|
|
Human monoclonal antibodies as candidate therapeutics against emerging viruses |
Yujia Jin1, Cheng Lei1, Dan Hu1, Dimiter S. Dimitrov2(), Tianlei Ying1() |
1. Key Laboratory of Medical Molecular Virology of the Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China 2. Protein Interactions Section, Cancer and Inflammation Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA |
|
|
Abstract The emergence of new pathogens, such as severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), and Ebola virus, poses serious challenges to global public health and highlights the urgent need for novel antiviral approaches. Monoclonal antibodies (mAbs) have been successfully used to treat various diseases, particularly cancer and immunological disorders. Antigen-specific mAbs have been isolated using several different approaches, including hybridoma, transgenic mice, phage display, yeast display, and single B-cell isolation. Consequently, an increasing number of mAbs, which exhibit high potency against emerging viruses in vitro and in animal models of infection, have been developed. In this paper, we summarize historical trends and recent developments in mAb discovery, compare the advantages and disadvantages of various approaches to mAb production, and discuss the potential use of such strategies for the development of antivirals against emerging diseases. We also review the application of recently developed human mAbs against SARS-CoV, MERS-CoV, and Ebola virus and discuss prospects for the development of mAbs as therapeutic agents against emerging viral diseases.
|
Keywords
human monoclonal antibodies
emerging infectious diseases
SARS-CoV
MERS-CoV
Ebola virus
|
Corresponding Author(s):
Dimiter S. Dimitrov,Tianlei Ying
|
Just Accepted Date: 30 October 2017
Online First Date: 21 November 2017
Issue Date: 04 December 2017
|
|
1 |
Drosten C, Günther S, Preiser W, van der Werf S, Brodt HR, Becker S, Rabenau H, Panning M, Kolesnikova L, Fouchier RA, Berger A, Burguière AM, Cinatl J, Eickmann M, Escriou N, Grywna K, Kramme S, Manuguerra JC, Müller S, Rickerts V, Stürmer M, Vieth S, Klenk HD, Osterhaus AD, Schmitz H, Doerr HW. Identification of a novel coronavirus in patients with severe acute respiratory syndrome. N Engl J Med 2003; 348(20): 1967–1976
https://doi.org/10.1056/NEJMoa030747
pmid: 12690091
|
2 |
Ksiazek TG, Erdman D, Goldsmith CS, Zaki SR, Peret T, Emery S, Tong S, Urbani C, Comer JA, Lim W, Rollin PE, Dowell SF, Ling AE, Humphrey CD, Shieh WJ, Guarner J, Paddock CD, Rota P, Fields B, DeRisi J, Yang JY, Cox N, Hughes JM, LeDuc JW, Bellini WJ, Anderson LJ; SARS Working Group. A novel coronavirus associated with severe acute respiratory syndrome. N Engl J Med 2003; 348(20): 1953–1966
https://doi.org/10.1056/NEJMoa030781
pmid: 12690092
|
3 |
Peiris JS, Lai ST, Poon LL, Guan Y, Yam LY, Lim W, Nicholls J, Yee WK, Yan WW, Cheung MT, Cheng VC, Chan KH, Tsang DN, Yung RW, Ng TK, Yuen KY; SARS study group. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 2003; 361(9366): 1319–1325
https://doi.org/10.1016/S0140-6736(03)13077-2
pmid: 12711465
|
4 |
Fouchier RA, Kuiken T, Schutten M, van Amerongen G, van Doornum GJ, van den Hoogen BG, Peiris M, Lim W, Stöhr K, Osterhaus AD. Aetiology: Koch’s postulates fulfilled for SARS virus. Nature 2003; 423(6937): 240
https://doi.org/10.1038/423240a
pmid: 12748632
|
5 |
Kuiken T, Fouchier RA, Schutten M, Rimmelzwaan GF, van Amerongen G, van Riel D, Laman JD, de Jong T, van Doornum G, Lim W, Ling AE, Chan PK, Tam JS, Zambon MC, Gopal R, Drosten C, van der Werf S, Escriou N, Manuguerra JC, Stöhr K, Peiris JS, Osterhaus AD. Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome. Lancet 2003; 362(9380): 263–270
https://doi.org/10.1016/S0140-6736(03)13967-0
pmid: 12892955
|
6 |
World Health Organization. WHO SARS Risk Assessment and Preparedness Framework. See www.who.int/entity/csr/resources/publications/CDS_CSR_ARO_2004_2.pdf. 2014
|
7 |
Feldmann H, Geisbert TW. Ebola haemorrhagic fever. Lancet 2011; 377(9768): 849–862
https://doi.org/10.1016/S0140-6736(10)60667-8
pmid: 21084112
|
8 |
World Health Organization. Ebola Situation Report — 30 March 2016. See . 2016
|
9 |
Lyon GM, Mehta AK, Varkey JB, Brantly K, Plyler L, McElroy AK, Kraft CS, Towner JS, Spiropoulou C, Ströher U, Uyeki TM, Ribner BS; Emory Serious Communicable Diseases Unit. Clinical care of two patients with Ebola virus disease in the United States. N Engl J Med 2014; 371(25): 2402–2409
https://doi.org/10.1056/NEJMoa1409838
pmid: 25390460
|
10 |
Winau F, Winau R. Emil von Behring and serum therapy. Microbes Infect 2002; 4(2): 185–188
https://doi.org/10.1016/S1286-4579(01)01526-X
pmid: 11880051
|
11 |
Berry JD, Gaudet RG. Antibodies in infectious diseases: polyclonals, monoclonals and niche biotechnology. N Biotechnol 2011; 28(5): 489–501
https://doi.org/10.1016/j.nbt.2011.03.018
pmid: 21473942
|
12 |
Casadevall A. Passive antibody therapies: progress and continuing challenges. Clin Immunol 1999; 93(1): 5–15
https://doi.org/10.1006/clim.1999.4768
pmid: 10497006
|
13 |
Dimitrov DS, Marks JD. Therapeutic antibodies: current state and future trends— is a paradigm change coming soon? Methods Mol Biol 2009; 525: 1–27, xiii
https://doi.org/10.1007/978-1-59745-554-1_1
pmid: 19252861
|
14 |
Zhu Z, Dimitrov AS, Chakraborti S, Dimitrova D, Xiao X, Broder CC, Dimitrov DS. Development of human monoclonal antibodies against diseases caused by emerging and biodefense-related viruses. Expert Rev Anti Infect Ther 2006; 4(1): 57–66
https://doi.org/10.1586/14787210.4.1.57
pmid: 16441209
|
15 |
Shulman M, Wilde CD, Köhler G. A better cell line for making hybridomas secreting specific antibodies. Nature 1978; 276(5685): 269–270
https://doi.org/10.1038/276269a0
pmid: 714156
|
16 |
Smith GP. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 1985; 228(4705): 1315–1317
https://doi.org/10.1126/science.4001944
pmid: 4001944
|
17 |
Smith GP, Petrenko VA. Phage Display. Chem Rev 1997; 97(2): 391–410
https://doi.org/10.1021/cr960065d
pmid: 11848876
|
18 |
Gao C, Mao S, Kaufmann G, Wirsching P, Lerner RA, Janda KD. A method for the generation of combinatorial antibody libraries using pIX phage display. Proc Natl Acad Sci USA 2002; 99(20): 12612–12616
https://doi.org/10.1073/pnas.192467999
pmid: 12239343
|
19 |
McCafferty J, Fitzgerald KJ, Earnshaw J, Chiswell DJ, Link J, Smith R, Kenten J. Selection and rapid purification of murine antibody fragments that bind a transition-state analog by phage display. Appl Biochem Biotechnol 1994; 47(2-3): 157–173
https://doi.org/10.1007/BF02787932
pmid: 7944335
|
20 |
Davies EL, Smith JS, Birkett CR, Manser JM, Anderson-Dear DV, Young JR. Selection of specific phage-display antibodies using libraries derived from chicken immunoglobulin genes. J Immunol Methods 1995; 186(1): 125–135
https://doi.org/10.1016/0022-1759(95)00143-X
pmid: 7561141
|
21 |
Sok D, Briney B, Jardine JG, Kulp DW, Menis S, Pauthner M, Wood A, Lee EC, Le KM, Jones M, Ramos A, Kalyuzhniy O, Adachi Y, Kubitz M, MacPherson S, Bradley A, Friedrich GA, Schief WR, Burton DR. Priming HIV-1 broadly neutralizing antibody precursors in human Ig loci transgenic mice. Science 2016; 353(6307): 1557–1560
https://doi.org/10.1126/science.aah3945
pmid: 27608668
|
22 |
Murphy AJ, Macdonald LE, Stevens S, Karow M, Dore AT, Pobursky K, Huang TT, Poueymirou WT, Esau L, Meola M, Mikulka W, Krueger P, Fairhurst J, Valenzuela DM, Papadopoulos N, Yancopoulos GD. Mice with megabase humanization of their immunoglobulin genes generate antibodies as efficiently as normal mice. Proc Natl Acad Sci USA 2014; 111(14): 5153–5158
https://doi.org/10.1073/pnas.1324022111
pmid: 24706856
|
23 |
Lipke PN, Kurjan J. Sexual agglutination in budding yeasts: structure, function, and regulation of adhesion glycoproteins. Microbiol Rev 1992; 56(1): 180–194
pmid: 1579109
|
24 |
Boder ET, Wittrup KD. Yeast surface display for directed evolution of protein expression, affinity, and stability. Methods Enzymol 2000; 328: 430–444
https://doi.org/10.1016/S0076-6879(00)28410-3
pmid: 11075358
|
25 |
Boder ET, Wittrup KD. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 1997; 15(6): 553–557
https://doi.org/10.1038/nbt0697-553
pmid: 9181578
|
26 |
Kieke MC, Cho BK, Boder ET, Kranz DM, Wittrup KD. Isolation of anti-T cell receptor scFv mutants by yeast surface display. Protein Eng 1997; 10(11): 1303–1310
https://doi.org/10.1093/protein/10.11.1303
pmid: 9514119
|
27 |
Wardemann H, Yurasov S, Schaefer A, Young JW, Meffre E, Nussenzweig MC. Predominant autoantibody production by early human B cell precursors. Science 2003; 301(5638): 1374–1377
https://doi.org/10.1126/science.1086907
pmid: 12920303
|
28 |
Walker LM, Phogat SK, Chan-Hui PY, Wagner D, Phung P, Goss JL, Wrin T, Simek MD, Fling S, Mitcham JL, Lehrman JK, Priddy FH, Olsen OA, Frey SM, Hammond PW; Protocol G Principal Investigators, Kaminsky S, Zamb T, Moyle M, Koff WC, Poignard P, Burton DR. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009; 326(5950): 285–289
https://doi.org/10.1126/science.1178746
pmid: 19729618
|
29 |
Walker LM, Huber M, Doores KJ, Falkowska E, Pejchal R, Julien JP, Wang SK, Ramos A, Chan-Hui PY, Moyle M, Mitcham JL, Hammond PW, Olsen OA, Phung P, Fling S, Wong CH, Phogat S, Wrin T, Simek MD; Protocol G Principal Investigators, Koff WC, Wilson IA, Burton DR, Poignard P. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011; 477(7365): 466–470
https://doi.org/10.1038/nature10373
pmid: 21849977
|
30 |
Traggiai E, Becker S, Subbarao K, Kolesnikova L, Uematsu Y, Gismondo MR, Murphy BR, Rappuoli R, Lanzavecchia A. An efficient method to make human monoclonal antibodies from memory B cells: potent neutralization of SARS coronavirus. Nat Med 2004; 10(8): 871–875
https://doi.org/10.1038/nm1080
pmid: 15247913
|
31 |
Aman P, Ehlin-Henriksson B, Klein G. Epstein-Barr virus susceptibility of normal human B lymphocyte populations. J Exp Med 1984; 159(1): 208–220
https://doi.org/10.1084/jem.159.1.208
pmid: 6319530
|
32 |
Brès P. The epidemic of Ebola haemorrhagic fever in Sudan and Zaire, 1976: introductory note. Bull World Health Organ 1978; 56(2): 245
|
33 |
Li H, Ying T, Yu F, Lu L, Jiang S. Development of therapeutics for treatment of Ebola virus infection. Microbes Infect 2015; 17(2): 109–117
https://doi.org/10.1016/j.micinf.2014.11.012
pmid: 25498866
|
34 |
Ka D, Fall G, Diallo VC, Faye O, Fortes LD, Faye O, Bah EI, Diallo KM, Balique F, Ndour CT, Seydi M, Sall AA. Ebola virus imported from Guinea to Senegal, 2014. Emerg Infect Dis 2017; 23(6): 1026–1028
https://doi.org/10.3201/eid2306.161092
pmid: 28518019
|
35 |
Li YH, Chen SP. Evolutionary history of Ebola virus. Epidemiol Infect 2014; 142(6): 1138–1145
https://doi.org/10.1017/S0950268813002215
pmid: 24040779
|
36 |
Huang Y, Xu L, Sun Y, Nabel GJ. The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein. Mol Cell 2002; 10(2): 307–316
https://doi.org/10.1016/S1097-2765(02)00588-9
pmid: 12191476
|
37 |
Geisbert TW, Jahrling PB. Differentiation of filoviruses by electron microscopy. Virus Res 1995; 39(2-3): 129–150
https://doi.org/10.1016/0168-1702(95)00080-1
pmid: 8837880
|
38 |
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 2008; 454(7201): 177–182
https://doi.org/10.1038/nature07082
pmid: 18615077
|
39 |
Hood CL, Abraham J, Boyington JC, Leung K, Kwong PD, Nabel GJ. Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity. J Virol 2010; 84(6): 2972–2982
https://doi.org/10.1128/JVI.02151-09
pmid: 20053739
|
40 |
Richardson JS, Yao MK, Tran KN, Croyle MA, Strong JE, Feldmann H, Kobinger GP. Enhanced protection against Ebola virus mediated by an improved adenovirus-based vaccine. PLoS One 2009; 4(4): e5308
https://doi.org/10.1371/journal.pone.0005308
pmid: 19390586
|
41 |
Jones SM, Feldmann H, Ströher U, Geisbert JB, Fernando L, Grolla A, Klenk HD, Sullivan NJ, Volchkov VE, Fritz EA, Daddario KM, Hensley LE, Jahrling PB, Geisbert TW. Live attenuated recombinant vaccine protects nonhuman primates against Ebola and Marburg viruses. Nat Med 2005; 11(7): 786–790
https://doi.org/10.1038/nm1258
pmid: 15937495
|
42 |
Warfield KL, Swenson DL, Olinger GG, Kalina WV, Aman MJ, Bavari S. Ebola virus-like particle-based vaccine protects nonhuman primates against lethal Ebola virus challenge. J Infect Dis 2007; 196(Supplement_2): S430–S437
|
43 |
Dowling W, Thompson E, Badger C, Mellquist JL, Garrison AR, Smith JM, Paragas J, Hogan RJ, Schmaljohn C. Influences of glycosylation on antigenicity, immunogenicity, and protective efficacy of Ebola virus GP DNA vaccines. J Virol 2007; 81(4): 1821–1837
https://doi.org/10.1128/JVI.02098-06
pmid: 17151111
|
44 |
Qiu X, Fernando L, Alimonti JB, Melito PL, Feldmann F, Dick D, Ströher U, Feldmann H, Jones SM. Mucosal immunization of cynomolgus macaques with the VSVDeltaG/ZEBOVGP vaccine stimulates strong ebola GP-specific immune responses. PLoS One 2009; 4(5): e5547
https://doi.org/10.1371/journal.pone.0005547
pmid: 19440245
|
45 |
Qiu X, Audet J, Wong G, Pillet S, Bello A, Cabral T, Strong JE, Plummer F, Corbett CR, Alimonti JB. Successful treatment of Ebola virus–infected cynomolgus macaques with monoclonal antibodies. Sci Transl Med 2012; 4(138): 138ra81
|
46 |
Olinger GG Jr, Pettitt J, Kim D, Working C, Bohorov O, Bratcher B, Hiatt E, Hume SD, Johnson AK, Morton J, Pauly M, Whaley KJ, Lear CM, Biggins JE, Scully C, Hensley L, Zeitlin L. Delayed treatment of Ebola virus infection with plant-derived monoclonal antibodies provides protection in rhesus macaques. Proc Natl Acad Sci USA 2012; 109(44): 18030–18035
https://doi.org/10.1073/pnas.1213709109
pmid: 23071322
|
47 |
Kugelman JR, Kugelman-Tonos J, Ladner JT, Pettit J, Keeton CM, Nagle ER, Garcia KY, Froude JW, Kuehne AI, Kuhn JH, Bavari S, Zeitlin L, Dye JM, Olinger GG, Sanchez-Lockhart M, Palacios GF. Emergence of Ebola virus escape variants in infected nonhuman primates treated with the MB-003 antibody cocktail. Cell Reports 2015; 12(12): 2111–2120
https://doi.org/10.1016/j.celrep.2015.08.038
pmid: 26365189
|
48 |
Qiu X, Wong G, Audet J, Bello A, Fernando L, Alimonti JB, Fausther-Bovendo H, Wei H, Aviles J, Hiatt E, Johnson A, Morton J, Swope K, Bohorov O, Bohorova N, Goodman C, Kim D, Pauly MH, Velasco J, Pettitt J, Olinger GG, Whaley K, Xu B, Strong JE, Zeitlin L, Kobinger GP. Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp. Nature 2014; 514(7520): 47–53
pmid: 25171469
|
49 |
Corti D, Misasi J, Mulangu S, Stanley DA, Kanekiyo M, Wollen S, Ploquin A, Doria-Rose NA, Staupe RP, Bailey M, Shi W, Choe M, Marcus H, Thompson EA, Cagigi A, Silacci C, Fernandez-Rodriguez B, Perez L, Sallusto F, Vanzetta F, Agatic G, Cameroni E, Kisalu N, Gordon I, Ledgerwood JE, Mascola JR, Graham BS, Muyembe-Tamfun JJ, Trefry JC, Lanzavecchia A, Sullivan NJ. Protective monotherapy against lethal Ebola virus infection by a potently neutralizing antibody. Science 2016; 351(6279): 1339–1342
https://doi.org/10.1126/science.aad5224
pmid: 26917593
|
50 |
Misasi J, Gilman MS, Kanekiyo M, Gui M, Cagigi A, Mulangu S, Corti D, Ledgerwood JE, Lanzavecchia A, Cunningham J, Muyembe-Tamfun JJ, Baxa U, Graham BS, Xiang Y, Sullivan NJ, McLellan JS. Structural and molecular basis for Ebola virus neutralization by protective human antibodies. Science 2016; 351(6279): 1343–1346
https://doi.org/10.1126/science.aad6117
pmid: 26917592
|
51 |
Dowall SD, Callan J, Zeltina A, Al-Abdulla I, Strecker T, Fehling SK, Krähling V, Bosworth A, Rayner E, Taylor I, Charlton S, Landon J, Cameron I, Hewson R, Nasidi A, Bowden TA, Carroll MW. Development of a cost-effective ovine polyclonal antibody-based product, EBOTAb, to treat Ebola virus infection. J Infect Dis 2016; 213(7): 1124–1133
https://doi.org/10.1093/infdis/jiv565
pmid: 26715676
|
52 |
Li W, Moore MJ, Vasilieva N, Sui J, Wong SK, Berne MA, Somasundaran M, Sullivan JL, Luzuriaga K, Greenough TC, Choe H, Farzan M. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 2003; 426(6965): 450–454
https://doi.org/10.1038/nature02145
pmid: 14647384
|
53 |
Poutanen SM, Low DE, Henry B, Finkelstein S, Rose D, Green K, Tellier R, Draker R, Adachi D, Ayers M, Chan AK, Skowronski DM, Salit I, Simor AE, Slutsky AS, Doyle PW, Krajden M, Petric M, Brunham RC, McGeer AJ; National Microbiology Laboratory, Canada; Canadian Severe Acute Respiratory Syndrome Study Team. Identification of severe acute respiratory syndrome in Canada. N Engl J Med 2003; 348(20): 1995–2005
https://doi.org/10.1056/NEJMoa030634
pmid: 12671061
|
54 |
Qin E, Zhu Q, Yu M, Fan B, Chang G, Si B, Yang B, Peng W, Jiang T, Liu B, Deng Y, Liu H, Zhang Y, Wang C, Li Y, Gan Y, Li X, Lü F, Tan G, Cao W, Yang R, Wang J, Li W, Xu Z, Li Y, Wu Q, Lin W, Chen W, Tang L, Deng Y, Han Y, Li C, Lei M, Li G, Li W, Lü H, Shi J, Tong Z, Zhang F, Li S, Liu B, Liu S, Dong W, Wang J, Wong GKS, Yu J, Yang H. A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01). Chin Sci Bull 2003; 48(10): 941–948
https://doi.org/10.1007/BF03184203
|
55 |
Gallagher TM, Buchmeier MJ. Coronavirus spike proteins in viral entry and pathogenesis. Virology 2001; 279(2): 371–374
https://doi.org/10.1006/viro.2000.0757
pmid: 11162792
|
56 |
Moore KM, Jackwood MW, Hilt DA. Identification of amino acids involved in a serotype and neutralization specific epitope within the s1 subunit of avian infectious bronchitis virus. Arch Virol 1997; 142(11): 2249–2256
https://doi.org/10.1007/s007050050239
pmid: 9672590
|
57 |
Sui J, Li W, Murakami A, Tamin A, Matthews LJ, Wong SK, Moore MJ, Tallarico ASC, Olurinde M, Choe H, Anderson LJ, Bellini WJ, Farzan M, Marasco WA. Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association. Proc Natl Acad Sci USA 2004; 101(8): 2536–2541
https://doi.org/10.1073/pnas.0307140101
pmid: 14983044
|
58 |
Sui J, Li W, Roberts A, Matthews LJ, Murakami A, Vogel L, Wong SK, Subbarao K, Farzan M, Marasco WA. Evaluation of human monoclonal antibody 80R for immunoprophylaxis of severe acute respiratory syndrome by an animal study, epitope mapping, and analysis of spike variants. J Virol 2005; 79(10): 5900–5906
https://doi.org/10.1128/JVI.79.10.5900-5906.2005
pmid: 15857975
|
59 |
Yang ZY, Werner HC, Kong WP, Leung K, Traggiai E, Lanzavecchia A, Nabel GJ. Evasion of antibody neutralization in emerging severe acute respiratory syndrome coronaviruses. Proc Natl Acad Sci USA 2005; 102(3): 797–801
https://doi.org/10.1073/pnas.0409065102
pmid: 15642942
|
60 |
Zhu Z, Chakraborti S, He Y, Roberts A, Sheahan T, Xiao X, Hensley LE, Prabakaran P, Rockx B, Sidorov IA, Corti D, Vogel L, Feng Y, Kim JO, Wang LF, Baric R, Lanzavecchia A, Curtis KM, Nabel GJ, Subbarao K, Jiang S, Dimitrov DS. Potent cross-reactive neutralization of SARS coronavirus isolates by human monoclonal antibodies. Proc Natl Acad Sci USA 2007; 104(29): 12123–12128
https://doi.org/10.1073/pnas.0701000104
pmid: 17620608
|
61 |
van Boheemen S, de Graaf M, Lauber C, Bestebroer TM, Raj VS, Zaki AM, Osterhaus AD, Haagmans BL, Gorbalenya AE, Snijder EJ, Fouchier RA. Genomic characterization of a newly discovered coronavirus associated with acute respiratory distress syndrome in humans. MBio 2012; 3(6): e00473–e12
https://doi.org/10.1128/mBio.00473-12
pmid: 23170002
|
62 |
Al-Tawfiq JA, Memish ZA. Middle East respiratory syndrome coronavirus: epidemiology and disease control measures. Infect Drug Resist 2014; 7: 281–287
|
63 |
Butler D. Receptor for new coronavirus found. Nature 2013; 495(7440): 149–150
https://doi.org/10.1038/495149a
pmid: 23486032
|
64 |
Peiris JS, Guan Y, Yuen KY. Severe acute respiratory syndrome. Nat Med 2004; 10(12 Suppl): S88–S97
https://doi.org/10.1038/nm1143
pmid: 15577937
|
65 |
Al-Tawfiq JA, Memish ZA. An update on Middle East respiratory syndrome: 2 years later. Expert Rev Respir Med 2015; 9(3): 327–335
https://doi.org/10.1586/17476348.2015.1027689
pmid: 25790840
|
66 |
Lu G, Hu Y, Wang Q, Qi J, Gao F, Li Y, Zhang Y, Zhang W, Yuan Y, Bao J, Zhang B, Shi Y, Yan J, Gao GF. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature 2013; 500(7461): 227–231
https://doi.org/10.1038/nature12328
pmid: 23831647
|
67 |
Gorrell MD, Gysbers V, McCaughan GW. CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand J Immunol 2001; 54(3): 249–264
https://doi.org/10.1046/j.1365-3083.2001.00984.x
pmid: 11555388
|
68 |
Yang Y, Du L, Liu C, Wang L, Ma C, Tang J, Baric RS, Jiang S, Li F. Receptor usage and cell entry of bat coronavirus HKU4 provide insight into bat-to-human transmission of MERS coronavirus. Proc Natl Acad Sci USA 2014; 111(34): 12516–12521
https://doi.org/10.1073/pnas.1405889111
pmid: 25114257
|
69 |
Ying T, Du L, Ju TW, Prabakaran P, Lau CC, Lu L, Liu Q, Wang L, Feng Y, Wang Y, Zheng BJ, Yuen KY, Jiang S, Dimitrov DS. Exceptionally potent neutralization of Middle East respiratory syndrome coronavirus by human monoclonal antibodies. J Virol 2014; 88(14): 7796–7805
https://doi.org/10.1128/JVI.00912-14
pmid: 24789777
|
70 |
Jiang L, Wang N, Zuo T, Shi X, Poon KM, Wu Y, Gao F, Li D, Wang R, Guo J, Fu L, Yuen KY, Zheng BJ, Wang X, Zhang L. Potent neutralization of MERS-CoV by human neutralizing monoclonal antibodies to the viral spike glycoprotein. Sci Transl Med 2014; 6(234): 234ra59
https://doi.org/10.1126/scitranslmed.3008140
pmid: 24778414
|
71 |
Tang XC, Agnihothram SS, Jiao Y, Stanhope J, Graham RL, Peterson EC, Avnir Y, Tallarico AS, Sheehan J, Zhu Q, Baric RS, Marasco WA. Identification of human neutralizing antibodies against MERS-CoV and their role in virus adaptive evolution. Proc Natl Acad Sci USA 2014; 111(19): E2018–E2026
https://doi.org/10.1073/pnas.1402074111
pmid: 24778221
|
72 |
Ying T, Prabakaran P, Du L, Shi W, Feng Y, Wang Y, Wang L, Li W, Jiang S, Dimitrov DS, Zhou T. Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. Nat Commun 2015; 6: 8223
https://doi.org/10.1038/ncomms9223
pmid: 26370782
|
73 |
Corti D, Passini N, Lanzavecchia A, Zambon M. Rapid generation of a human monoclonal antibody to combat Middle East respiratory syndrome. J Infect Public Health 2016; 9(3): 231–235
https://doi.org/10.1016/j.jiph.2016.04.003
pmid: 27102927
|
74 |
Pascal KE, Coleman CM, Mujica AO, Kamat V, Badithe A, Fairhurst J, Hunt C, Strein J, Berrebi A, Sisk JM, Matthews KL, Babb R, Chen G, Lai KM, Huang TT, Olson W, Yancopoulos GD, Stahl N, Frieman MB, Kyratsous CA. Pre- and postexposure efficacy of fully human antibodies against Spike protein in a novel humanized mouse model of MERS-CoV infection. Proc Natl Acad Sci USA 2015; 112(28): 8738–8743
https://doi.org/10.1073/pnas.1510830112
pmid: 26124093
|
75 |
Bossart KN, Geisbert TW, Feldmann H, Zhu Z, Feldmann F, Geisbert JB, Yan L, Feng YR, Brining D, Scott D, Wang Y, Dimitrov AS, Callison J, Chan YP, Hickey AC, Dimitrov DS, Broder CC, Rockx B. A neutralizing human monoclonal antibody protects african green monkeys from hendra virus challenge. Sci Transl Med 2011; 3(105): 105ra103
https://doi.org/10.1126/scitranslmed.3002901
pmid: 22013123
|
76 |
Geisbert TW, Mire CE, Geisbert JB, Chan YP, Agans KN, Feldmann F, Fenton KA, Zhu Z, Dimitrov DS, Scott DP, Bossart KN, Feldmann H, Broder CC. Therapeutic treatment of Nipah virus infection in nonhuman primates with a neutralizing human monoclonal antibody. Sci Transl Med 2014; 6(242): 242ra82
https://doi.org/10.1126/scitranslmed.3008929
pmid: 24964990
|
77 |
Roopenian DC, Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 2007; 7(9): 715–725
https://doi.org/10.1038/nri2155
pmid: 17703228
|
78 |
Wang L, Ying T. New directions for half-life extension of protein therapeutics: the rise of antibody Fc domains and fragments. Curr Pharm Biotechnol 2016; 17(15): 1348–1352
https://doi.org/10.2174/1389201017666160823144032
pmid: 27552847
|
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
|
Shared |
|
|
|
|
|
Discussed |
|
|
|
|