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Cryptococcal Protease(s) and the Activation of SARS-CoV-2 Spike (S) Protein.
Mjokane, Nozethu; Maliehe, Maphori; Folorunso, Olufemi S; Ogundeji, Adepemi O; Gcilitshana, Onele M N; Albertyn, Jacobus; Pohl, Carolina H; Sebolai, Olihile M.
  • Mjokane N; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Maliehe M; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Folorunso OS; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Ogundeji AO; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Gcilitshana OMN; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Albertyn J; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Pohl CH; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
  • Sebolai OM; Department of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, Bloemfontein 9301, South Africa.
Cells ; 11(3)2022 01 27.
Article in English | MEDLINE | ID: covidwho-1662647
ABSTRACT
In this contribution, we report on the possibility that cryptococcal protease(s) could activate the SARS-CoV-2 spike (S) protein. The S protein is documented to have a unique four-amino-acid sequence (underlined, SPRRAR↓S) at the interface between the S1 and S2 sites, that serves as a cleavage site for the human protease, furin. We compared the biochemical efficiency of cryptococcal protease(s) and furin to mediate the proteolytic cleavage of the S1/S2 site in a fluorogenic peptide. We show that cryptococcal protease(s) processes this site in a manner comparable to the efficiency of furin (p > 0.581). We conclude the paper by discussing the impact of these findings in the context of a SARS-CoV-2 disease manifesting while there is an underlying cryptococcal infection.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Bacterial Proteins / Cryptococcus neoformans / Aspartic Acid Proteases / Spike Glycoprotein, Coronavirus / SARS-CoV-2 Type of study: Observational study Limits: Humans Language: English Year: 2022 Document Type: Article Affiliation country: Cells11030437

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Bacterial Proteins / Cryptococcus neoformans / Aspartic Acid Proteases / Spike Glycoprotein, Coronavirus / SARS-CoV-2 Type of study: Observational study Limits: Humans Language: English Year: 2022 Document Type: Article Affiliation country: Cells11030437