Role of Genetic Variants and Gene Expression in the Susceptibility and Severity of COVID-19
2
조회
0
다운로드
3
인용
0
참고문헌
키워드
초록
Since its first report in December 2019, coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has rapidly emerged as a pandemic affecting nearly all countries worldwide. As the COVID-19 pandemic progresses, the need to identify genetic risk factors for susceptibility to this serious illness has emerged. Host genetic factors, along with other risk factors may help determine susceptibility to respiratory tract infections. It is hypothesized that the ACE2 gene, encoding angiotensin-converting enzyme 2 (ACE2), is a genetic risk factor for SARS-CoV-2 infection and is required by the virus to enter cells. Together with ACE2, transmembrane protease serine 2 (TMPRSS2) and dipeptidyl peptidase-4 (DPP4) also play an important role in disease severity. Evaluating the role of genetic variants in determining the direction of respiratory infections will help identify potential drug target candidates for further study in COVID-19 patients. We have summarized the latest reports demonstrating that ACE2 variants, their expression, and epigenetic factors may influence an individual’s susceptibility to SARS-CoV-2 infection and disease outcome.
Abstract
Since its first report in December 2019, coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has rapidly emerged as a pandemic affecting nearly all countries worldwide. As the COVID-19 pandemic progresses, the need to identify genetic risk factors for susceptibility to this serious illness has emerged. Host genetic factors, along with other risk factors may help determine susceptibility to respiratory tract infections. It is hypothesized that the ACE2 gene, encoding angiotensin-converting enzyme 2 (ACE2), is a genetic risk factor for SARS-CoV-2 infection and is required by the virus to enter cells. Together with ACE2, transmembrane protease serine 2 (TMPRSS2) and dipeptidyl peptidase-4 (DPP4) also play an important role in disease severity. Evaluating the role of genetic variants in determining the direction of respiratory infections will help identify potential drug target candidates for further study in COVID-19 patients. We have summarized the latest reports demonstrating that ACE2 variants, their expression, and epigenetic factors may influence an individual’s susceptibility to SARS-CoV-2 infection and disease outcome.
참고문헌 (73)
- Ki Ho Hong, "Guidelines for Laboratory Diagnosis of Coronavirus Disease 2019 (COVID-19) in Korea", Annals of Laboratory Medicine, 40(5), pp.351~360 (2020), 대한진단검사의학회[DOI]
- Mitra P, "COVID-19 pandemic in India: what lies ahead", Ind J Clin Biochem, 35, pp.257~259 (2020)
- Heungsup Sung, "COVID-19 Molecular Testing in Korea: Practical Essentials and Answers From Experts Based on Experiences of Emergency Use Authorization Assays", Annals of Laboratory Medicine, 40(6), pp.439~447 (2020), 대한진단검사의학회[DOI]
- Mitra P, "Association of comorbidities with coronavirus disease 2019: a review", Ann Natl Acad Med Sci (India), 56, pp.102~111 (2020)
- "Coronavirus disease (COVID-19) dashboard"[URL]
- Lingeswaran M, "Inflammation, immunity and immunogenetics in COVID-19: a narrative review", Indian J Clin Biochem, 35, pp.260~273 (2020)
- Lacoma A, "Impact of host genetics and biological response modifiers on respiratory tract infections", Front Immunol, 10, pp.1013~ (2019)
- Benetti E, "ACE2gene variants may underlie interindividual variability and susceptibility to COVID-19 in the Italian population", Eur J Hum Genet, pp.1~13 (2020)
- Chen YY, "Relationship between genetic variants of ACE2 gene and circulating levels of ACE2 and its metabolites", J Clin Pharm Ther, 43, pp.189~195 (2018)
- Patel SK, "Association of ACE2 genetic variants with blood pressure, left ventricular mass, and cardiac function in Caucasians with type 2 diabetes", Am J Hypertens, 25, pp.216~222 (2012)
- Zhang SF, "Epidemiology characteristics of human coronaviruses in patients with respiratory infection symptoms and phylogenetic analysis of HCoV-OC43 during 2010-2015 in Guangzhou", PLoS One, 13, pp.e0191789~ (2018)
- Hu B, "Bat origin of human coronaviruses", Virol J, 12, pp.221~ (2015)
- Pyrc K, "The novel human coronaviruses NL63 and HKU1", J Virol, 81, pp.3051~3057 (2007)
- Devaux CA, "ACE2 receptor polymorphism: susceptibility to SARS-CoV-2, hypertension, multi-organ failure, and COVID-19 disease outcome", J Microbiol Immunol Infect, 53, pp.425~435 (2020)
- Ye J, "Molecular pathology in the lungs of severe acute respiratory syndrome patients", Am J Pathol, 170, pp.538~545 (2007)
- To KF, "Tissue and cellular tropism of the coronavirus associated with severe acute respiratory syndrome: an in-situ hybridization study of fatal cases", J Pathol, 202, pp.157~163 (2004)
- Nicholls JM, "Lung pathology of fatal severe acute respiratory syndrome", Lancet, 361, pp.1773~1778 (2003)
- Hamming I, "Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis", J Pathol, 203, pp.631~637 (2004)
- Tipnis SR, "A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase", J Biol Chem, 275, pp.33238~33243 (2000)
- Patel VB, "Role of the ACE2", angiotensin 1–7 axis of the renin-angiotensin system in heart failure, 2016, pp.118, 1313~1326
- Vickers C, "Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase", J Biol Chem, 277, pp.14838~14843 (2002)
- Gheblawi M, "Angiotensin converting Enzyme 2: SARS-CoV-2 receptor and regulator of the renin-angiotensin system: celebrating the 20th anniversary of the discovery of ACE2", Circ Res, 126, pp.1456~1474 (2020)
- Yan R, "Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2", Science, 367, pp.1444~1448 (2020)
- Li W, "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus", Nature, 426, pp.450~454 (2003)
- Walls AC, "Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein", Cell, 181, pp.281~292.e6 (2020)
- Fu J, "Expressions and significances of the angiotensin-converting enzyme 2 gene, the receptor of SARS-CoV-2 for COVID-19", Mol Biol Rep, 47, pp.4383~4392 (2020)
- Chen Y, "Structure analysis of the receptor binding of 2019-nCoV", Biochem Biophys Res Commun, 525, pp.135~140 (2020)
- Zhou P, "A pneumonia outbreak associated with a new coronavirus of probable bat origin", Nature, 579, pp.270~273 (2020)
- Qiu Y, "Predicting the angiotensin converting enzyme 2 (ACE2) utilizing capability as the receptor of SARS-CoV-2", Microbes Infect, 22, pp.221~225 (2020)
- Li W, "Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2", EMBO J, 24, pp.1634~1643 (2005)
- Wan Y, "Receptor recognition by the novel coronavirus from Wuhan: an analysis based on decade-long structural studies of SARS coronavirus", J Virol, 94, pp.e00127-20~ (2020)
- Rice GI, "Circulating activities of angiotensin-converting enzyme, its homolog, angiotensin-converting enzyme 2, and neprilysin in a family study", Hypertension, 48, pp.914~920 (2006)
- Ciaglia E, "COVID-19 infection and circulating ACE2 levels: protective role in women and children", Front Pediatr, 8, pp.206~ (2020)
- Mushtaq Hussain, "Structural variations in human ACE2 may influence its binding with SARS‐CoV‐2 spike protein", Journal of Medical Virology, 92(9), pp.1580~1586 (2020), Wiley[DOI]
- Xia S, "Inhibition of SARSCoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion", Cell Res, 30, pp.343~355 (2020)
- Wang D, "Clinical characteristics of 138 hospitalized patients with 2019 novel coronavirus–infected pneumonia in Wuhan, China", JAMA, 323, pp.1061~1069 (2020)
- Guan WJ, "Clinical characteristics of coronavirus disease 2019 in China", N Engl J Med, 382, pp.1708~1720 (2020)
- Chen J, "Individual variation of the SARS-CoV-2 receptor ACE2 gene expression and regulation", Aging Cell, 19, pp.e13168~ (2020)
- Cao Y, "Comparative genetic analysis of the novel coronavirus (2019-nCoV", SARS-CoV-2) receptor ACE2 in different populations, 2020, pp.6, 11~
- Zhao Y, "Single-cell RNA expression profiling of ACE2, the receptor of SARS-CoV-2", Am J Respir Crit Care Med, 202, pp.756~759 (2020)
- Li M, "Expression of the SARS-CoV-2 cell recep-tor gene ACE2 in a wide variety of human tissues", Infect Dis Poverty, 9, pp.45~ (2020)
- Bénéteau-Burnat B, "Serum angiotensin-converting enzyme in healthy and sarcoidotic children: comparison with the reference interval for adults", Clin Chem, 36, pp.344~346 (1990)
- Day CW, "A new mouse-adapted strain of SARS-CoV as a lethal model for evaluating antiviral agents in vitro and in vivo", Virology, 395, pp.210~222 (2009)
- Ghadhanfar E, "The role of ACE2, angiotensin-(1–7) and Mas1 receptor axis in glucocorticoid-induced intrauterine growth restriction", Reprod Biol Endocrinol, 15, pp.97~ (2017)
- [URL]
- Lucas JM, "The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis", Cancer Discov, 4, pp.1310~1325 (2014)
- Hoffmann M, "SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2and is blocked by a clinically proven protease inhibitor", Cell, 181, pp.271~280.e8 (2020)
- Böttcher E, "Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium", J Virol, 80, pp.9896~9898 (2006)
- Shulla A, "A. transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry", J Virol, 85, pp.873~882 (2011)
- Watanabe R, "Entry from the cell surface of severe acute respiratory syndrome coronavirus with cleaved S protein as revealed by pseudotype virus bearing cleaved S protein", J Virol, 82, pp.11985~11991 (2008)
- Belouzard S, "Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites", Proc Natl Acad Sci, 106, pp.5871~5876 (2009)
- Matsuyama S, "Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2", J Virol, 84, pp.12658~12664 (2010)
- Kam YW, "Cleavage of the SARS coronavirus spike glycoprotein by airway proteases enhances virus entry into human bronchial epithelial cells in vitro", PLoS One, 4, pp.e7870~ (2009)
- Heurich A, "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein", J Virol, 88, pp.1293~1307 (2014)
- Asselta R, "ACE2 and TMPRSS2variants and expression as candidates to sex and country differences in COVID-19 severity in Italy", Aging (Albany NY), 12, pp.10087~10098 (2020)
- FitzGerald LM, "Association of TMPRSS2-ERG gene fusion with clinical characteristics and outcomes: results from a population-based study of prostate cancer", BMC Cancer, 8, pp.230~ (2008)
- Clinckemalie L, "Androgen regulation of the TMPRSS2 gene and the effect of a SNP in an androgen response element", Mol Endocrinol, 27, pp.2028~2040 (2013)
- Senapati S, "Assessment of risk conferred by coding and regulatory variations of TMPRSS2and CD26 in susceptibility to SARS-CoV-2 infection in human", J Genet, 99, pp.53~ (2020)
- Vankadari N, "Emerging WuHan (COVID-19) coronavirus:glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26", Emerg Microbes Infect, 9, pp.601~604 (2020)
- Beutler B, "Innate immunity: an overview", Mol Immunol, 40, pp.945~959 (2004)
- Ivashkiv LB, "Regulation of type I interferon responses", Nat Rev Immunol, 14, pp.36~49 (2014)
- Schneider WM, "Interferon-stimulated genes: a complex web of host defenses", Annu Rev Immunol, 32, pp.513~545 (2014)
- García-Sastre A, "Type 1 interferons and the virus–host relationship: a lesson in détente", Science, 312, pp.879~882 (2006)
- Stender JD, "Epigenomic control of the innate immune response", Curr Opin Pharmacol, 13, pp.582~587 (2013)
- Agalioti T, "Ordered recruitment of chromatin modifying and general transcription factors to the IFN-β promoter", Cell, 103, pp.667~678 (2000)
- Busslinger M, "Epigenetic control of immunity", Cold Spring Harb Perspect Biol, 6, pp.a019307~ (2014)
- Smale ST, "Chromatin contributions to the regulation of innate immunity", Annu Rev Immunol, 32, pp.489~511 (2014)
- Marban C, "Recruitment of chromatin-modifying enzymes by CTIP2 promotes HIV-1 transcriptional silencing", EMBO J, 26, pp.412~423 (2007)
- Corley MJ, "methylation analysis of the COVID-19 host cell receptor, angiotensin convert enzyme 2 gene (ACE2) in the respiratory system reveal age and gender differences", Preprints, pp.2020030295~ (2020)
- Pinto BGG, "ACE2 Expression is Increased in the Lungs of Patients with Comorbidities Associated with Severe COVID-19", J Infect Dis, 222, pp.556~563 (2020)
- Sawalha AH, "Epigenetic dysregulation of ACE2and interferonregulated genes might suggest increased COVID-19 susceptibility and severity in lupus patients", Clin Immunol, 215, pp.108410~ (2020)
- Pfeffer S, "Identification of virus-encoded microRNAs", Science, 304, pp.734~736 (2004)
- Saçar Demirci MD, "Computational analysis of microRNAmediated interactions in SARS-CoV-2 infection", PeerJ, 8, pp.e9369~ (2020)
