Kallikrein 13 serves as a priming protease during infection by the human coronavirus HKU1
Author(s) -
Aleksandra Milewska,
Katherine Falkowski,
Magdalena Kulczycka,
Ewa Bielecka,
Antoniskalska,
Paweł Mak,
Adam Lesner,
Marek Ochman,
Maciej Urlik,
Eleftherios P. Diamandis,
Ioannis Prassas,
Jan Potempa,
Tomasz Kantyka,
Krzysztof Pyrć
Publication year - 2020
Publication title -
science signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.659
H-Index - 154
eISSN - 1937-9145
pISSN - 1945-0877
DOI - 10.1126/scisignal.aba9902
Subject(s) - kallikrein , coronavirus , protease , virology , priming (agriculture) , covid-19 , biology , viral entry , microbiology and biotechnology , chemistry , enzyme , medicine , virus , biochemistry , viral replication , botany , germination , disease , outbreak , infectious disease (medical specialty)
Human coronavirus HKU1 (HCoV-HKU1) is associated with respiratory disease and is prevalent worldwide, but an in vitro model for viral replication is lacking. An interaction between the coronaviral spike (S) protein and its receptor is the primary determinant of tissue and host specificity; however, viral entry is a complex process requiring the concerted action of multiple cellular elements. Here, we found that the protease kallikrein 13 (KLK13) was required for the infection of human respiratory epithelial cells and was sufficient to mediate the entry of HCoV-HKU1 into nonpermissive RD cells. We also demonstrated the cleavage of the HCoV-HKU1 S protein by KLK13 in the S1/S2 region, suggesting that KLK13 is the priming enzyme for this virus. Together, these data suggest that protease distribution and specificity determine the tissue and cell specificity of the virus and may also regulate interspecies transmission.
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