序章 緒論
1. Barre-Sinoussi, F., Chermann, J. C., Rey, F., Nugeyre, M. T., Chamaret, S., Gruest, J., Dauguet, C., Axler-Blin, C., Vezinet-Brun, F., Rouzioux, C., Rozenbaum, W., Montagnier, L: Isolation of a T- lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science 1984; 220 (4599): 868-71.
2. Gallo, R. C., Salahuddin, S. Z., Popovic, M., Shearer, G. M., Kaplan, M., Haynes, B. F., Palker, T. J., Redfield, R., Oleske, J., Safai, B., et al.,: Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS. Science 1984;224(4648):500-503.
3. Gao, F., Bailes, E., Robertson, D. L., Chen, Y., Rodenburg, C. M., Michael, S. F., Cummins, L. B., Arthur, L. O., Peeters, M., Shaw, G. M., Sharp, P. M., Hahn, B. H.: Origin of HIV-1 in the chimpanzee Pan troglodytes troglodytes. Nature 1999; 397(6718):436-41.
4. Zhu, P., Liu, J., Bess, J., Jr., Chertova, E., Lifson, J. D., Grise, H., Ofek, G. A., Taylor, K. A., Roux, K. H.: Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006;441(7095): 847-52.
5. Zanetti, G., Briggs, J. A., Grunewald, K., Sattentau, Q. J., Fuller, S. D.: Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog 2006;2(8): e83.
6. Niedrig, M., Gelderblom, H. R., Pauli, G., Marz, J., Bickhard, H., Wolf, H., Modrow, S.: Inhibition of infectious human immunodeficiency virus type 1 particle formation by Gag protein-derived peptides. J Gen Virol 1994;75(Pt 6): 1469-74.
7. Briggs, J. A., Grunewald, K., Glass, B., Forster, F., Krausslich, H. G., Fuller, S. D.: The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 2006;14(1): 15-20.
8. German Advisory Committee Blood, Subgroup 'Assessment of Pathogens Transmissible by Blood: Human Immunodeficiency Virus (HIV). Transfus Med Hemother 2016;43(3):203-22.
9. 徳永研三 、古田里佳、川村名子、足立昭夫: ヒト免疫不全ウイルス（HIV）の制御遺伝子の機能. 蛋白質 核酸 酵素; 40 （9）： 1079-1091.（1995）
10. Engelman, A., Cherepanov, P.: The structural biology of HIV-1: mechanistic and therapeutic insights Nat Rev Microbiol 2012;10(4): 279-90.
11. Deeks, S. G., Overbaugh, J., Phillips, A., Buchbinder, S.: HIV infection. Nat Rev Dis Primers 2015;1: 15035.
12. Dean M., Carrington, M., Winkler, C., Huttley, G. A., Smith, M. W., Allikmets, R., Goedert, J. J., Buchbinder, S. P., Vittinghoff, E., Gomperts, E., Donfield, S., Vlahov, D., Kaslow, R., Saah, A., Rinaldo, C., Detels. R., O'Brien, S. J.: Genetic restriction of HIV-1 infection and progression to AIDS by a deletion allele of the CKR5 structural gene. Hemophilia Growth and Development Study, Multicenter AIDS Cohort Study, Multicenter Hemophilia Cohort Study, San Francisco City Cohort, ALIVE Study. Science 1996;273(5283):1856-62.
13. Feng, Y., Broder, C. C., Kennedy, P.E., Berger, E. A.: HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 1996;272(5263): 872-7.
14. Chan, D. C., Fass, D., Berger, J. M., Kim, P. S.: Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997;89(2): 263-73.
15. Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., Wiley, D. C.: Atomic structure of the ectodomain from HIV-1 gp41. Nature 1997;387(6631): 426-30.
16. Buzon, V., Natrajan, G., Schibli, D., Campelo, F., Kozlov, M. M., Weissenhorn, W.: Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog 2010;6(5): e1000880.
17. Sousa, R., Chung, Y. J., Rose, J. P., Wang, B. C.: Crystal structure of bacteriophage T7 RNA polymerase at 3.3 A resolution.: Nature 1993;364(6438): 593-9.
18. Colomer-Lluch, M., Ruiz, A., Moris, A., Prado, J. G.: Restriction Factors: From Intrinsic Viral Restriction to Shaping Cellular Immunity Against HIV-1. Front Immunol 2018;9: 2876.
19. Sheehy, A.M., Gaddis, N.C., Choi, J.D., Malim, M.H.: Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002;418(6898):646–50.
20. Brenchley, J. M., Price, D. A., Douek, D. C.: HIV disease: fallout from a mucosal catastrophe? Nat Immunol 2006;7(3): 235–9.
21. Finkelshtein, D., Werman, A., Novick, D., Barak, S., Rubinstein, M.: LDL receptor and its family members serve as the cellular receptors for vesicular stomatitis virus. Proc Natl Acad Sci U S A 2013;110(18): 7306-11.
22. Amirache, F., Levy, C., Costa, C., Mangeot, P. E., Torbett, B. E., Wang, C. X., Negre, D., Cosset, F. L., Verhoeyen, E.: Mystery solved: VSV-G-LVs do not allow efficient gene transfer into unstimulated T cells, B cells, and HSCs because they lack the LDL receptor. Blood 2014;123(9): 1422-4.
23. Burns, J. M., Jr., Shreffler, W. G., Benson, D. R., Ghalib, H. W., Badaro, R., Reed, S. G.: Molecular characterization of a kinesin-related antigen of Leishmania chagasi that detects specific antibody in African and American visceral leishmaniasis. Proc Natl Acad Sci U S A 1993;90(2): 775-9.
24. Chen, B. K., Saksela, K., Andino, R., Baltimore, D.: Distinct modes of human immunodeficiency virus type 1 proviral latency revealed by superinfection of nonproductively infected cell lines with recombinant luciferase-encoding viruses. J Virol 1994;68(2): 654-60.
25. Aso H., Nagaoka, S., Kawakami, E., Ito, J., Islam, S., Tan, B. J. Y., Nakaoka, S., Ashizaki, K., Shiroguchi, K., Suzuki, Y., Satou, Y., Koyanagi, Y., Sato, K.: Multiomics Investigation Revealing the Characteristics of HIV-1-Infected Cells In Vivo. Cell Rep 2020;32(2): 107887.
26. England, C. G., Ehlerding, E. B., Cai, W.: NanoLuc: A Small Luciferase is Brightening up the Field of Bioluminescence. Bioconjug Chem 2016;27(5): 1175–1187.
第1章 HiBiT ペプチドタグを利用した超迅速HIV-1 定量系の樹立
1. Adachi, A., Gendelman, H. E., Koenig, S., Folks, T., Willey, R., Rabson, A., and Martin, M. A.: Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J Virol 1986;59(2): 284–91.
2. Barré-Sinoussi, F., Chermann, J., Rey, F., Nugeyre, M., Chamaret, S., Gruest, J., Dauguet, C., Axler- Blin, C., Vézinet-Brun, F., Rouzioux, C., Rozenbaum, W., and Montagnier, L. (1983) Isolation of a T- lymphotropic retrovirus froma patient at risk for acquired immune deficiency syndrome (AIDS). Science 1983;220(4599): 868–71.
3. Goudsmit, J., Lange, J. M., Paul, D. A., and Dawson, G. J.: Antigenemia and antibody titers to core and envelope antigens in AIDS, AIDSrelated complex, and subclinical human immunodeficiency virus infection. J. Infect. Dis. 1987;155(3): 558–60.
4. Dixon, A. S., Schwinn, M. K., Hall, M. P., Zimmerman, K., Otto, P., Lubben, T. H., Butler, B. L., Binkowski, B. F., Machleidt, T., Kirkland, T. A.,Wood, M. G., Eggers, C. T., Encell, L. P., andWood, K. V.: NanoLuc complementation reporter optimized for accurate measurement of protein interactions in cells. ACS Chem. Biol. 2016;11(2): 400–8.
5. Tamura, T., Fukuhara, T., Uchida, T., Ono, C., Mori, H., Sato, A., Fauzyah, Y., Okamoto, T., Kurosu, T., Setoh, Y. X., Imamura, M., Tautz, N., Sakoda, Y., Khromykh, A. A., Chayama, K., Matsuura, Y.: Characterization of Recombinant Flaviviridae Viruses Possessing a Small Reporter Tag. J Virol 2018;92(2).
6. Tamura, T., Igarashi, M., Enkhbold, B., Suzuki, T., Okamatsu, M., Ono, C., Mori, H., Izumi, T., Sato, A., Fauzyah, Y., Okamoto, T., Sakoda, Y., Fukuhara, T., Matsuura, Y.: In Vivo Dynamics of Reporter Flaviviridae Viruses. J Virol 2019;93(22).
7. Tada, T., Zhang, Y., Koyama, T., Tobiume, M., Tsunetsugu-Yokota, Y., Yamaoka, S., Fujita, H., Tokunaga, K.: MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins. Nat Med 2015;21(12): 1502–7.
8. Kinomoto, M., Kanno, T., Shimura, M., Ishizaka, Y., Kojima, A., Kurata, T., Sata, T., and Tokunaga, K.: All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition. Nucleic Acids Res. 2007;35(9): 2955–64.
9. Wiznerowicz, M., Trono, D.: Conditional suppression of cellular genes: Lentivirus vector-mediated drug-inducible RNA interference. J Virol 2003; 77(16): 8957–61.
10. Tsunetsugu-Yokota, Y., Akagawa, K., Kimoto, H., Suzuki, K., Iwasaki, M., Yasuda, S., Häusser, G., Hultgren, C., Meyerhans, A., Takemori, T.: Monocyte-derived cultured dendritic cells are susceptible to human immunodeficiency virus infection and transmit virus to resting T cells in the process of nominal antigen presentation. J Virol 1995;69(7), 4544–7.
11. Dang, Y.,Wang, X., Zhou, T., York, I. A., Zheng, Y.H.: Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. J Virol 2009;83(17), 8544–52.
12. Yamashita, T., Kamada, K., Hatcho, K., Adachi, A., Nomaguchi, M.: Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F. Microbes Infect 2008 10(10-11): 1142–9.
13. Russell, R. A., Pathak, V. K.: Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J Virol 2007;81(15): 8201–10.
14. Tian, C., Yu, X., Zhang, W., Wang, T., Xu, R., Yu, X. F.: Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J Virol 2006;80(6): 3112–5.
15. Salamango, D. J., Ikeda, T., Moghadasi, S. A., Wang, J., McCann, J. L., Serebrenik, A. A., Ebrahimi,D., Jarvis, M. C., Brown,W. L., Harris, R. S.: HIV-1 Vif triggers cell cycle arrest by degrading cellular PPP2R5 phospho-regulators. Cell Rep 2019;29(5): 1057–65.
16. Delenda, C., Gaillard, C.: Real-time quantitative PCR for the design of lentiviral vector analytical assays. Gene Ther 2005;12 Suppl. 1: S36–50.
17. Geraerts, M., Willems, S., Baekelandt, V., Debyser, Z., Gijsbers, R.: Comparison of lentiviral vector titration methods. BMC Biotechnol 2006;6: 34.
18. Vermeire, J., Naessens, E., Vanderstraeten, H., Landi, A., Iannucci, V., Van Nuffel, A., Taghon, T., Pizzato, M., Verhasselt, B.: Quantification of reverse transcriptase activity by real-time PCR as a fast and accurate method for titration of HIV, lenti- and retroviral vectors. PLoS One 2012;7(12): e50859.
19. Kirui, J., Freed, E. O.: Generation and validation of a highly sensitive bioluminescent HIV-1 reporter vector that simplifies measurement of virus release. Retrovirology 2020;17(1): 12.
20. Ozono, S., Zhang, Y., Tobiume, M., Kishigami, S., Tokunaga, K.: Super-rapid quantitation of the production of HIV-1 harboring a luminescent peptide tag. J Biol Chem 2020;295(37): 13023-30.
21. hen, J. C.., Krucinski, J., Miercke, L. J. W., Finer-Moore, J. S., Tang, A. H., Leavitt, A. D., Stroud, R. M.: Crystal structure of the HIV- 1 integrase catalytic core and C-terminal domains: A model for viral DNA binding. Proc Natl Acad Sci U S A 2000;97(15): 8233–8.
第2章 HiBiT ペプチドタグを有するレンチウイルスベクター系を用いたCOVID-19研究への応用
1. Wu, F., Zhao, S., Yu, B., Chen, Y. M., Wang, W., Song, Z. G., Hu, Y., Tao, Z. W., Tian, J. H., Pei, Y. Y., Yuan, M. L., Zhang, Y. L., Dai, F. H., Liu, Y., Wang, Q. M., Zheng, J. J., Xu, L., Holmes, E. C., Zhang, Y. Z.: A new coronavirus associated with human respiratory disease in China. Nature 2020;579(7798):265-9.
2. Li, Q., Guan, X., Wu, P., Wang, X., Zhou, L., Tong, Y., Ren, R., Leung, K. S. M., Lau, E. H. Y., Wong, J. Y., Xing, X., Xiang, N., Wu, Y., Li, C., Chen, Q., Li, D., Liu, T., Zhao, J., Liu, M., Tu, W., Chen, C., Jin, L., Yang, R., Wang, Q., Zhou, S., Wang, R., Liu, H., Luo, Y., Liu, Y., Shao, G., Li, H., Tao, Z., Yang, Y., Deng, Z., Liu, B., Ma, Z., Zhang, Y., Shi, G., Lam, T. T. Y., Wu, J. T., Gao, G. F., Cowling, B. J., Yang, B., Leung, G. M., Feng, Z.: Early transmission dynamics in Wuhan, China, of novel coronavirus–infected pneumonia. N Engl J Med 2020;382(13): 1199–1207.
3. Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., Cheng, Z., Yu, T., Xia, J., Wei, Y., Wu, W., Xie, X., Yin, W., Li, H., Liu, M., Xiao, Y., Gao, H., Guo, L., Xie, J., Wang, G., Jiang, R., Gao, Z., Jin, Q., Wang, J., Cao, B.: Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. Lancet 2020;395(10223): 497–506.
4. Zhou, P., Yang, X. L., Wang, X. G., Hu, B., Zhang, L., Zhang, W., Si, H. R., Zhu, Y., Li, B., Huang, C. L., Chen, H. D., Chen, J., Luo, Y., Guo, H., Jiang, R. D., Liu, M. Q., Chen, Y., Shen, X. R., Wang, X., Zheng, X. S., Zhao, K., Chen, Q. J., Deng, F., Liu, L. L., Yan, B., Zhan, F. X., Wang, Y. Y., Xiao, G. F., Shi, Z. L.: A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 2020;579(7798): 270–3.
5. Perlman, S., Netland, J.: Coronaviruses post-SARS: update on replication and pathogenesis. Nat Rev Microbiol 2009;7(6): 439-50.
6. Brian, D. A., Baric, R. S.: Coronavirus genome structure and replication. Curr Top Microbiol Immunol 2005;287: 1-30.
7. Hamre, D., Procknow, J. J.: A new virus isolated from the human respiratory tract. Proc Soc Exp Biol Med 1966;121(1): 190-3.
8. McIntosh, K., Dees, J. H., Becker, W. B., Kapikian, A. Z., Chanock, R. M.: Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease. Proc Natl Acad Sci U S A 1967;57(4): 933-40.
9. Tyrrell, D. A., Bynoe, M. L.: Cultivation of a Novel Type of Common-Cold Virus in Organ Cultures. Br Med J 1965;1(5448): 1467-70.
10. van der Hoek, L.Pyrc, K., Jebbink, M. F., Vermeulen-Oost, W., Berkhout, R. J., Wolthers, K. C., Wertheim-van Dillen, P. M., Kaandorp, J., Spaargaren, J., Berkhout, B.: Identification of a new human coronavirus. Nat Med 2004;10(4): 368-73.
11. Woo, P. C., Lau, S. K., Tsoi, H. W., Huang, Y., Poon, R. W., Chu, C. M., Lee, R. A., Luk, W. K., Wong, G. K., Wong, B. H., Cheng, V. C., Tang, B. S., Wu, A. K., Yung, R. W., Chen, H., Guan, Y., Chan, K. H., Yuen, K. Y.: Clinical and molecular epidemiological features of coronavirus HKU1- associated community-acquired pneumonia. J Infect Dis 2005; 192(11): 1898-907.
12. Pyrc, K., Berkhout, B., van der Hoek, L.: The novel human coronaviruses NL63 and HKU1. J Virol 2007; 81(7): 3051-7.
13. Drosten, C., Gunther, S., Preiser, W., van der Werf, S., Brodt, H. R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A., Berger, A., Burguiere, A. M., Cinatl, J., Eickmann, M., Escriou, N., Grywna, K., Kramme, S., Manuguerra, J. C., Muller, S., Rickerts, V., Sturmer, M., Vieth, S., Klenk, H. D., Osterhaus, A. D., Schmitz, H., Doerr, H. W.: Identification of a novel coronavirus in patients with severe acute respiratory syndrome. N Engl J Med 2003;348(20): 1967- 76.
14. Fouchier, R. A., Kuiken, T., Schutten, M., van Amerongen, G., van Doornum, G. J., van den Hoogen, B. G., Peiris, M., Lim, W., Stohr, K., Osterhaus, A. D.: Aetiology: Koch's postulates fulfilled for SARS virus. Nature 2003;423(6937): 240.
15. Ksiazek, T. G., Erdman, D., Goldsmith, C. S., Zaki, S. R., Peret, T., Emery, S., Tong, S., Urbani, C., Comer, J. A., Lim, W., Rollin, P. E., Dowell, S. F., Ling, A. E., Humphrey, C. D., Shieh, W. J., Guarner, J., Paddock, C. D., Rota, P., Fields, B., DeRisi, J., Yang, J. Y., Cox, N., Hughes, J. M., LeDuc, J. W., Bellini, W. J., Anderson, L. J., Sars Working Group: A novel coronavirus associated with severe acute respiratory syndrome. N Engl J Med 2003;348(20): 1953-66.
16. Kuiken, T., Fouchier, R. A., Schutten, M., Rimmelzwaan, G. F., van Amerongen, G., van Riel, D., Laman, J. D., de Jong, T., van Doornum, G., Lim, W., Ling, A. E., Chan, P. K., Tam, J. S., Zambon, M. C., Gopal, R., Drosten, C., van der Werf, S., Escriou, N., Manuguerra, J. C., Stohr, K., Peiris, J. S., Osterhaus, A. D.: Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome. Lancet 2003;362(9380): 263-70.
17. Zaki, A. M., van Boheemen, S., Bestebroer, T. M., Osterhaus, A. D., Fouchier, R. A.: Isolation of a novel coronavirus from a man with pneumonia in Saudi Arabia. N Engl J Med 2012;367(19): 1814- 20.
18. World Health Organization.: Middle East Respiratory Syndrome Coronavirus (Mers-cov)—Saudi Arabia. Available online: http://www.who.int/csr/don/07-november-2014-mers/en/ (accessed on 1 December 2014).
19. Li, W., Shi, Z., Yu, M., Ren, W., Smith, C., Epstein, J. H., Wang, H., Crameri, G., Hu, Z., Zhang, H., Zhang, J., McEachern, J., Field, H., Daszak, P., Eaton, B. T., Zhang, S., Wang, L. F.: Bats are natural reservoirs of SARS-like coronaviruses. Science 2005;310(5748): 676-9.
20. Hemida, M. G., Perera, R. A., Wang, P., Alhammadi, M. A., Siu, L. Y., Li, M., Poon, L. L., Saif, L., Alnaeem, A., Peiris, M.: Middle East Respiratory Syndrome (MERS) coronavirus seroprevalence in domestic livestock in Saudi Arabia, 2010 to 2013. Euro Surveill 2013;18(50): 20659.
21. Azhar, E. I., El-Kafrawy, S. A., Farraj, S. A., Hassan, A. M., Al-Saeed, M. S., Hashem, A. M., Madani, T. A.: Evidence for camel-to-human transmission of MERS coronavirus. N Engl J Med 2014;370(26): 2499-505.
22. Heald-Sargent, T., Gallagher, T.: Ready, set, fuse! The coronavirus spike protein and acquisition of fusion competence. Viruses 2012; 4(4):557-80.
23. Li, F.: Receptor recognition and cross-species infections of SARS coronavirus. Antiviral Res 2013;100(1):246-.54.
24. Belouzard, S., Millet, J. K., Licitra, B. N., Whittaker, G. R.: Mechanisms of coronavirus cell entry mediated by the viral spike protein. Viruses 2012;4(6): 1011-33.
25. Hoffmann, M., Kleine-Weber, H., Schroeder, S., Kruger, N., Herrler, T., Erichsen, S. Schiergens, T. S., Herrler, G., Wu, N. H., Nitsche, A., Muller, M. A., Drosten, C., Pohlmann, S.: SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 2020;181(2): 271–280.
26. Matsuyama, S., Nao, N., Shirato, K., Kawase, M., Saito, S., Takayama, I., Nagata, N., Sekizuka, T., Katoh, H., Kato, F., Sakata, M., Tahara, M., Kutsuna, S., Ohmagari, N., Kuroda, M., Suzuki, T., Kageyama, T., Takeda, M.: Enhanced isolation of SARS-CoV-2 by TMPRSS2 expressing cells. Proc Natl Acad Sci USA 2000;117(13): 7001–7003.
27. Ozono, S., Zhang, Y., Tobiume, M., Kishigami, S., Tokunaga, K.: Super-rapid quantitation of the production of HIV-1 harboring a luminescent peptide tag. J Biol Chem 2020;295(37), 13023–30.
28. Li, 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, M.: Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 2003;426(6965): 450–54.
29. Haga, S., Yamamoto, N., Nakai-Murakami, C., Osawa, Y., Tokunaga, K., Sata, T., Yamamoto, N., Sasazuki, T., Ishizaka, Y.: Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry. Proc. Natl Acad Sci USA 2008;105(22): 7809–14.
30. Yang, Z. Y., Huang, Y., Ganesh, L., Leung, K., Kong, W. P., Schwartz, O., Subbarao, K., Nabel, G. J.: 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 2004;78(11):5642– 50.
31. Niwa, H., Yamamura, K., Miyazaki, J.: Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 1991;108(2):193–99.
32. Tada, T., Zhang, Y., Koyama, T., Tobiume, M., Tsunetsugu-Yokota, Y., Yamaoka, S., Fujita, H., Tokunaga, K.: MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins. Nat Med 2015;21(12):1502–07.
33. Piller, S. C., Dubay, J. W., Derdeyn, C. A., Hunter, E.: Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: effects on glycoprotein incorporation and infectivity. J Virol 2000;74(24):11717–23.
34. Witting, S. R., Vallanda, P. & Gamble, A. L. Characterization of a third generation lentiviral vector pseudotyped with Nipah virus envelope proteins for endothelial cell transduction. Gene Ther 2013; 20: 997–1005.
35. Christodoulopoulos, I., Cannon, P. M.: Sequences in the cytoplasmic tail of the gibbon ape leukemia virus envelope protein that prevent its incorporation into lentivirus vectors. J Virol 2001;75(9), 4129– 38.
36. Wei, X., Li, X., Cui, J.: Evolutionary perspectives on novel coronaviruses identified in pneumonia cases in China. Natl Sci Rev 2020;7(2):239–42.
37. Ou, J., Zhou, Z., Dai, R., Zhang, J., Zhao, S., Wu, X., Lan, W., Ren, Y., Cui, L., Lan, Q., Lu, L., Seto, D., Chodosh, J., Wu, J., Zhang, G., Zhang, Q.: V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity. J Virol 2021;95(16): e00617-21.
38. Zehender, G., Lai, A., Bergna, A., Meroni, L., Riva, A., Balotta, C., Tarkowski, M., Gabrieli, A., Bernacchia, D., Rusconi, S., Rizzardini, G., Antinori, S., Galli, M.: Genomic characterization and phylogenetic analysis of SARS-COV-2 in Italy. J Med Virol 2020;92(9): 1637–40.
39. Gambaro, F., Behillil, S., Baidaliuk, A., Donati, F., Albert, M., Alexandru, A., Vanpeene, M., Bizard, M., Brisebarre, A., Barbet, M., Derrar, F., van der Werf, S., Enouf, V., Simon-Loriere, E.: Introductions and early spread of SARS-CoV-2 in France, 24 January to 23 March 2020. Euro Surveill 2020;25(26)
40. Diez-Fuertes, F., Iglesias-Caballero, M., Garcia-Perez, J., Monzon, S., Jimenez, P., Varona, S., Cuesta, I., Zaballos, A., Jimenez, M., Checa, L., Pozo, F., Perez-Olmeda, M., Thomson, M. M., Alcami, J., Casas, I.: A Founder Effect Led Early SARS-CoV-2 Transmission in Spain. J Virol 2021;95(3): e01583-20.
41. Gudbjartsson, D. F., Gudbjartsson, D. F., Helgason, A., Jonsson, H., Magnusson, O. T., Melsted, P., Norddahl, G. L., Saemundsdottir, J., Sigurdsson, A., Sulem, P., Agustsdottir, A. B., Eiriksdottir, B., Fridriksdottir, R., Gardarsdottir, E. E., Georgsson, G., Gretarsdottir, O. S., Gudmundsson, K. R., Gunnarsdottir, T. R., Gylfason, A., Holm, H., Jensson, B. O., Jonasdottir, A., Jonsson, F., Josefsdottir, K. S., Kristjansson, T., Magnusdottir, D. N., le Roux, L., Sigmundsdottir, G., Sveinbjornsson, G., Sveinsdottir, K. E., Sveinsdottir, M., Thorarensen, E. A., Thorbjornsson, B., Love, A., Masson, G., Jonsdottir, I., Moller, A. D., Gudnason, T., Kristinsson, K. G., Thorsteinsdottir, U., Stefansson, K.: Spread of SARS-CoV-2 in the Icelandic population. N Engl J Med 2020;382(24): 2302–15.
42. Leary, S., Gaudieri, S., Parker, M. D., Chopra, A., James, I., Pakala, S., Alves, E., John, M., Lindsey, B. B., Keeley, A. J., Rowland-Jones, S. L., Swanson, M. S., Ostrov, D. A., Bubenik, J. L., Das, S., Sidney, J., Sette, A., Covid- Genomics UK consortium, de Silva, T. I., Phillips, E., Mallal, S.: Generation of a novel SARS-CoV-2 sub-genomic RNA due to the R203K/G204R variant in nucleocapsid: homologous recombination has potential to change SARS-CoV-2 at both protein and RNA level. Preprint at bioRxiv 2021; https://doi.org/10.1101/2020.04.10.029454
43. Gonzalez-Reiche, A. S., Hernandez, M. M., Sullivan, M. J., Ciferri, B., Alshammary, H., Obla, A., Fabre, S., Kleiner, G., Polanco, J., Khan, Z., Alburquerque, B., van de Guchte, A., Dutta, J., Francoeur, N., Melo, B. S., Oussenko, I., Deikus, G., Soto, J., Sridhar, S. H., Wang, Y. C., Twyman, K., Kasarskis, A., Altman, D. R., Smith, M., Sebra, R., Aberg, J., Krammer, F., Garcia-Sastre, A., Luksza, M., Patel, G., Paniz-Mondolfi, A., Gitman, M., Sordillo, E. M., Simon, V., van Bakel, H.: Introductions and early spread of SARS-CoV-2 in the New York City area. Science 2020;369(6501): 297–301.
44. Sungnak, W., Huang, N., Becavin, C., Berg, M., Queen, R., Litvinukova, M., Talavera-Lopez, C., Maatz, H., Reichart, D., Sampaziotis, F., Worlock, K. B., Yoshida, M., Barnes, J. L., H. C. A. Lung Biological Network.: SARS-CoV-2 entry factors are highly expressed in nasal epithelial cells together with innate immune genes. Nat Med 2020;26(5): 681–87.
45. Lamers, M. M., Beumer, J., van der Vaart, J., Knoops, K., Puschhof, J., Breugem, T. I., Ravelli, R. B. G., Paul van Schayck, J., Mykytyn, A. Z., Duimel, H. Q., van Donselaar, E., Riesebosch, S., Kuijpers, H. J. H., Schipper, D., van de Wetering, W. J., de Graaf, M., Koopmans, M., Cuppen, E., Peters, P. J., Haagmans, B. L., Clevers, H.: SARS-CoV-2 productively infects human gut enterocytes. Science 2020;369(6499): 50–54.
46. Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., Niu, P., Zhan, F., Ma, X., Wang, D., Xu, W., Wu, G., Gao, G. F., Tan, W., China Novel Coronavirus, Investigating Research, Team : A novel coronavirus from patients with pneumonia in China, 2019. N Engl J Med 2020;382(8): 727–33.
47. Gu, J., Korteweg, C.: Pathology and pathogenesis of severe acute respiratory syndrome. Am J Pathol 2007;170(4): 1136–47.
48. To, K. K., Tsang, O. T., Leung, W. S., Tam, A. R., Wu, T. C., Lung, D. C.,Yip, C. C., Cai, J. P., Chan, J. M., Chik, T. S., Lau, D. P., Choi, C. Y., Chen, L. L., Chan, W. M., Chan, K. H., Ip, J. D., Ng, A. C., Poon, R. W., Luo, C. T., Cheng, V. C., Chan, J. F., Hung, I. F., Chen, Z., Chen, H., Yuen, K. Y.: Temporal profiles of viral load in posterior oropharyngeal saliva samples and serum antibody responses during infection by SARS-CoV- 2: an observational cohort study. Lancet Infect Dis 2020;20(5): 565–74.
49. Arons, M. M., Hatfield, K. M., Reddy, S. C., Kimball, A., James, A., Jacobs, J. R., Taylor, J., Spicer,K., Bardossy, A. C., Oakley, L. P., Tanwar, S., Dyal, J. W., Harney, J., Chisty, Z., Bell, J. M., Methner, M., Paul, P., Carlson, C. M., McLaughlin, H. P, Thornburg, N., Tong, S., Tamin, A., Tao, Y., Uehara, A., Harcourt, J., Clark, S., Brostrom-Smith, C., Page, L. C., Kay, M., Lewis, J., Montgomery, P., Stone, N. D., Clark, T. A., Honein, M. A., Duchin, J. S., Jernigan, J. A., Public, Health-Seattle, King, County, Cdc Covid- Investigation Team.: Presymptomatic SARS-CoV-2 infections and transmission in a skilled nursing facility. N Engl J Med 2020;382(22): 2081–90.
50. Rivett, L., Sridhar, S., Sparkes, D., Routledge, M., Jones, N. K., Forrest, S., Young, J., Pereira-Dias, J., Hamilton, W. L., Ferris, M., Torok, M. E., Meredith, L., Citiid-Nihr Covid- BioResource Collaboration, Curran, M. D., Fuller, S., Chaudhry, A., Shaw, A., Samworth, R. J., Bradley, J. R., Dougan, G., Smith, K. G., Lehner, P. J., Matheson, N. J., Wright, G., Goodfellow, I. G., Baker, S., Weekes, M. P.: Screening of healthcare workers for SARS-CoV-2 highlights the role of asymptomatic carriage in COVID-19 transmission. Elife 2020;9: e58728.
51. Leung, G. M., Chung, P. H., Tsang, T., Lim, W., Chan, S. K., Chau, P., Donnelly, C. A., Ghani, A. C., Fraser, C., Riley, S., Ferguson, N. M., Anderson, R. M., Law, Y. L., Mok, T., Ng, T., Fu, A., Leung, P. Y., Peiris, J. S., Lam, T. H., Hedley, A. J.: SARS-CoV antibody prevalence in all Hong Kong patient contacts. Emerg Infect Dis 2004;10(9): 1653–56.
52. Hu, J., He, C. L., Gao, Q. Z., Zhang, G. J., Cao, X. X., Long, Q. X., Deng, H. J., Huang, L. Y., Chen, J., Wang, K., Tang, N., Huang, A. L.: D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity. Preprint at bioRxiv 2020; https://doi.org/10.1101/2020.06.20.161323
53. Pellis, L., Scarabel, F., Stage, H. B., Overton, C. E., Chappell, L. H. K., Fearon, E., Bennett, E., Lythgoe, K. A., House, T. A., Hall, I., University of Manchester, Covid-Modelling Group: Challenges in control of COVID-19: short doubling time and long delay to effect of interventions. Philos Trans R Soc Lond B Biol Sci 2021;376 (1829): 20200264.
54. Wu, J. T., Leung, K., Leung, G. M.: Nowcasting and forecasting the potential domestic and international spread of the 2019-nCoV outbreak originating in Wuhan, China: a modelling study. Lancet 2020;395(10225): 689–697.
55. Ozono, S., Zhang, Y., Ode, H., Sano, K., Tan, T. S., Imai, K., Miyoshi, K., Kishigami, S., Ueno, T., Iwatani, Y., Suzuki, T., Tokunaga, K.: SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity. Nat Commun 2021;12(1): 848.
56. Shang, J., Wan, Y., Luo, C., Ye, G., Geng, Q., Auerbach, A., Li, F.: Cell entry mechanisms of SARS- CoV-2. Proc Natl Acad Sci U S A 2020;117(21): 11727–11734.
57. Yurkovetskiy, L., Wang, X., Pascal, K. E., Tomkins-Tinch, C., Nyalile, T. P., Wang, Y., Baum, A., Diehl, W. E., Dauphin, A., Carbone, C., Veinotte, K., Egri, S. B., Schaffner, S. F., Lemieux, J. E., Munro, J. B., Rafique, A., Barve, A., Sabeti, P. C., Kyratsous, C. A., Dudkina, N. V., Shen, K., Luban, J.: Structural and functional analysis of the D614G SARSCoV- 2 spike protein variant. Cell 2020;183(3): 739–751.e738.
58. Zhang, L., Jackson, C. B., Mou, H., Ojha, A., Peng, H., Quinlan, B. D., Rangarajan, E. S., Pan, A., Vanderheiden, A., Suthar, M. S., Li, W., Izard, T., Rader, C., Farzan, M., Choe, H.: SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity. Nat Commun 2020;11(1): 6013.
59. Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., Hastie, K. M., Parker, M. D., Partridge, D. G., Evans, C. M., Freeman, T. M., de Silva, T. I., Sheffield, Covid-Genomics Group, McDanal, C., Perez, L. G., Tang, H., Moon-Walker, A., Whelan, S. P., LaBranche, C. C., Saphire, E. O., Montefiori, D. C.: Tracking changes in SARS-CoV-2 spike: evidence that D614G increases infectivity of the COVID- 19 virus. Cell 2020;182(4): 812–827.e819.
60. Daniloski, Z., Jordan, T. X., Ilmain, J. K., Guo, X., Bhabha, G., tenOever, B. R., Sanjana, N. E.: The Spike D614G mutation increases SARS-CoV-2 infection of multiple human cell types. Elife 2021;10.
論文の公開元へ
