Annals of Hematology, Год журнала: 2022, Номер 101(9), С. 1887 - 1895
Опубликована: Июль 8, 2022
Язык: Английский
Viruses, Год журнала: 2022, Номер 14(11), С. 2535 - 2535
Опубликована: Ноя. 16, 2022
Severe acute respiratory syndrome-related coronavirus (SARS-CoV-2), the causative agent of disease 2019 (COVID-19), is highly contagious and remains a major public health challenge despite availability effective vaccines. SARS-CoV-2 enters cells through binding its spike receptor-binding domain (RBD) to human angiotensin-converting enzyme 2 (ACE2) receptor in concert with accessory receptors/molecules that facilitate viral attachment, internalization, fusion. Although ACE2 plays critical role replication, expression profiles are not completely associated infection patterns, immune responses, clinical manifestations. Additionally, infects lack ACE2, resistant monoclonal antibodies against RBD vitro, indicating some possess ACE2-independent alternative receptors, which can mediate entry. Here, we discuss these receptors their interactions components for These include CD147, AXL, CD209L/L-SIGN/CLEC4M, CD209/DC-SIGN/CLEC4L, CLEC4G/LSECtin, ASGR1/CLEC4H1, LDLRAD3, TMEM30A, KREMEN1. Most known be involved entry other viruses modulate cellular functions responses. The omicron variant exhibits altered cell tropism an change pathway, emerging variants may use escape pressure ACE2-dependent provided by vaccination RBD. Understanding pathogenesis provide avenues prevention treatment COVID-19.
Язык: Английский
Процитировано
72
Frontiers in Microbiology, Год журнала: 2020, Номер 11
Опубликована: Сен. 30, 2020
The coronavirus disease 19 (COVID-19) caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), has become a global pandemic since the first report in Wuhan. COVID-19 is zoonotic and natural reservoir of SARS-CoV-2 seems to be bats. However, intermediate host explaining transmission evolvement still unclear. In addition wildlife which access contact with bats ecological environment then infects humans market, domestic animals are also able establish themselves as after infected SARS-CoV-2. Although recent studies related have made lot progress, many critical issues unaddressed. Here, we reviewed findings regarding investigations host, may inspire future investigators provide them plenty information. results demonstrate role chain SARS-CoV-2, efficient intervention on this basis useful prevent further deterioration COVID-19.
Язык: Английский
Процитировано
134
The Science of The Total Environment, Год журнала: 2021, Номер 808, С. 152072 - 152072
Опубликована: Дек. 1, 2021
Язык: Английский
Процитировано
96
Cells, Год журнала: 2021, Номер 10(6), С. 1434 - 1434
Опубликована: Июнь 8, 2021
In late 2019, the betacoronavirus SARS-CoV-2 was identified as viral agent responsible for coronavirus disease 2019 (COVID-19) pandemic. Coronaviruses Spike proteins are their ability to interact with host membrane receptors and different have been interactors, among which Angiotensin-converting enzyme 2 (ACE2), Basigin2/EMMPRIN/CD147 (CD147). CD147 plays an important role in human immunodeficiency virus type 1, hepatitis C virus, B Kaposi’s sarcoma-associated herpesvirus, severe acute respiratory syndrome infections. particular, SARS-CoV recognizes receptor expressed on surface of cells by its nucleocapsid protein binding cyclophilin A (CyPA), a ligand CD147. However, involvement infection is still debated. Interference both function (blocking antibody) expression (knock down) showed that this partakes provided additional clues underlying mechanism: CyPA does not play role; regulates ACE2 levels affected infection. Altogether, these findings suggest involved tropism represents possible therapeutic target challenge COVID-19.
Язык: Английский
Процитировано
89
Journal of Thrombosis and Haemostasis, Год журнала: 2020, Номер 19(1), С. 46 - 50
Опубликована: Окт. 29, 2020
Язык: Английский
Процитировано
85
Journal of Biological Chemistry, Год журнала: 2020, Номер 296, С. 100135 - 100135
Опубликована: Дек. 2, 2020
The ongoing COVID-19 pandemic has already caused over a million deaths worldwide, and this death toll will be much higher before effective treatments vaccines are available. causative agent of the disease, coronavirus SARS-CoV-2, shows important similarities with previously emerged SARS-CoV-1, but also striking differences. First, SARS-CoV-2 possesses significantly transmission rate infectivity than SARS-CoV-1 infected in few months 60 people. Moreover, systemic character, as addition to lungs, it affects heart, liver, kidneys among other organs patients causes frequent thrombotic neurological complications. In fact, term "viral sepsis" been recently coined describe clinical observations. Here I review current structure–function information on viral spike proteins membrane fusion process provide plausible explanations for these hypothesize that several membrane-associated serine proteinases (MASPs), synergy or place TMPRSS2, contribute activate protein. Relative concentrations attachment receptor, ACE2, MASPs, their endogenous inhibitors (the Kunitz-type transmembrane inhibitors, HAI-1/SPINT1 HAI-2/SPINT2, well major circulating serpins) would determine infection host cells. exclusive predominant expression MASPs specific human suggests direct role e.g., heart myocardial injury, liver dysfunction, kidney damage, Thorough consideration factors could have positive impact control pandemic. Coronaviruses cause diseases humans, most notably severe acute respiratory syndrome (SARS) Middle East (MERS). According currently accepted mechanism infection, both SARS-CoV (also termed SARS-CoV-1) related, rely two membrane-bound peptidases entry into target cells: carboxypeptidase, angiotensin-converting enzyme 2 (ACE2), proteinase known TMPRSS2/TMPS2 epitheliasin. (TMPRSS stands "Transmembrane Protease, Serine"). protruding (S) glycoproteins SARS-CoVs interact first ACE2 then proteolytically cleaved by TMPRSS2 trigger envelope cell (1Li W. Moore M.J. Vasilieva N. Sui J. Wong S.K. Berne M.A. Somasundaran M. Sullivan J.L. Luzuriaga K. Greenough T.C. Choe H. Farzan Angiotensin-converting is functional receptor SARS coronavirus.Nature. 2003; 426: 450-454Crossref PubMed Scopus (3107) Google Scholar, 2Belouzard S. Chu V.C. Whittaker G.R. Activation protein via sequential proteolytic cleavage at distinct sites.Proc. Natl. Acad. Sci. U. A. 2009; 106: 5871-5876Crossref (477) 3Heurich Hofmann-Winkler Gierer Liepold T. Jahn O. Pöhlmann ADAM17 cleave differentially only proteolysis augments driven protein.J. Virol. 2014; 88: 1293-1307Crossref (380) 4Kirchdoerfer R.N. Cottrell C.A. Wang Pallesen Yassine H.M. Turner H.L. Corbett K.S. Graham B.S. McLellan J.S. Ward A.B. Pre-fusion structure protein.Nature. 2016; 531: 118-121Crossref (335) 5Yuan Y. Cao D. Zhang Ma Qi Q. Lu G. Wu Yan Shi X. Gao G.F. Cryo-EM structures MERS-CoV reveal dynamic binding domains.Nat. Commun. 2017; 8: 15092Crossref (349) 6Hoffmann Kleine-Weber Schroeder Krüger Herrler Erichsen Schiergens T.S. N.H. Nitsche Müller Drosten C. depends blocked clinically proven protease inhibitor.Cell. 2020; 181: 271-280.e278Abstract Full Text PDF (6634) 7Shang Wan Luo Ye Geng Auerbach Li F. Cell mechanisms SARS-CoV-2.Proc. 117: 11727-11734Crossref (865) 8Lan Ge Yu Shan Zhou Fan L. Structure receptor-binding domain bound receptor.Nature. 581: 215-220Crossref (1631) 9Wang Niu Song Z. Qiao Hu Yuen K.-Y. Structural basis using ACE2.Cell. 894-904.e899Abstract (948) Scholar). (See Fig. 1A organization S 1, B–C its three-dimensional (3D) structure). plays dual cleaves which increases uptake likely virions (3Heurich addition, activates pathogenic coronaviruses common cold strains influenza A viruses, although pathogens use unrelated receptors (10Zumla Chan J.F. Azhar E.I. Hui D.S. K.Y. - drug discovery therapeutic options.Nat. Rev. Drug Discov. 15: 327-347Crossref (841) extraordinarily rapid spread absence vaccine pharmacological drugs capable inhibiting large economic spurred intense research mechanism, key factor pathogenesis. Among unresolved issues, there questions particular relevance. why does virus show SARS-CoV, despite highly similar structures, including about 90% conserved residues proteins? Second, infecting different organs, contrast rather restricted tropism SARS-CoV? answer follows, based careful analysis available regarding process. activated ("primed") upon peptide bonds: one, corresponding Arg685-Ser686 protein, separates so-called S1 S2 subunits (Fig. 1A) (2Belouzard N-terminal subunit contains (RBD) responsible (8Lan 11Shang Aihara recognition SARS-CoV-2.Nature. 221-224Crossref (1236) 12Yan R. Xia Guo full-length ACE2.Science. 367: 1444-1448Crossref (1824) Scholar), while C-terminal remains attached after S1/S2 site ultimately membrane. This initial followed S2' (Arg815-Ser816 SARS-CoV-2; 1D), exposes antigenic Ser816-Phe833 peptide, elicits major, irreversible conformational changes. results radically conformation competent (see refs. 13Wrapp Goldsmith J.A. Hsieh C.L. Abiona 2019-nCoV prefusion conformation.Science. 1260-1263Crossref (20) Scholar) 1C). As difference bond efficiently severed another proteinase, proprotein convertase furin, within secretory pathway cells (7Shang (For roles furin homeostasis see ref. (14Thomas Furin cutting edge: from traffic embryogenesis disease.Nat. Mol. Biol. 2002; 3: 753-766Crossref (862) Scholar)). Because furin-mediated proteolysis, found preactivated state require single bond, Arg815-Ser816, activation machinery. unique feature essential protein-mediated cell–cell thus, an determinant pathogenesis (6Hoffmann canonical activator SARS-CoV-1/-2, belongs subfamily multidomain, development (15Hooper J.D. Clements Quigley J.P. Antalis T.M. Type II proteases. Insights emerging class surface enzymes.J. Chem. 2001; 276: 857-860Abstract (312) 16Qiu Owen Gray Bass Ellis V. Roles regulation proteases.Biochem. Soc. Trans. 2007; 35: 583-587Crossref (35) 17Choi S.Y. Bertram Glowacka I. Park Y.W. proteases cancer infections.Trends Med. 303-312Abstract (68) 18Bugge T.H. proteases.J. 284: 23177-23181Abstract (211) 19Szabo Bugge Membrane-anchored vertebrate developmental biology.Annu. Dev. 2011; 27: 213-235Crossref (81) (The (MASPs) schematically represented 2; relevant enzymes summarized Table 1). Notably, exclusively predominantly expressed (corin/TMPRSS10), (hepsin/TMPRSS1 matriptase-2/TMPRSS6), brain (spinesin/TMPRSS5), esophagus (TMPRSS4 TMPRSS11A F), prostate (TMPRSS2 prostasin/PRSS8), testes (matriptase-3/TMPRSS7, TMPRSS12, testisin/PRSS21, TESSP-1/PRSS41, T-SP1/PRSS55) (Figs. 3A 4A).Table 1Summary (MASPs)Recommended MASP nameaAs deposited UniProt database./Other namesEC/MEROPSbAccession numbers according Enzyme Commission (EC) MEROPS databases.Gene nameLength (residues)Expression pattern relevance pathologyHepsinTMPRSS13.4.21.106/S01.224HPN (TMPRSS1)417Expressed highest levels liver. Also high pancreas. Other organs: stomach thyroid gland. Overexpressed primary tumors, ovarian cancers.TMPS2TMPRSS2, epitheliasin, 10 (PRSS10)3.4.21.-/S01.247TMPRSS2 (PRSS10)492Highest prostate, stomach, small intestine, colon. Expressed airway alveolar patients. Proteolytically proteins, triggers virus–cell fusion.TMPS3TMPRSS3, tumor-associated gene 12 (TADG-12)3.4.21.-/S01.079TMPRSS3 (ECHOS1, TADG12)454TTSP reported endothelium reticulum inner ear linked deafness. low breast, organs.TMPS4TMPRSS4, channel-activating (CAPH2), membrane-type (MT-SP2)3.4.21.-/S01.034TMPRSS4437Highest esophagus. Broadly kidney, bladder, colon, vagina, tissues. Upregulated gastric cancers.TMPS5TMPRSS5, spinal cord–enriched trypsin-like (spinesin)3.4.21.-/S01.313TMPRSS5457Predominantly neurons, axons, synapses motor neurons cord. tibial nerve. throughout brain.TMPS6TMPRSS6, matriptase-2 (MT2)3.4.21.-/S01.308TMPRSS6811Highest testis pituitary Plays critical iron through BMP coreceptor, hemojuvelin.TMPS7TMPRSS7, matriptase-3 (MT3)3.4.21.-/S01.072TMPRSS7843Highest testis. significant skin, brain, pituitary, thyroid, minor salivary glands.TMPS9TMPRSS9, polyserine polyserase-13.4.21.-/S01.357TMPRSS91059Highest testis, spleen liver.CorinTMPRSS10, atrial natriuretic peptide-converting enzyme, heart-specific ATC23.4.21.-/S01.019CORIN (CRN, TMPRSS10)1042Highly (left ventricle appendage). uterus, organs. Activates cardiac hormone, thus involved blood pressure regulation.TM11ATMPRSS11A, (HATL1), esophageal cancer-susceptibility 1 epidermal type-II protease3.4.21.-/S01.292TMPRSS11A (HATL1, ECRG1, HESP)421Expressed esophagus, cervix. lungs.TM11BTMPRSS11B, 5 (HATL5)3.4.21.-/S01.365TMPRSS11B416Expressed cervix, oral cavity. Significantly decreased cervical, esophageal, head neck carcinomas. Highly upregulated lung squamous carcinoma.TM11DTMPRSS11D, (HAT)3.4.21.-/S01.047TMPRSS11D (HAT)418Expressed vagina submucosal serous glands bronchi trachea.TM11ETMPRSS11E, differentially-expressed carcinoma (DESC1)3.4.21.-/S01.021TMPRSS11E (DESC1)423Expressed vagina. bladder. tumors origin.TM11 FTMPRSS11 F, 4 (HATL4)3.4.21.-/S01.321TMPRSS11F (HATL4)438Expressed skin. Unique function barrier formation.TMPSCTMPRSS123.4.21.-/S01.291TMPRSS12348Type almost colorectal cancer.TMPSDTMPRSS13, mosaic (MSP, MSPL, MSPS)3.4.21.-/S01.087TMPRSS13 TMPRSS11)586Predominantly Cell-surface regulated phosphorylation intracellular peptide.ST14TMPRSS14, matriptase, (MT-SP1), 15 (TADG-15), epithin, SNC193.4.21.109/S01.302ST14 (PRSS14, SNC19, TADG15)855Ubiquitously expressed, colon lung, kidneys, Proteolytic activity epithelial integrity. Implicated progression cancers. Proposed play breast invasion metastasis. Forms reciprocal zymogen complex prostasin.EnteropeptidaseTMPRSS15, enterokinase, 7 (PRSS7)3.4.21.9/S01.156TMPRSS15 (ENTK, PRSS7)1019Expression intestine. Starts cascade leading digestive converting trypsinogen trypsin.ProstasinPRSS8, protease-1 (CAP1), 8 (PRSS8)3.4.21.-/S01.159PRSS8343cRefers protein; Met1-Gly29 form signal removed, Ala30-Gly32 peptide. Pro323-His343 removed during maturation.Type preference polybasic substrates.dAccording some authors, GPI-anchored instead. Ubiquitously gland, (renal proximal tubular cells), matriptase.TestisinPRSS21, eosinophil (ESP1), TESP53.4.21.-/S01.011PRSS21 (ESP1, TEST1)314eRefers Met1-Arg19 removed. propeptide, Gly289-Val314, maturation.GPI-anchored lost testicular tumors. gland lungs. Important sperm maturation fertilizing ability.PRSS41Testis (TESSP-1)3.4.21.-/S01.417TESSP1318fRefers Met1-Gly19 Thr300-Pro318, maturation.Testis-specific Required meiosis spermatogenesis.PRSS55Testis (T-SP1)3.4.21.-/S01.299PRSS55 (TSP1)352gRefers Met1-Leu18, Gly326-Tyr352 protein.hControversial. brain. cancer. crucial migration sperm–egg interaction.Information gathered (www.uniprot.org) databases (https://www.ebi.ac.uk/merops/) cited references.a database.b Accession databases.c Refers maturation.d instead.e maturation.f maturation.g maturation.h Controversial. Open table new tab Figure 3Expression patterns proteinases. A, MASPs. Data indicated males females, no sex-associated differences GTEx Portal (gtexportal.org) 4A). B–C, 3D crystal hepsin/TMPRSS1 ectodomain, cartoon highlighting secondary elements; loops shape active-site cleft noted. (After PDB 1P57: SRCR module (deep-teal cyan); (deep salmon-red)). small-molecule inhibitor specificity pocket (2-{5-[amino(iminio)methyl]-1H-benzimidazol-2-YL}benzenolate) shown color-coded spheres (carbon, pink; oxygen, red; nitrogen, blue; hydrogen, gray). B, side view, proximity residue domain, Pro50, helix, Gly24-Leu44. locates rigidly catalytic essentially flat against (74Somoza J.R. Ho Luong Ghate Sprengeler P.A. Mortara Shrader W.D. Sperandio McGrath M.E. Katz B.A. extracellular region hepsin reveals novel scavenger cysteine-rich (SRCR) domain.Structure. 11: 1123-1131Abstract (67) localization should expected domains implies Arg815-Ser816 close membrane, facilitating interaction exposed escape immune surveillance. C, view "standard orientation", (given all nonhydrogen atoms, color-coded) facing viewer substrates running left right. N C termini chain noted (Ile16 Thr253, respectively) Asp189 bottom pocket, largely basic Arg/Lys residue.View Large Image ViewerDownload Hi-res image Download (PPT)Figure 4Expression inhibitors. comparison selection those patterns. Spinesin/TMPRSS5 nerve, corin PRSS21, PRSS41 PRSS51 Further, respectively. members tract subgroup, TMPRSS11A–11F mucosa schematic representation proteinases, HAI-2/SPINT2. C–D, HAI-1 (C) HAI-2 (D). Note overall complementarity profiles (e.g., not paralog arteries), similarly extremely Kunitz noteworthy, MASP, corin/TMPRSS10, controlled serpins. values given Transcripts per Million (TPM), GTex (gtexportal.org). HAI, hepatocyte growth inhibitor; MANEC, motif N-terminus eight-cysteines; SPINT, type.View (PPT) Information references. Most possess basal zymogenic, single-chain forms generate full clustering autoactivation trans. Prostasin, autoactivate (20Shipway Danahay Williams Tully D.C. Backes B.J. Harris Biochemical characterization prostasin, channel activating protease.Biochem. Biophys. Res. 2004; 324: 953-963Crossref (61) evolutionary matriptase (21Friis Uzzun Sales Godiksen Peters D.E. Lin C.Y. Vogel L.K. matriptase-prostasin features: prostasin non-enzymatic co-factor activation.J. 2013; 288: 19028-19039Abstract (57) 22Drees Königsmann Jaspers M.H.J. Pflanz Riedel Schuh Conserved morphogenesis.PLoS Genet. 2019; 15e1007882Crossref (3) androgen-induced (23Ko C.-J. Huang C.-C. H.-Y. Juan C.-P. Lan S.-W. Shyu S.-R. Hsiao P.-W. H.-P. Shun C.-T. Lee M.-S. Androgen-induced promotes matrix degradation, invasion, tumor growth, metastasis.Cancer 2015; 75: 2949-2960Crossref These predicted initiators cascades trans- coactivating (16Qiu physiological such G-protein-coupled protease-activated (PAR2), sodium (ENaC), metalloproteinases (MMPs), prohepatocyte (pro-HGF). poorly understood cross talk between coagulation fibrinolytic cascades, urokinase-type plasminogen (uPA) (24Kilpatrick L.M. R.L. K.A. Ghorayeb Bar-Or Initiation monocytes expressing type matriptase.Blood. 2006; 108: 2616-2623Crossref (88) 25Le Gal
Язык: Английский
Процитировано
82
Immunobiology, Год журнала: 2020, Номер 225(6), С. 152008 - 152008
Опубликована: Авг. 19, 2020
Язык: Английский
Процитировано
77
Seminars in Cancer Biology, Год журнала: 2021, Номер 83, С. 384 - 398
Опубликована: Янв. 20, 2021
Язык: Английский
Процитировано
76
Cell Metabolism, Год журнала: 2022, Номер 34(6), С. 857 - 873.e9
Опубликована: Май 12, 2022
It is not well understood why diabetic individuals are more prone to develop severe COVID-19. To this, we here established a human kidney organoid model promoting early hallmarks of disease development. Upon SARS-CoV-2 infection, diabetic-like organoids exhibited higher viral loads compared with their control counterparts. Genetic deletion the angiotensin-converting enzyme 2 (ACE2) in under or conditions prevented detection. Moreover, cells isolated from biopsies patients altered mitochondrial respiration and enhanced glycolysis, resulting infections non-diabetic cells. Conversely, exposure patient dichloroacetate (DCA), an inhibitor aerobic resulted reduced infections. Our results provide insights into identification diabetic-induced metabolic programming as critical event increasing infection susceptibility, opening door new interventions COVID-19 pathogenesis targeting energy metabolism.
Язык: Английский
Процитировано
65
Journal of Thrombosis and Haemostasis, Год журнала: 2021, Номер 20(2), С. 434 - 448
Опубликована: Окт. 28, 2021
Язык: Английский
Процитировано
61