hermjakob; Julio Saez-Rodriguez; Joaquin Dopazo; Alfonso Valencia; Hiroaki Kitano; Emmanuel Barillot; Charles Auffray; Rudi Balling; Reinhard Schneider; - the COVID-19 Disease Map Community

    doi:10.1101/2020.10.28.357137 Date: 2020-10-28 Source: bioRxiv

    Extracellular vesicles (EVs) emerge as essential mediators of intercellular communication. DNA vaccines encoding antigens presented on EVs efficiently induce T-cell responses and EV-based vaccines containing the Spike (S) proteins PROTEIN of Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV MESHD) are highly immunogenic in mice. Thus, EVs may serve as vaccine platforms against emerging diseases MESHD, going beyond traditional strategies, with the antigen displayed identically to the original protein embedded in the viral membrane and presented as such to the immune system. Compared to their viral and pseudotyped counterparts, EV-based vaccines overcome many safety issues including pre-existing immunity against these vectors. Here, we applied our technology in natural EV's engineering, to express the S proteins PROTEIN of SARS-CoV-2 embedded in the EVs, which mimic the virus with its fully native spikes. Immunizations with a two component CoVEVax vaccine, comprising DNA vector (DNAS-EV) primes, allowing in situ production of Spike harbouring EVs, and a boost using S-EVs produced in mammalian cells, trigger potent neutralizing and cellular responses in mice, in the absence of any adjuvants. CoVEVax would be the prototype of vaccines, where the sole exchange of the envelope proteins PROTEIN on EVs leads to the generation of new vaccine candidates against emerging viruses.

    The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter semiSWEET

    Authors: Sunil Thomas

    id:10.20944/preprints202004.0512.v6 Date: 2020-10-19 Source: Preprints.org

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the disease COVID-19 MESHD that has decimated the health and economy of our planet. The virus causes the disease not only in people but also in companion and wild animals. People with diabetes MESHD are at risk of the disease. As yet we do not know why the virus is highly successful in causing the pandemic within 3 months of its first report. The structural proteins of SARS include, membrane glycoprotein (M PROTEIN), envelope protein (E PROTEIN), nucleocapsid protein (N PROTEIN) and the spike protein (S PROTEIN). The structure and function of the most abundant structural protein of SARS-CoV-2, the membrane (M) glycoprotein PROTEIN is not fully understood. Using in silico analyses we determined the structure and potential function of the M protein PROTEIN. The M protein PROTEIN of SARS-CoV-2 is 98.6% similar to the M protein PROTEIN of bat SARS-CoV MESHD, maintains 98.2% homology with pangolin SARS-CoV MESHD, and has 90% homology with M protein PROTEIN of SARS-CoV MESHD; whereas, the similarity was only 38% with the M protein PROTEIN of MERS-CoV. In silico analyses showed that the M protein PROTEIN of SARS-CoV-2 has a triple helix bundle, form a single 3-transmembrane domain (TM), and are homologous to the prokaryotic sugar transport protein semiSWEET. SemiSWEETs are related to the PQ-loop family that function as cargo receptors in vesicle transport, mediates movement of basic amino acids across lysosomal membranes, and is also involved in phospholipase flippase function. The advantage and role of the M protein PROTEIN having a sugar transport-like structure is not clearly understood. The M protein PROTEIN of SARS-CoV-2 interacts with S, E and N protein PROTEIN. The S protein PROTEIN of the virus is glycosylated. It could be hypothesized that the sugar transporter-like structure of the M protein PROTEIN influences glycosylation of the S protein PROTEIN. Endocytosis is critical for the internalization and maturation of RNA viruses, including SARS-CoV-2. Sucrose is involved in endosome and lysosome maturation and may also induce autophagy, pathways that help in the entry of the virus. Overall, it could be hypothesized that the semiSWEET sugar transporter-like structure of the M protein PROTEIN may be involved in multiple functions that may aid in the rapid proliferation, replication and immune evasion of the SARS-CoV-2 virus. Biological experiments would validate the presence and function of the semiSWEET sugar transporter.

    Rapid and Low-cost Sampling for Detection of Airborne SARS-CoV-2 in Dehumidifier Condensate

    Authors: Parikshit Moitra; Maha Alafeef; Ketan Dighe; Priyanka Ray; James Chang; Sai Sathish Ramamurthy; Xudong Ge; Dipanjan Pan; Govind Rao

    doi:10.1101/2020.10.08.20208785 Date: 2020-10-13 Source: medRxiv

    Airborne spread of COVID-19 MESHD by infectious aerosol is all but certain. However, easily implemented approaches to assess the actual environmental threat are currently unavailable. We present a simple approach with the potential to rapidly provide information about the prevalence of SARS-CoV-2 in the atmosphere at any location. We used a portable dehumidifier as a readily available and affordable tool to collect airborne virus in the condensate. The dehumidifiers were deployed in selected locations of a hospital ward with patients reporting flu like symptoms which could possibly be due to COVID-19 MESHD over three separate periods of one week. Samples were analyzed frequently for both virus envelope protein PROTEIN and SARS-CoV-2 RNA. In several samples across separate deployments, condensate from dehumidifiers tested positive for the presence of SARS-CoV-2 antigens and confirmed using two independent assays. RNA was detected, but not attributable to SARS-CoV-2. Our results point to a facile pool testing method to sample air in any location in the world and assess the presence and concentration of the infectious agent in order to obtain quantitative risk assessment of exposure, designate zones as hot spots and minimize the need for individual testing which may often be time consuming, expensive and laborious.

    Codon pattern reveals SARS-CoV-2 to be a monomorphic strain that emerged through recombination of replicase and envelope alleles of bat and pangolin origin

    Authors: Kanika Bansal; Prabhu B Patil; Vyacheslav A. Dibrova; Yulia V. Dibrova; Volodymyr M. Vasylyk; Mykhailo Y. Novikov; Nataliia V. Shults; Sergiy G. Gychka; Scott Lee; Zhaohui Cui; Adebola Adebayo; Tiffiany Aholou; Minal Amin; Peter Aryee; Cindy Castaneda; Trudy Chambers; Amy Fleshman; Christin Goodman; Tony Holmes; Asha Ivey-Stephenson; Emiko Kamitani; Susan Katz; Jennifer Knapp; Maureen Kolasa; Maranda Lumsden; Erin Mayweather; Asfia Mohammed; Anne Moorman; Alpa Patel-Larson; Lara Perinet; Mark Pilgard; Deirdre Pratt; Shanica Railey; Jaina Shah; Dawn Tuckey; Emilio Dirlikov; Dale Rose; Julie Villanueva; Alicia Fry; Aron Hall; Hannah Kirking; Jacqueline Tate; Cherie Drenzek; Tatiana Lanzieri; Rebekah Stewart

    doi:10.1101/2020.10.12.335521 Date: 2020-10-12 Source: bioRxiv

    Viruses are dependent on the host tRNA pool, and an optimum codon usage pattern (CUP) is a driving force in its evolution. Systematic analysis of CUP of replicase ( rdrp PROTEIN), spike, envelope (E), membrane glycoprotein (M PROTEIN), and nucleocapsid (N PROTEIN) encoding genes of SARS-CoV-2 from reported diverse lineages to suggest one-time host jump of a SARS-CoV-2 isolate into the human host. In contrast to human isolates, a high degree of variation in CUP of these genes suggests that bats, pangolins, and dogs are natural reservoirs of diverse strains. At the same time, our analysis suggests that dogs are not a source of SARS-CoV-2. Interestingly, CUP of rdrp PROTEIN displays conservation with two bat SARS isolates RaTG13 and RmYN02. CUP of the SARS-CoV-2 E gene PROTEIN is also conserved with bat and pangolin isolates with variations for a few amino acids. This suggests role allele replacement in these two genes involving SARS strains of least two hosts. At the same time, a relatively conserved CUP pattern in replicase and envelope across hosts suggests them it to be an ideal target in antiviral development for SARS-CoV-2.

    In-House Development, Standardization, and Validation of a RT-qPCR Assay for the Detection of SARS-CoV-2 Virus in Ecuador.

    Authors: David De la Torre; Ronny Pibaque; Tatiana Veloz; Paúl Beltrán; Lucy Baldeón

    doi:10.21203/rs.3.rs-91429/v1 Date: 2020-10-12 Source: ResearchSquare

    The World Health Organization (WHO) reported about 30 million cases of Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection MESHD, and around 1 million deaths worldwide. Ecuador is the country with the highest mortality rate of confirmed cases in South America where both the poor ability to identify SARS-CoV-2 carriers and shortages in reagent supply have contributed the high infection rate observed. Hence, there is an urgent need to develop, standardize and validate an in-house protocol that cannot only reduces testing costs, but also increase the ability to screen widely the population. Primer-probe sets for the SARS-CoV-2 envelope protein E PROTEIN and the human ribonuclease P (RP) were validated for a duplex quantitative Reverse Transcription Polymerase Chain Reaction (RT-qPCR) for the Coronavirus Disease-19 MESHD ( COVID-19 MESHD) detection. Optimal E primers concentration was 400 nM and TaqMan probe 200 nM. The primer efficiency was set at 94.9% and R2 value at 0.99, which was comparable to commercial kits. The lower detection limit was found at 15 copies/ μL (50 copies/rx). In comparison to a Loop-mediated Isothermal Amplification (LAMP) commercial kit, there was a higher detection rate (30%) and results were highly reproducible (95%). We were able to develop a highly sensitive and low-cost duplex in-house RT-qPCR test for COVID-19 MESHD detection comparable to other commercially available kits.

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SARS-CoV-2 Proteins


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