1 Zhou, P. et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579, 270-273, doi:10.1038/s41586-020-2012-7 (2020).
2 Zhu, N. et al. A Novel Coronavirus from Patients with Pneumonia in China, 2019. The New England journal of medicine 382, 727-733, doi:10.1056/NEJMoa2001017 (2020).
3 Rothan, H. A. & Byrareddy, S. N. The epidemiology and pathogenesis of coronavirus disease (COVID-19) outbreak. J Autoimmun 109, 102433, doi:10.1016/j.jaut.2020.102433 (2020).
4 Li, W. et al. Bats are natural reservoirs of SARS-like coronaviruses. Science 310, 676-679, doi:10.1126/science.1118391 (2005).
5 Hoffmann, M. et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell, doi:10.1016/j.cell.2020.02.052 (2020).
6 Wrapp, D. et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science (New York, N.Y 367, 1260-1263, doi:10.1126/science.abb2507 (2020).
7 Yan, R. et al. Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2. Science (New York, N.Y, doi:10.1126/science.abb2762 (2020).
8 Mullard, A. First antibody against COVID-19 spike protein enters phase I. Nat Rev Drug Discov 19, 435, doi:10.1038/d41573-020-00108-x (2020).
9 Bost, P. et al. Host-Viral Infection Maps Reveal Signatures of Severe COVID-19 Patients. Cell 181, 1475-1488 e1412, doi:10.1016/j.cell.2020.05.006 (2020).
10 Chi, X. et al. A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2. Science (New York, N.Y, doi:10.1126/science.abc6952 (2020).
11 Baum, A. et al. Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies. Science (New York, N.Y, doi:10.1126/science.abd0831 (2020).
12 Liu, A., Li, Y., Peng, J., Huang, Y. & Xu, D. Antibody responses against SARS-CoV-2 in COVID-19 patients. Journal of medical virology, doi:10.1002/jmv.26241 (2020).
13 Long, Q. X. et al. Antibody responses to SARS-CoV-2 in patients with COVID-19. Nat Med 26, 845-848, doi:10.1038/s41591-020-0897-1 (2020).
14 Wu, Y. et al. A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2. Science (New York, N.Y 368, 1274-1278, doi:10.1126/science.abc2241 (2020).
15 Brouwer, P. J. M. et al. Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability. Science (New York, N.Y, doi:10.1126/science.abc5902 (2020).
16 Rogers, T. F. et al. Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model. Science (New York, N.Y, doi:10.1126/science.abc7520 (2020).
17 Hansen, J. et al. Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail. Science (New York, N.Y, doi:10.1126/science.abd0827 (2020).
18 Shi, R. et al. A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2. Nature, doi:10.1038/s41586-020-2381-y (2020).
19 Ju, B. et al. Human neutralizing antibodies elicited by SARS-CoV-2 infection. Nature, doi:10.1038/s41586-020-2380-z (2020).
20 Chen, X. et al. Human monoclonal antibodies block the binding of SARS-CoV-2 spike protein to angiotensin converting enzyme 2 receptor. Cell Mol Immunol 17, 647-649, doi:10.1038/s41423-020-0426-7 (2020).
21 Monteil, V. et al. Inhibition of SARS-CoV-2 Infections in Engineered Human Tissues Using Clinical-Grade Soluble Human ACE2. Cell, doi:10.1016/j.cell.2020.04.004 (2020).
22 Batlle, D., Wysocki, J. & Satchell, K. Soluble angiotensin-converting enzyme 2: a potential approach for coronavirus infection therapy? Clin Sci (Lond) 134, 543-545, doi:10.1042/CS20200163 (2020).
23 Davidson, A. M., Wysocki, J. & Batlle, D. Interaction of SARS-CoV-2 and Other Coronavirus With ACE (Angiotensin-Converting Enzyme)-2 as Their Main Receptor: Therapeutic Implications. Hypertension 76, 1339-1349, doi:10.1161/HYPERTENSIONAHA.120.15256 (2020).
24 Thery, C., Zitvogel, L. & Amigorena, S. Exosomes: composition, biogenesis and function. Nat Rev Immunol 2, 569-579, doi:10.1038/nri855 (2002).
25 Stoorvogel, W., Kleijmeer, M. J., Geuze, H. J. & Raposo, G. The biogenesis and functions of exosomes. Traffic 3, 321-330, doi:10.1034/j.1600-0854.2002.30502.x (2002).
26 Costa-Silva, B. et al. Pancreatic cancer exosomes initiate pre-metastatic niche formation in the liver. Nat Cell Biol 17, 816-826, doi:10.1038/ncb3169 (2015).
27 Peinado, H. et al. Melanoma exosomes educate bone marrow progenitor cells toward a pro-metastatic phenotype through MET. Nat Med 18, 883-891, doi:10.1038/nm.2753 (2012).
28 Kamerkar, S. et al. Exosomes facilitate therapeutic targeting of oncogenic KRAS in pancreatic cancer. Nature 546, 498-503, doi:10.1038/nature22341 (2017).
29 Chen, G. et al. Exosomal PD-L1 contributes to immunosuppression and is associated with anti-PD-1 response. Nature 560, 382-386, doi:10.1038/s41586-018-0392-8 (2018).
30 Poggio, M. et al. Suppression of Exosomal PD-L1 Induces Systemic Anti-tumor Immunity and Memory. Cell 177, 414-427 e413, doi:10.1016/j.cell.2019.02.016 (2019).
31 Murphy, D. E. et al. Extracellular vesicle-based therapeutics: natural versus engineered targeting and trafficking. Exp Mol Med 51, 1-12, doi:10.1038/s12276-019-0223-5 (2019).
32 Mendt, M. et al. Generation and testing of clinical-grade exosomes for pancreatic cancer. JCI Insight 3, doi:10.1172/jci.insight.99263 (2018).
33 Chen, L., Xiang, B., Wang, X. & Xiang, C. Exosomes derived from human menstrual blood-derived stem cells alleviate fulminant hepatic failure. Stem Cell Res Ther 8, 9, doi:10.1186/s13287-016-0453-6 (2017).
34 Kibria, G. et al. A rapid, automated surface protein profiling of single circulating exosomes in human blood. Sci Rep 6, 36502, doi:10.1038/srep36502 (2016).
35 Vlassov, A. V., Magdaleno, S., Setterquist, R. & Conrad, R. Exosomes: current knowledge of their composition, biological functions, and diagnostic and therapeutic potentials. Biochimica et biophysica acta 1820, 940-948, doi:10.1016/j.bbagen.2012.03.017 (2012).
36 Lindeman, R. M., PF; Gold, RZ. Introduction to bivariate and multivariate analysis. Vereniging voor Statistiek Bulletin 14, 11--14 (1980).
37 Groemping, U. Relative Importance for Linear Regression in R: The Package relaimpo. 2006 17, 27, doi:10.18637/jss.v017.i01 (2006).
38 Linsky, T. W. et al. De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2. Science 370, 1208-1214, doi:10.1126/science.abe0075 (2020).
39 Tu, Y. F. et al. A Review of SARS-CoV-2 and the Ongoing Clinical Trials. Int J Mol Sci 21, doi:10.3390/ijms21072657 (2020).
40 Ison, M. G., Wolfe, C. & Boucher, H. W. Emergency Use Authorization of Remdesivir: The Need for a Transparent Distribution Process. JAMA 323, 2365-2366, doi:10.1001/jama.2020.8863 (2020).
41 Kibria, G., Ramos, E. K., Wan, Y., Gius, D. R. & Liu, H. Exosomes as a Drug Delivery System in Cancer Therapy: Potential and Challenges. Mol Pharm 15, 3625-3633, doi:10.1021/acs.molpharmaceut.8b00277 (2018).
42 Roefs, M. T., Sluijter, J. P. G. & Vader, P. Extracellular Vesicle-Associated Proteins in Tissue Repair. Trends Cell Biol, doi:10.1016/j.tcb.2020.09.009 (2020).
43 Walsh, K. A. et al. SARS-CoV-2 detection, viral load and infectivity over the course of an infection. J Infect 81, 357-371, doi:10.1016/j.jinf.2020.06.067 (2020).
44 Harding, C. V., Heuser, J. E. & Stahl, P. D. Exosomes: looking back three decades and into the future. J Cell Biol 200, 367-371, doi:10.1083/jcb.201212113 (2013).
45 Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. Elife 7, doi:10.7554/eLife.42166 (2018).
46 Schneider, C. A., Rasband, W. S. & Eliceiri, K. W. NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9, 671-675, doi:10.1038/nmeth.2089 (2012).
47 Amanat, F. et al. A serological assay to detect SARS-CoV-2 seroconversion in humans. medRxiv : the preprint server for health sciences, doi:10.1101/2020.03.17.20037713 (2020).
48 McDade, T. W. et al. High seroprevalence for SARS-CoV-2 among household members of essential workers detected using a dried blood spot assay. PloS one 15, e0237833, doi:10.1371/journal.pone.0237833 (2020).
49 Yuan, M. et al. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science (New York, N.Y.) 368, 630-633, doi:10.1126/science.abb7269 (2020).