Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinM (17)

ProteinE (17)

ProteinS (12)

ProteinN (11)

ORF3a (3)


SARS-CoV-2 Proteins
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    Vaccine Design, Adaptation, and Cloning Design for Multiple Epitope-Based Vaccine Derived From SARS-CoV-2 Surface Glycoprotein (S PROTEIN), Membrane Protein (M PROTEIN) and Envelope Protein (E PROTEIN): In silico approach

    Authors: Peter T. Habib

    doi:10.21203/ Date: 2021-02-14 Source: ResearchSquare

    The SARS Coronavirus-2 (SARS-CoV-2) pandemic has become a global epidemic that has increased the scientific community's concern about developing and finding a counteraction against this lethal virus. So far, hundreds of thousands of people have been infected by the pandemic due to contamination and spread. This research was therefore carried out to develop potential epitope-based vaccines against the SARS-CoV-2 virus using reverse vaccinology and immunoinformatics approaches. Three potential vaccine constructs were designed after intensive computational experimentation, and one vaccine model was chosen as the best vaccine based on a molecular docking analysis that is intended to work efficiently against SARS-CoV-2. In order to verify biological stability and find an appropriate mass production technique for the chosen vaccine, molecular dynamics simulation, and silico codon adaptation studies were subsequently carried out. This study should help to maintain current research efforts to secure a definitive preventive measure against this contagious disease.

    Structure-function investigation of a new VUI-202012/01 SARS-CoV-2 variant

    Authors: Jasdeep Singh; Nasreen Z Ehtesham; Syed Asad Rahman; Yakob G. Tsegay; Daniel S. Abebe; Mesay G. Edo; Endalkachew H. Maru; Wuletaw C. Zewde; Lydia K. Naylor; Dejen F. Semane; Menayit T. Deresse; Bereket B. Tezera; Lovisa Skoglund; Jamil Yousef; Elisa Pin; Wanda Christ; Mikaela Olausson; My Hedhammar; Hanna Tegel; Sara Mangsbo; Mia Phillipson; Anna Manberg; Sophia Hober; Peter Nilsson; Charlotte Thalin; Samuel Bates; Chevaun Morrison-Smith; Benjamin Nicholson; Edmond Wong; Leena El-Mufti; Michael Kann; Anna Bolling; Brooke Fortin; Hayden Ventresca; Wen Zhou; Santiago Pardo; Megan Kwock; Aditi Hazra; Leo Cheng; Rushdy Ahmad; James A. Toombs; Rebecca Larson; Haley Pleskow; Nell Meosky Luo; Christina Samaha; Unnati M. Pandya; Pushpamali De Silva; Sally Zhou; Zakary Ganhadeiro; Sara Yohannes; Rakiesha Gay; Jacqueline Slavik; Shibani S. Mukerji; Petr Jarolim; David R. Walt; Becky C. Carlyle; Lauren L. Ritterhouse; Sara Suliman

    doi:10.1101/2021.01.01.425028 Date: 2021-01-04 Source: bioRxiv

    The SARS-CoV-2 (Severe Acute Respiratory Syndrome-Coronavirus MESHD) has accumulated multiple mutations during its global circulation. Recently, a new strain of SARS-CoV-2 (VUI 202012/01) had been identified leading to sudden spike in COVID-19 MESHD cases in South-East England. The strain has accumulated 23 mutations which have been linked to its immune evasion and higher transmission capabilities. Here, we have highlighted structural-function impact of crucial mutations occurring in spike (S), ORF8 PROTEIN and nucleocapsid (N) protein PROTEIN of SARS-CoV-2. Some of these mutations might confer higher fitness to SARS-CoV-2 MESHD. SummarySince initial outbreak of COVID-19 MESHD in Wuhan city of central China, its causative agent; SARS-CoV-2 virus has claimed more than 1.7 million lives out of 77 million populations and still counting. As a result of global research efforts involving public-private-partnerships, more than 0.2 million complete genome sequences have been made available through Global Initiative on Sharing All Influenza Data (GISAID). Similar to previously characterized coronaviruses (CoVs), the positive-sense single-stranded RNA SARS-CoV-2 genome codes for ORF1ab PROTEIN non-structural proteins (nsp(s)) followed by ten or more structural/nsps [1, 2]. The structural proteins include crucial spike (S), nucleocapsid (N PROTEIN), membrane (M), and envelope (E) proteins PROTEIN. The S protein PROTEIN mediates initial contacts with human hosts while the E and M proteins PROTEIN function in viral assembly and budding. In recent reports on evolution of SARS-CoV-2, three lineage defining non-synonymous mutations; namely D614G in S protein PROTEIN (Clade G), G251V in ORF3a PROTEIN (Clade V) and L84S in ORF 8 (Clade S) were observed [2-4]. The latest pioneering works by Plante et al and Hou et al have shown that compared to ancestral strain, the ubiquitous D614G variant (clade G) of SARS-CoV-2 exhibits efficient replication in upper respiratory tract epithelial cells and transmission, thereby conferring higher fitness MESHD [5, 6]. As per latest WHO reports on COVID-19 MESHD, a new strain referred as SARS-CoV-2 VUI 202012/01 (Variant Under Investigation, year 2020, month 12, variant 01) had been identified as a part of virological and epidemiological analysis, due to sudden rise MESHD in COVID-19 MESHD detected cases in South-East England [7]. Preliminary reports from UK suggested higher transmissibility (increase by 40-70%) of this strain, escalating Ro (basic reproduction number) of virus to 1.5-1.7 [7, 8]. This apparent fast spreading variant inculcates 23 mutations; 13 non-synonymous, 6 synonymous and 4 amino acid deletions [7]. In the current scenario, where immunization programs have already commenced in nations highly affected by COVID-19 MESHD, advent of this new strain variant has raised concerns worldwide on its possible role in disease severity and antibody responses. The mutations also could also have significant impact on diagnostic assays owing to S gene target failures.

    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/ 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.

    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:

    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.

    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.

    Phylogenetic analysis of variable and conserved genomic regions in severe acute respiratory syndrome coronavirus 2 ( COVID-19 MESHD)

    Authors: Abeer F. El Nahas; Nasema M. Elkatatny; Haitham G. Abo-Al-Ela

    doi:10.21203/ Date: 2020-10-05 Source: ResearchSquare

    SARS-CoV-2 has rapidly spread around the world. Several mutations have been detected in its genome, but they do not seem to affect the abilities of the virus to spread or infect MESHD. We aimed to explore the conserved genomic regions in coronavirus that could contain the key strengths of the virus. SARS-CoV-2 sequence data were retrieved from Genbank from the period of December 2019 to March 2020. Phylogenetic analyses were conducted for 207 sequences using MEGAX compared with the reference sequence (MN908947.3- CHN-Wuhan Dec-2019). The analysis included seven important genomic regions, the ORF1ab PROTEIN gene (21,290 bp), S gene (3,822 bp), Orf3a PROTEIN gene (827 bp), E gene PROTEIN (227 bp), M gene (669 bp), and N gene PROTEIN (1,259 bp), which play critical roles in virus invasion and replication. Furthermore, the variant nucleotides and amino acids were detected by MEGAX and BLAST. Through the phylogenetic analysis and amino acid substitution, the ORF1ab PROTEIN gene showed 11 conserved regions and also several variable sites. The E and M genes were mainly conserved, and all sequences were included in one clade, with one or two amino acid variants. Orf3a PROTEIN and the N gene PROTEIN have four conserved sites distributed along the genes. The S gene has 12 mutations and four main large conserved regionsWe conclude that the favored occurrence of mutations at the ORFab and Orf3a PROTEIN genes during the SARS-CoV epidemic is an important mechanism for virus pathogenesis. The E and M proteins PROTEIN have an almost conserved structure, whereas the S and N genes PROTEIN have many conserved regions, which could serve as possible targets for vaccine design for SARS-CoV MESHD.

    Engineering Novel Epitope-Based Subunit Vaccine against SARS-CoV-2 by Exploring the Immunoinformatics Approach

    Authors: Bishajit Sarkar; Md. Asad Ullah; Yusha Araf; Mohammad Shahedur Rahman

    id:10.20944/preprints202009.0631.v1 Date: 2020-09-26 Source:

    As the number of infections and deaths MESHD caused by the recent COVID-19 MESHD COVID-19 MESHD pandemic is increasing dramatically day-by-day, scientists are rushing towards developing possible counter-measures to fight the deadly virus, SARS-CoV-2. Although many efforts have already been put forward for designing and developing potential vaccines, however, most of them are proved to possess negative consequences. Therefore, in this study, the methods of immunoinformatics were exploited to design novel epitope-based subunit vaccine against the SARS-CoV-2, targeting four essential proteins of the virus i.e., spike glycoprotein PROTEIN, nucleocapsid phosphoprotein, membrane glycoprotein PROTEIN, and envelope protein PROTEIN. The highly antigenic, non-allergenic, non-toxic, non-human homolog and 100% conserved (across other isolates from different regions of the world) epitopes were used for constructing the vaccine. In total, fourteen CTL epitopes and eighteen HTL epitopes were used to construct the vaccine. Thereafter, several in silico validations i.e., the molecular docking, molecular dynamics simulation (including the RMSF and RMSD studies), and immune simulation studies were also performed which predicted that the designed vaccine should be quite safe, effective, and stable within the biological environment. Finally, in silico cloning and codon adaptation studies were also conducted to design an effective mass production strategy of the vaccine. However, more in vivo and in vitro studies are required on the predicted vaccine to finally validate its safety and efficacy.

    Mutational Analysis of SARS-CoV-2 Genome in African Population

    Authors: Olabode E. Omotoso; Ayoade Desmond Babalola; Amira Matareek; Lele Zhao; Virginia Ledda; Lucie Abeler- Dorner; Michelle Kendall; Anel Nurtay; Hao-Yuan Cheng; Ta-Chou Ng; Hsien-Ho Lin; Rob Hinch; Joanna Masel; A. Marm Kilpatrick; Christophe Fraser; Raquel Gonzalez Seoane; Clara Martinez Diago; Esther Canedo Carballeira; Macarena Alferez Alvarez Mallo; Cristina Casanova Pedraz; Onofre Alomar Mateu; Cristina Lesmes Heredia; Juan Carlos Wizner de Alva; Ruth Bernardo Vega; Montserrat Macia Badia; Cristina Alvarez Colomo; Antonio Sanchez Munoz; Laia Pratcorona Alicart; Ruben Alonso Saiz; Monica Lopez Rodriguez; Maria Carmen Barbancho Lopez; Marta Meca Casbas; Oscar Vaquerizo Ruiz; Eva Moran Antolin; Maria Jose Nunez Valera; Camino Fernandez Fernandez; Albert Tubau Navarra; Alejandra M Cano Garcia; Carmen Baena Luque; Susana Soldevilla Perez; Irene Gastaca Abasolo; Jose Adanez Garcia; Maria Teulon Gonzalez; Alberto Puertas Prieto; Rosa Ostos; Maria del Pilar Guadix Martin; Monica Catalina Coello; Maria Luisa De la Cruz Conti; Africa Cano Aguilar; Jose A Sainz Bueno

    doi:10.1101/2020.09.07.286088 Date: 2020-09-07 Source: bioRxiv

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a highly infectious and pathogenic virus has claimed lot of lives globally since its outbreak in December 2019 posing dire threat on public health, global economy, social and human interaction. At moderate rate, mutations in the SARS-CoV-2 genome are evolving which might have contributed to viral genome variability, transmission, replication efficiency and virulence in different regions of the world. The present study elucidated the mutational landscape in SARS-CoV-2 genome among the African population, which may have contributed to the virulence, pathogenicity and transmission observed in the region. Multiple sequence alignment of the SARS-CoV-2 genome (356 viral protein sequences) was performed using ClustalX version 2.1 and phylogenetic tree was built using Molecular Evolutionary Genetics Analysis (MEGA) X software. ORF1ab PROTEIN polyprotein, spike glycoprotein PROTEIN, ORF3 HGNC, ORF8 PROTEIN and nucleocapsid phosphoprotein were observed as mutational hotspots in the African population and may be of keen interest in the adaptability of SARS-CoV-2 to the human host. While, there is conservation in the envelope protein PROTEIN, membrane glycoprotein PROTEIN, ORF6 PROTEIN, ORF7a PROTEIN, ORF7b PROTEIN and ORF10 PROTEIN. The accumulation of moderate mutations (though slowly) in the SARS-CoV-2 genome as revealed in our study, could be a promising strategy to develop drugs or vaccines with respect to the viral conserved domains and host cellular proteins and/or receptors involved in viral invasion and replication to avoid a new viral wave due to drug resistance and vaccine evasion.

    The SARS-CoV-2 Envelope and Membrane proteins modulate maturation and retention of the Spike protein PROTEIN, allowing optimal formation of VLPs in presence of Nucleoprotein PROTEIN

    Authors: Bertrand Boson; Vincent Legros; Bingjie Zhou; Cyrille Mathieu; François-Loïc Cosset; Dimitri Lavillette; Solene Denolly; Xia Cai; Zhiping Sun; Wendong Han; Rong Ye; Hongjun Chen; Qiang Ding; Qiliang Cai; Di Qu; Youhua Xie; Zhenghong Yuan; Rong Zhang; Arthur G Calise; Bradley L Pulver; Dominic Ruocco; Greggory E Mojares; Michael P Eagan; Kristy L Ziontz; Paul Mastrokyriakos; Stuart L Goldberg; Felecia Cerrato; Maha Farhat; Damien Slater; Jason B Harris; John Branda; David Hooper; Jessie M Gaeta; Travis P. Baggett; James O'Connell; Andreas Gnirke; Tami D Lieberman; Anthony Philippakis; Meagan Burns; Catherine Brown; Jeremy Luban; Edward T Ryan; Sarah E Turbett; Regina C LaRocque; William P. Hanage; Glen Gallagher; Lawrence C Madoff; Sandra Smole; Virginia M. Pierce; Eric S Rosenberg; Pardis Sabeti; Daniel J Park; Bronwyn L MacInnis

    doi:10.1101/2020.08.24.260901 Date: 2020-08-24 Source: bioRxiv

    The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a {beta}-coronavirus, is the causative agent of the COVID-19 MESHD COVID-19 MESHD pandemic. Like for other coronaviruses, its particles are composed of four structural proteins, namely Spike S, Envelope E, Membrane M and Nucleoprotein N PROTEIN proteins. The involvement of each of these proteins and their interplays during the assembly process of this new virus are poorly-defined and are likely {beta}-coronavirus-type different. Therefore, we sought to investigate how SARS-CoV-2 behaves for its assembly by expression assays of S, in combination with E, M and/or N. By combining biochemical and imaging assays, we showed that E and M regulate intracellular trafficking of S and hence its furin-mediated processing. Indeed, our imaging data revealed that S remains at ERGIC or Golgi compartments upon expression of E or M, like for SARS-CoV-2 infected MESHD cells. By studying a mutant of S, we showed that its cytoplasmic tail, and more specifically, its C-terminal retrieval motif, is required for the M-mediated retention in the ERGIC, whereas E induces S retention by modulating the cell secretory pathway. We also highlighted that E and M induce a specific maturation of S N-glycosylation MESHD, which is observed on particles and lysates from infected cells independently of its mechanisms of intracellular retention. Finally, we showed that both M, E and N are required for optimal production of virus-like-proteins. Altogether, our results indicated that E and M proteins PROTEIN influence the properties of S proteins PROTEIN to promote assembly of viral particles. Our results therefore highlight both similarities and dissimilarities in these events, as compared to other {beta}-coronaviruses. Author SummaryThe severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the COVID-19 pandemic MESHD. Its viral particles are composed of four structural proteins, namely Spike S, Envelope E, Membrane M and Nucleoprotein N PROTEIN proteins, though their involvement in the virion assembly remain unknown for this particular coronavirus. Here we showed that presence of E and M influence the localization and maturation of S protein PROTEIN, in term of cleavage and N-glycosylation maturation. Indeed, E protein PROTEIN is able to slow down the cell secretory pathway whereas M-induced retention of S requires the retrieval motif in S C-terminus. We also highlighted that E and M might regulate the N glycosylation maturation of S independently of its intracellular retention mechanism. Finally, we showed that the four structural proteins are required for optimal formation of virus-like particles, highlighting the involvement of N, E and M in assembly of infectious particles. Altogether, our results highlight both similarities and dissimilarities in these events, as compared to other {beta}-coronaviruses.

    Molecular features similarities between SARS-CoV-2, SARS, MERS and key human genes could favour the viral infections and trigger collateral effects

    Authors: Lucas Maldonado Sr.; Laura Kamenetzky

    doi:10.1101/2020.06.23.167072 Date: 2020-06-25 Source: bioRxiv

    In December 2019 rising pneumonia MESHD cases caused by a novel {beta}-coronavirus (SARS-CoV-2) occurred in Wuhan, China, which has rapidly spread worldwide causing thousands of deaths. The WHO declared the SARS-CoV-2 outbreak as a public health emergency of international concern therefore several scientists are dedicated to the study of the new virus. Since human viruses have codon usage biases that match highly expressed proteins in the tissues they infect MESHD and depend on host cell machinery for replication and co-evolution, we selected the genes that are highly expressed in the tissue of human lungs to perform computational studies that permit to compare their molecular features with SARS, SARS-CoV-2 and MERS genes. In our studies, we analysed 91 molecular features for 339 viral genes and 463 human genes that consisted of 677873 codon positions. Hereby, we found that A/T bias in viral genes could propitiate the viral infection MESHD favoured by a host dependant specialization using the host cell machinery of only some genes. The envelope protein E PROTEIN, the membrane glycoprotein M PROTEIN and ORF7 could have been further benefited by a high rate of A/T in the third codon position. Thereby, the mistranslation or de-regulation of protein synthesis could produce collateral effects, as a consequence of viral occupancy of the host translation machinery due tomolecular similarities with viral genes. Furthermore, we provided a list of candidate human genes whose molecular features match those of SARS-CoV-2, SARSand MERS genes, which should be considered to be incorporated into genetic population studies to evaluate thesusceptibility to respiratory viral infections MESHD caused by these viruses. The results presented here, settle the basis for further research in the field of human genetics associated with the new viral infection, COVID-19 MESHD, caused by SARS-CoV-2 and for the development of antiviral preventive methods.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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