Synergistic activation of bat SARS-like coronaviruses spike protein by elastase and TMPRSS2

• Published in: Scientific reports Vol. 15; no. 1; pp. 26469 - 16
• Main Authors: Yamamoto, Yuichiro, Inoue, Tetsuya, Sugiyama, Naoto, Furukawa, Miyu, Sato, Kaoru, Onodera, Taishi, Takahashi, Yoshimasa, Wakita, Takaji, Fukasawa, Masayoshi, Noguchi, Kohji
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 21.07.2025; Nature Publishing Group; Nature Portfolio
• Subjects: 631/326; 631/337; ACE2; Amino acids; Angiotensin-converting enzyme 2; Animals; Bat SARS-like coronavirus; Benzamidines - pharmacology; Cells; Chiroptera - virology; Chlorocebus aethiops; Coronaviridae; Coronaviruses; COVID-19; Disease transmission; Elastase; Epidemics; Experiments; Guanidines; Humanities and Social Sciences; Humans; Infections; Infectivity; Inflammation; Khosta-2; Medical research; Middle East respiratory syndrome; multidisciplinary; Pancreatic Elastase - metabolism; Proteases; Proteins; Proteolysis; RaTG13; Respiratory diseases; Sarbecovirus; Science; Science (multidisciplinary); Serine Endopeptidases - metabolism; Severe acute respiratory syndrome; Severe acute respiratory syndrome coronavirus 2; Severe acute respiratory syndrome-related coronavirus - metabolism; Spike Glycoprotein, Coronavirus - genetics; Spike Glycoprotein, Coronavirus - metabolism; Spike protein; Statistical analysis; Thermolysin; Trypsin; Vero Cells; Virus Internalization; Viruses; Zoonoses; Bat SARS-like coronavirus; Elastase; Spike protein; Khosta-2; RaTG13

Although numerous sarbecoviruses have been identified in bats, but most lack the ability to infect human cells. Some barriers limit coronavirus zoonosis, including susceptibility to host proteases. Here, we investigated whether exogenous protease treatment can circumvent host restrictions in two sev...