Development of novel entry inhibitors targeting emerging viruses

Expert Review of Anti-Infective Therapy

Volumn 10, Issue 10, 2012, Pages 1129-1138

  Zhou, Yanchen ^a   Simmons, Graham ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

antiviral therapies; broad spectrum viral entry inhibitors; emerging viruses; high throughput screening; viral entry

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; 4 BENZOYL 1 [(4 METHOXY 1H PYRROLO[2,3 B]PYRIDIN 3 YL)OXOACETYL] 2 METHYLPIPERAZINE; [1 [(1 FORMYL 2 PHENYLETHYL)CARBAMOYL] 2 METHYLPROPYL]CARBAMIC ACID BENZYL ESTER; ANTIVIRUS AGENT; ARBIDOL; CATHEPSIN B; CATHEPSIN L; CHLOROQUINE; CHLORPROMAZINE; CID 23631927; CYANOVIRIN N; CYTOCHALASIN D; EMODIN; LJ 001; MARAVIROC; N (3 PROPYLCARBAMOYLOXIRANE 2 CARBONYL)ISOLEUCYLPROLINE; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; WORTMANNIN; WRR 182; WRR 183; WRR 495;

CONFORMATIONAL TRANSITION; DRUG STRUCTURE; EBOLA VIRUS; ENDOCYTOSIS; ENDOSOME; HIGH THROUGHPUT SCREENING; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS; INFLUENZA; LYSOSOME; MEMBRANE FUSION; NONHUMAN; PINOCYTOSIS; REVIEW; SARS CORONAVIRUS; UNSPECIFIED SIDE EFFECT; VIRUS ATTACHMENT; VIRUS CELL INTERACTION; VIRUS ENTRY; VIRUS MUTATION; VIRUS TRANSMISSION;

ANTIVIRAL AGENTS; COMMUNICABLE DISEASES, EMERGING; HIGH-THROUGHPUT SCREENING ASSAYS; HOST-PATHOGEN INTERACTIONS; RECEPTORS, VIRUS; VIRUS ATTACHMENT; VIRUS INTERNALIZATION;

EID: 84870599997     PISSN: 14787210     EISSN: 17448336     Source Type: Journal    
DOI: 10.1586/eri.12.104     Document Type: Review

References (113)

1. Snell NJ. Ribavirin-current status of a broad spectrum antiviral agent. Expert Opin. Pharmacother. 2(8), 1317-1324 (2001).
2. Wong AC, Sandesara RG, Mulherkar N, Whelan SP, Chandran K. A forward genetic strategy reveals destabilizing mutations in the Ebolavirus glycoprotein that alter its protease dependence during cell entry. J. Virol. 84(1), 163-175 (2010).
3. Zhaori G. Antiviral treatment of SARS: can we draw any conclusions? CMAJ 169 (11), 1165-1166 (2003).
4. Chong HT, Kamarulzaman A, Tan CT et al. Treatment of acute Nipah encephalitis with ribavirin. Ann. Neurol. 49(6), 810-813 (2001).
5. Jahrling PB, Geisbert T W, Geisbert JB et al. Evaluation of immune globulin and recombinant interferon-alpha2b for treatment of experimental Ebola virus infections. J. Infect. Dis. 179(Suppl. 1), S224-S234 (1999).
6. Ignat'ev GM, Strel'tsova MA, Agafonov AP, Kashentseva EA, Prozorovskii NS. [Experimental study of possible treatment of Marburg hemorrhagic fever with desferal, ribavirin, and homologous interferon]. Vopr. Virusol. 41(5), 206-209 (1996).
7. Hoffmann HH, Kunz A, Simon VA, Palese P, Shaw ML. Broad-spectrum antiviral that interferes with de novo pyrimidine biosynthesis. Proc. Natl Acad. Sci. USA 108(14), 5777-5782 (2011).
8. Wong JP, Christopher ME, Salazar AM et al. Broad-spectrum and virus-specifc nucleic acid-based antivirals against infuenza. Front. Biosci. (Schol. Ed.). 2, 791-800 (2010).
9. Furuta Y, Takahashi K, Shiraki K et al. T-705 (favipiravir) and related compounds: novel broad-spectrum inhibitors of RNA viral infections. Antiviral Res. 82(3), 95-102 (2009).
10. Chamoun AM, Chockalingam K, Bobardt M et al. PD 404, 182 is a virocidal small molecule that disrupts hepatitis C virus and human immunodefciency virus. Antimicrob. Agents Chemother. 56(2), 672-681 (2012).
11. Pöhlmann S, Reeves JD. Cellular entry of HIV: evaluation of therapeutic targets. Curr. Pharm. Des. 12(16), 1963-1973 (2006).
12. Singh IP, Chauthe SK. Small molecule HIV entry inhibitors: part II. Attachment and fusion inhibitors:2004-2010. Expert Opin. Ther. Pat. 21(3), 399-416 (2011).
13. Emau P, Tian B, O'Keefe BR et al. Griffthsin, a potent HIV entry inhibitor, is an excellent candidate for anti-HIV microbicide. J. Med. Primatol. 36(4-5), 244-253 (2007).
14. Zhou Y, Agudelo J, Lu K et al. Inhibitors of SARS-CoV entry-identifcation using an internally-controlled dual envelope pseudovirion assay. Antiviral Res. 92(2), 187-194 (2011).
15. Talekar A, Pessi A, Glickman F et al. Rapid screening for entry inhibitors of highly pathogenic viruses under low-level biocontainment. PLoS ONE 7(3), e30538 (2012).
16. Wool-Lewis RJ, Bates P. Characterization of Ebola virus entry by using pseudotyped viruses: identifcation of receptor-defcient cell lines. J. Virol. 72(4), 3155-3160 (1998).
17. Simmons G, Reeves JD, Rennekamp AJ, Amberg SM, Piefer AJ, Bates P. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc. Natl Acad. Sci. USA 101(12), 4240-4245 (2004).
18. Matsuura Y, Tani H, Suzuki K et al. Characterization of pseudotype VSV possessing HCV envelope proteins. Virology 286(2), 263-275 (2001).
19. Basu A, Mills DM, Bowlin TL. High-throughput screening of viral entry inhibitors using pseudotyped virus. Curr. Protoc. Pharmacol. Chapter 13, Unit 13B.3 (2010).
20. Baldick CJ, Wichroski MJ, Pendri A et al A novel small molecule inhibitor of hepatitis C virus entry. PLoS Pathog 6(9), e1001086 (2010).
21. Filone CM, Heise M, Doms RW, Bertolotti-Ciarlet A. Development and characterization of a Rift Valley fever virus cell-cell fusion assay using alphavirus replicon vectors. Virology 356(1-2), 155-164 (2006).
22. Wolf MC, Wang Y, Freiberg AN, Aguilar HC, Holbrook MR, Lee B. A catalytically and genetically optimized beta-lactamase-matrix based assay for sensitive, specifc, and higher throughput analysis of native henipavirus entry characteristics. Virol. J. 6, 119 (2009).
23. Kaufmann B, Chipman PR, Holdaway HA et al. Capturing a favivirus pre-fusion intermediate. PLoS Pathog. 5(11), e1000672 (2009).
24. Li L, Jose J, Xiang Y, Kuhn RJ, Rossmann MG. Structural changes of envelope proteins during alphavirus fusion. Nature 468(7324), 705-708 (2010).
25. Carette JE, Raaben M, Wong AC et al. Ebola virus entry requires the cholesterol transporter Niemann-Pick C1. Nature 477(7364), 340-343 (2011).
26. Côté M, Misasi J, Ren T et al. Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature 477(7364), 344-348 (2011).
27. Miller EH, Obernosterer G, Raaben M et al. Ebola virus entry requires the host-programmed recognition of an intracellular receptor. EMBO J. 31(8), 1947-1960 (2012).
28. Becker S, Spiess M, Klenk HD. The asialoglycoprotein receptor is a potential liver-specifc receptor for Marburg virus. J. Gen. Virol. 76 (Pt 2), 393-399 (1995).
29. Dominguez-Soto A, Aragoneses-Fenoll L, Martin-Gayo E et al. The DC-SIGN-related lectin LSECtin mediates antigen capture and pathogen binding by human myeloid cells. Blood 109(12), 5337-5345 (2007).
30. Lin G, Simmons G, Pöhlmann S et al Differential N-linked glycosylation of human immunodefciency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR. J. Virol. 77(2), 1337-1346 (2003).
31. Simmons G, Reeves JD, Grogan CC et al. DC-SIGN and DC-SIGNR bind Ebola glycoproteins and enhance infection of macrophages and endothelial cells. Virology 305(1), 115-123 (2003).
32. Takada A, Fujioka K, Tsuiji M et al. Human macrophage C-type lectin specifc for galactose and N-acetylgalactosamine promotes flovirus entry. J. Virol. 78(6), 2943-2947 (2004).
33. Navarro-Sanchez E, Altmeyer R, Amara A et al. Dendritic-cell-specifc ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep. 4(7), 723-728 (2003).
34. Tassaneetrithep B, Burgess TH, Granelli-Piperno A et al. DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells. J. Exp. Med. 197(7), 823-829 (2003).
35. Yang ZY, Huang Y, Ganesh L et al pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN. J. Virol. 78(11), 5642-5650 (2004).
36. Spillmann D. Heparan sulfate: anchor for viral intruders? Biochimie 83(8), 811-817 (2001).
37. Barth H, Schafer C, Adah MI et al. Cellular binding of hepatitis C virus envelope glycoprotein E2 requires cell surface heparan sulfate. J. Biol. Chem. 278(42), 41003-41012 (2003).
38. González ME, Alarcón B, Carrasco L. Polysaccharides as antiviral agents: antiviral activity of carrageenan. Antimicrob. Agents Chemother. 31(9), 1388-1393 (1987).
39. Krepstakies M, Lucifora J, Nagel CH et al A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses. J. Infect. Dis. 205(11), 1654-1664 (2012).
40. Donalisio M, Rusnati M, Civra A et al. Identifcation of a dendrimeric heparan sulfate-binding peptide that inhibits infectivity of genital types of human papillomaviruses. Antimicrob. Agents Chemother. 54(10), 4290-4299 (2010).
41. Schuksz M, Fuster MM, Brown JR et al. Surfen, a small molecule antagonist of heparan sulfate. Proc. Natl Acad. Sci. USA 105(35), 13075-13080 (2008).
42. Botos I, Wlodawer A. Cyanovirin-N: a sugar-binding antiviral protein with a new twist. Cell. Mol. Life Sci. 60(2), 277-287 (2003).
43. Barrientos LG, O'Keefe BR, Bray M, Sanchez A, Gronenborn AM, Boyd MR. Cyanovirin-N binds to the viral surface glycoprotein, GP1, 2 and inhibits infectivity of Ebola virus. Antiviral Res. 58(1), 47-56 (2003).
44. Barrientos LG, Lasala F, Otero JR, Sanchez A, Delgado R. In vitro evaluation of cyanovirin-N antiviral activity, by use of lentiviral vectors pseudotyped with flovirus envelope glycoproteins. J. Infect. Dis. 189(8), 1440-1443 (2004).
45. O'Keefe BR, Giomarelli B, Barnard DL et al. Broad-spectrum in vitro activity and in vivo effcacy of the antiviral protein griffthsin against emerging viruses of the family Coronaviridae. J. Virol. 84(5), 2511-2521 (2010).
46. O'Keefe BR, Smee DF, Turpin JA et al. Potent anti-infuenza activity of cyanovirin-N and interactions with viral hemagglutinin. Antimicrob. Agents Chemother. 47(8), 2518-2525 (2003).
47. van der Meer FJ, de Haan CA, Schuurman NM et al. Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture. Antiviral Res. 76(1), 21-29 (2007).
48. Helle F, Wychowski C, Vu-Dac N, Gustafson KR, Voisset C, Dubuisson J. Cyanovirin-N inhibits hepatitis C virus entry by binding to envelope protein glycans. J. Biol. Chem. 281(35), 25177-25183 (2006).
49. Smee DF, Bailey KW, Wong MH et al. Treatment of infuenza A (H1N1) virus infections in mice and ferrets with cyanovirin-N. Antiviral Res. 80(3), 266-271 (2008).
50. Li W, Moore MJ, Vasilieva N et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426(6965), 450-454 (2003).
51. Negrete OA, Levroney EL, Aguilar HC et al. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436(7049), 401-405 (2005).
52. Kondratowicz AS, Lennemann NJ, Sinn PL et al. T-cell immunoglobulin and mucin domain 1 (TIM-1) is a receptor for Zaire Ebolavirus and Lake Victoria Marburgvirus. Proc. Natl Acad. Sci. USA 108(20), 8426-8431 (2011).
53. Ho TY, Wu SL, Chen JC, Li CC, Hsiang CY. Emodin blocks the SARS coronavirus spike protein and angiotensin-converting enzyme 2 interaction. Antiviral Res. 74(2), 92-101 (2007).
54. Lin PF, Blair W, Wang T et al. A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding. Proc. Natl Acad. Sci. USA 10 0 (19), 11013-11018 (2003).
55. Si Z, Madani N, Cox JM et al. Small-molecule inhibitors of HIV-1 entry block receptor-induced conformational changes in the viral envelope glycoproteins. Proc. Natl Acad. Sci. USA 101(14), 5036-5041 (2004).
56. Mercer J, Schelhaas M, Helenius A. Virus entry by endocytosis. Annu. Rev. Biochem. 79, 803-833 (2010).
57. Sanchez A. Analysis of flovirus entry into vero e6 cells, using inhibitors of endocytosis, endosomal acidifcation, structural integrity, and cathepsin (B and L) activity. J. Infect. Dis. 196(Suppl. 2), S251-S258 (2007).
58. Empig CJ, Goldsmith MA. Association of the caveola vesicular system with cellular entry by floviruses. J. Virol. 76 (10), 5266-5270 (2002).
59. Saeed MF, Kolokoltsov AA, Albrecht T, Davey RA. Cellular entry of Ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent traffcking through early and late endosomes. PLoS Pathog. 6 (9), e1001110 (2010).
60. Nanbo A, Imai M, Watanabe S et al. Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner. PLoS Pathog. 6(9), e1001121 (2010).
61. Mulherkar N, Raaben M, de la Torre JC, Whelan SP, Chandran K. The Ebola virus glycoprotein mediates entry via a non-classical dynamin-dependent macropinocytic pathway. Virology 419 (2), 72-83 (2011).
62. Saeed MF, Kolokoltsov AA, Freiberg AN, Holbrook MR, Davey RA. Phosphoinositide-3 kinase-Akt pathway controls cellular entry of Ebola virus. PLoS Pathog. 4(8), e1000141 (2008).
63. Krishnan MN, Sukumaran B, Pal U et al. Rab 5 is required for the cellular entry of dengue and West Nile viruses. J. Virol. 81(9), 4881-4885 (2007).
64. Pernet O, Pohl C, Ainouze M, Kweder H, Buckland R. Nipah virus entry can occur by macropinocytosis. Virology 395(2), 298-311 (2009).
65. Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308(5728), 1643-1645 (2005).
66. Schornberg K, Matsuyama S, Kabsch K, Delos S, Bouton A, White J. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 80 (8), 4174-4178 (2006).
67. Kaletsky RL, Simmons G, Bates P. Proteolysis of the Ebola virus glycoproteins enhances virus binding and infectivity. J. Virol. 81(24), 13378-13384 (2007).
68. Misasi J, Chandran K, Yang JY et al. Filoviruses require endosomal cysteine proteases for entry but exhibit distinct protease preferences. J. Virol. 86(6), 3284-3292 (2012).
69. Simmons G, Gosalia DN, Rennekamp AJ, Reeves JD, Diamond SL, Bates P. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc. Natl Acad. Sci. USA 102(33), 11876-11881 (2005).
70. Qiu Z, Hingley ST, Simmons G et al. Endosomal proteolysis by cathepsins is necessary for murine coronavirus mouse hepatitis virus type 2 spike-mediated entry. J. Virol. 80 (12), 5768-5776 (2006).
71. Hofmann H, Simmons G, Rennekamp AJ et al. Highly conserved regions within the spike proteins of human coronaviruses 229E and NL63 determine recognition of their respective cellular receptors. J. Virol. 80(17), 8639-8652 (2006).
72. Kawase M, Shirato K, Matsuyama S, Taguchi F. Protease-mediated entry via the endosome of human coronavirus 229E. J. Virol. 83(2), 712-721 (2009).
73. Glowacka I, Bertram S, Müller MA et al. Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J. Virol. 85(9), 4122-4134 (2011).
74. Matsuyama S, Nagata N, Shirato K, Kawase M, Takeda M, Taguchi F. Effcient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J. Virol. 84(24), 12658-12664 (2010).
75. Shulla A, Heald-Sargent T, Subramanya G, Zhao J, Perlman S, Gallagher T. A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry. J. Virol. 85(2), 873-882 (2011).
76. Bertram S, Glowacka I, Müller MA et al. Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease. J. Virol. 85(24), 13363-13372 (2011).
77. Simmons G, Bertram S, Glowacka I et al. Different host cell proteases activate the SARS-coronavirus spike-protein for cell-cell and virus-cell fusion. Virology 413 (2), 265-274 (2011).
78. Diederich S, Thiel L, Maisner A. Role of endocytosis and cathepsin-mediated activation in Nipah virus entry. Virology 375(2), 391-400 (2008).
79. Pager CT, Craft WW Jr, Patch J, Dutch RE. A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346(2), 251-257 (2006).
80. Pager CT, Dutch RE. Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J. Virol 79(20), 12714-12720 (2005).
81. Shah PP, Wang T, Kaletsky RL et al. A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and Ebola pseudotype virus infection into human embryonic kidney 293T cells. Mol Pharmacol. 78(2), 319-324 (2010).
82. Gnirss K, Kühl A, Karsten C et al. Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for effcient entry into cell lines and macrophages independent of TMPRSS2 expression. Virology 424(1), 3-10 (2012).
83. Goetz DH, Choe Y, Hansell E et al. Substrate specifcity profling and identifcation of a new class of inhibitor for the major protease of the SARS coronavirus. Biochemistry 46(30), 8744-8752 (2007).
84. Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat. Rev. Microbiol. 9(5), 369-381 (2011).
85. Vaney MC, Rey FA. Class II enveloped viruses. Cell. Microbiol. 13(10), 1451-1459 (2011).
86. Colman PM, Lawrence MC. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell Biol. 4(4), 309-319 (2003).
87. Melikyan GB. Membrane fusion mediated by human immunodefciency virus envelope glycoprotein. Curr. Top. Membr. 68, 81-106 (2011).
88. Kielian M, Rey FA. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 4(1), 67-76 (2006).
89. Lee GM, Craik CS. Trapping moving targets with small molecules. Science 324(5924), 213-215 (2009).
90. Doms RW Viral entry denied. N Engl J. Med. 351(8), 743-744 (2004).
91. Miller EH, Harrison JS, Radoshitzky SR et al. Inhibition of Ebola virus entry by a C-peptide targeted to endosomes. J. Biol. Chem. 286(18), 15854-15861 (2011).
92. Bosch BJ, Martina BE, Van Der Zee R et al. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad rep eat-derived peptides. Proc. Natl Acad. Sci. USA 101(22), 8455-8460 (2004).
93. Porotto M, Yokoyama CC, Palermo LM et al. Viral entry inhibitors targeted to the membrane site of action. J. Virol. 84(13), 6760-6768 (2010).
94. Lee KK, Pessi A, Gui L et al. Capturing a fusion intermediate of infuenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for infuenza virus. J. Biol. Chem. 286(49), 42141-42149 (2011).
95. Basu A, Li B, Mills DM et al. Identifcation of a small-molecule entry inhibitor for floviruses. J. Virol. 85(7), 3106-3119 (2011).
96. Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454(7201), 177-182 (2008).
97. Yermolina MV, Wang J, Caffrey M, Rong LL, Wardrop DJ. Discovery, synthesis, and biological evaluation of a novel group of selective inhibitors of floviral entry. J. Med. Chem. 54(3), 765-781 (2011).
98. Radoshitzky SR, Abraham J, Spiropoulou CF et al. Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses. Nature 446(7131), 92-96 (2007).
99. Larson RA, Dai D, Hosack VT et al. Identifcation of a broad-spectrum arenavirus entry inhibitor. J. Virol. 82(21), 10768-10775 (2008).
100. York J, Dai D, Amberg SM, Nunberg JH. pH-induced activation of arenavirus membrane fusion is antagonized by small-molecule inhibitors. J. Virol. 82(21), 10932-10939 (2008).
101. Thomas CJ, Casquilho-Gray HE, York J et al. A specifc interaction of small molecule entry inhibitors with the envelope glycoprotein complex of the Junín hemorrhagic fever arenavirus. J. Biol. Chem. 286(8), 6192-6200 (2011).
102. Nunberg JH, York J. The curious case of arenavirus entry, and its inhibition. Viruses 4(1), 83-101 (2012).
103. Zaitseva E, Yang ST, Melikov K, Pourmal S, Chernomordik LV Dengue virus ensures its fusion in late endosomes using compartment-specifc lipids. PLoS Pathog 6(10), e1001131 (2010).
104. Roth SL, Whittaker GR. Promotion of vesicular stomatitis virus fusion by the endosome-specifc phospholipid bis (monoacylglycero) phosphate (BMP). FEB S Lett. 585(6), 865-869 (2011).
105. Wolf MC, Freiberg AN, Zhang T et al. A broad-spectrum antiviral targeting entry of enveloped viruses. Proc. Natl Acad. Sci. USA 107(7), 3157-3162 (2010).
106. Glushkov RG. Arbidol. Drugs of the Future 17, 1079-1081 (1992).
107. Boriskin YS, Leneva IA, Pécheur EI, Polyak SJ. Arbidol: a broad-spectrum antiviral compound that blocks viral fusion. Curr. Med. Chem. 15(10), 997-1005 (2008).
108. Brooks MJ, Burtseva EI, Ellery PJ et al. Antiviral activity of arbidol, a broad-spectrum drug for use against respiratory viruses, varies according to test conditions. J. Med. Virol. 84(1), 170-181 (2012).
109. Pécheur EI, Lavillette D, Alcaras F et al Biochemical mechanism of hepatitis C virus inhibition by the broad-spectrum antiviral arbidol. Biochemistry 46(20), 6050-6059 (2007).
110. Glushkov RG, Gus'kova TA, Krylova LIu, Nikolaeva IS. [Mechanisms of arbidole's immunomodulating action]. Vestn. Akad. Med. Nauk SSSR 1999(3), 36-40 (1999).
111. Leneva IA, Russell RJ, Boriskin YS, Hay AJ. Characteristics of arbidol-resistant mutants of infuenza virus: implications for the mechanism of anti-infuenza action of arbidol. Antiviral Res. 81(2), 132-140 (2009).
112. Teissier E, Zandomeneghi G, Loquet A et al. Mechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidol. PLoS ONE 6(1), e15874 (2011).
113. Altman S, Bassler BL, Beckwith J et al An open letter to Elias Zerhouni. Science 307(5714), 1409-1410 (2005).