Pan-coronavirus fusion inhibitors possess potent inhibitory activity against HIV-1, HIV-2, and simian immunodeficiency virus

References

• Colman PM, Lawrence MC. The structural biology of type I viral membrane fusion. Nat Rev Mol Cell Biol. 2003;4:309–319.
   PubMed Web of Science ®Google Scholar
• Eckert DM, Kim PS. Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem. 2001;70:777–810.
   PubMed Web of Science ®Google Scholar
• Chan DC, Fass D, Berger JM, et al. Core structure of gp41 from the HIV envelope glycoprotein. Cell. 1997;89:263–273.
   PubMed Web of Science ®Google Scholar
• Chan DC, Kim PS. HIV entry and its inhibition. Cell. 1998;93:681–684.
   PubMed Web of Science ®Google Scholar
• He Y. Synthesized peptide inhibitors of HIV-1 gp41-dependent membrane fusion. Curr Pharm Des. 2013;19:1800–1809.
   PubMed Web of Science ®Google Scholar
• Zhu Y, Chong H, Yu D, et al. Design and characterization of cholesterylated peptide HIV-1/2 fusion inhibitors with extremely potent and long-lasting antiviral activity. J Virol. 2019;93:e02312–e02318.
   Web of Science ®Google Scholar
• Zhu Y, Zhang X, Ding X, et al. Exceptional potency and structural basis of a T1249-derived lipopeptide fusion inhibitor against HIV-1, HIV-2, and simian immunodeficiency virus. J Biol Chem. 2018;293:5323–5334.
   PubMed Web of Science ®Google Scholar
• Chong H, Zhu Y, Yu D, et al. Structural and functional characterization of membrane fusion inhibitors with extremely potent activity against HIV-1, HIV-2, and simian immunodeficiency virus. J Virol. 2018;92:e01088-18.
   PubMed Web of Science ®Google Scholar
• Chong H, Xue J, Zhu Y, et al. Design of novel HIV-1/2 fusion inhibitors with high therapeutic efficacy in rhesus monkey models. J Virol. 2018;92:e00775–18.
   PubMed Web of Science ®Google Scholar
• Ding X, Zhang X, Chong H, et al. Enfuvirtide (T20)-based lipopeptide is a potent HIV-1 cell fusion inhibitor: implication for viral entry and inhibition. J Virol. 2017;91:e00831–17.
   PubMed Web of Science ®Google Scholar
• Chong H, Wu X, Su Y, et al. Development of potent and long-acting HIV-1 fusion inhibitors. AIDS. 2016;30:1187–1196.
   PubMed Web of Science ®Google Scholar
• Zhu N, Zhang D, Wang W, et al. A novel coronavirus from patients with pneumonia in China, 2019. N Engl J Med. 2020;382:727–733.
   PubMed Web of Science ®Google Scholar
• Zhou P, Yang XL, Wang XG, et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579:270–273.
   PubMed Web of Science ®Google Scholar
• Zhu Y, Yu D, Yan H, et al. Design of potent membrane fusion inhibitors against SARS-CoV-2, an emerging coronavirus with high fusogenic activity. J Virol. 2020;94:e00635–20.
   PubMed Web of Science ®Google Scholar
• Zhu Y, Yu D, Hu Y, et al. SARS-CoV-2 derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. Signal Transduct Target Ther. 2021. In press.
   Web of Science ®Google Scholar
• Xia S, Yan L, Xu W, et al. A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike. Sci Adv. 2019;5:eaav4580.
   PubMed Web of Science ®Google Scholar
• Xia S, Liu M, Wang C, et al. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. Cell Res. 2020;30:343–355.
   PubMed Web of Science ®Google Scholar
• de Camp A, Hraber P, Bailer RT, et al. Global panel of HIV-1 Env reference strains for standardized assessments of vaccine-elicited neutralizing antibodies. J Virol. 2014;88:2489–2507.
   Web of Science ®Google Scholar
• Rimsky LT, Shugars DC, Matthews TJ. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol. 1998;72:986–993.
   PubMed Web of Science ®Google Scholar
• Greenberg ML, Cammack N. Resistance to enfuvirtide, the first HIV fusion inhibitor. J Antimicrob Chemother. 2004;54:333–340.
   PubMed Web of Science ®Google Scholar
• Wei X, Decker JM, Liu H, et al. Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob Agents Chemother. 2002;46:1896–1905.
   PubMed Web of Science ®Google Scholar
• Veiga S, Yuan Y, Li X, et al. Why are HIV-1 fusion inhibitors not effective against SARS-CoV? biophysical evaluation of molecular interactions. Biochim Biophys Acta. 2006;1760:55–61.
   PubMed Web of Science ®Google Scholar
• Kliger Y, Levanon EY. Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy. BMC Microbiol. 2003;3:20.
   PubMed Web of Science ®Google Scholar
• Zhang XW, Yap YL. Structural similarity between HIV-1 gp41 and SARS-CoV S2 proteins suggests an analogous membrane fusion mechanism. Theochem. 2004;677:73–76.
   Web of Science ®Google Scholar
• Ahmadi K, Farasat A, Rostamian M, et al. Enfuvirtide, an HIV-1 fusion inhibitor peptide, can act as a potent SARS-CoV-2 fusion inhibitor: an in silico drug repurposing study. J Biomol Struct Dyn. 2021 Jan 13:1–11. doi:https://doi.org/10.1080/07391102.2021.1871958 [Online ahead of print].
   Web of Science ®Google Scholar
• Su B, Yao C, Zhao QX, et al. Efficacy and safety of the long-acting fusion inhibitor albuvirtide in antiretroviral-experienced adults with human immunodeficiency virus-1: interim analysis of the randomized, controlled, phase 3, non-inferiority TALENT study. Chin Med J (Engl). 2020;133:2919–2927.
   PubMed Web of Science ®Google Scholar
• Dwyer JJ, Wilson KL, Davison DK, et al. Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus. Proc Natl Acad Sci USA. 2007;104:12772–12777.
   PubMed Web of Science ®Google Scholar
• He Y, Xiao Y, Song H, et al. Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor. J Biol Chem. 2008;283:11126–11134.
   PubMed Web of Science ®Google Scholar
• Xiong S, Borrego P, Ding X, et al. A helical short-peptide fusion inhibitor with highly potent activity against human immunodeficiency virus type 1 (HIV-1), HIV-2, and simian immunodeficiency virus. J Virol. 2017;91:e01839–16.
   Web of Science ®Google Scholar
• Liu S, Xiao G, Chen Y, et al. Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. Lancet. 2004;363:938–947.
   PubMed Web of Science ®Google Scholar
• Bosch BJ, Martina BE, Van Der Zee R, et al. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. Proc Natl Acad Sci USA. 2004;101:8455–8460.
   PubMed Web of Science ®Google Scholar
• Xia S, Zhu Y, Liu M, et al. Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. Cell Mol Immunol. 2020 Jul;17(7):765–767.
   PubMed Web of Science ®Google Scholar
• Outlaw VK, Bovier FT, Mears MC, et al. Inhibition of coronavirus entry in vitro and ex vivo by a lipid-conjugated peptide derived from the SARS-CoV-2 spike glycoprotein HRC domain. mBio. 2020 Oct 20;11(5):e01935-20.
   Web of Science ®Google Scholar
• Schutz D, Ruiz-Blanco YB, Munch J, et al. Peptide and peptide-based inhibitors of SARS-CoV-2 entry. Adv Drug Deliv Rev. 2020;167:47–65.
   PubMed Web of Science ®Google Scholar
• Qiu Z, Chong H, Yao X, et al. Identification and characterization of a subpocket on the N-trimer of HIV-1 Gp41: implication for viral entry and drug target. AIDS. 2015;29:1015–1024.
   Web of Science ®Google Scholar
• Crespillo S, Camara-Artigas A, Casares S, et al. Single-chain protein mimetics of the N-terminal heptad-repeat region of gp41 with potential as anti-HIV-1 drugs. Proc Natl Acad Sci USA. 2014;111:18207–18212.
   PubMed Web of Science ®Google Scholar