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Artikel ; Online: Aspergillus fumigatus secretes a protease(s) that displays in silico binding affinity towards the SARS-CoV-2 spike protein and mediates SARS-CoV-2 pseudovirion entry into HEK-293T cells.

Mjokane, Nozethu / Akintemi, Eric O / Sabiu, Saheed / Gcilitshana, Onele M N / Albertyn, Jacobus / Pohl, Carolina H / Sebolai, Olihile M

Virology journal

2024 Band 21, Heft 1, Seite(n) 58

Abstract: Background: The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also ... ...

Abstract	Background: The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. Methods: The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. Results: We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. Conclusion: These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
Mesh-Begriff(e)	Humans ; Peptide Hydrolases ; Spike Glycoprotein, Coronavirus ; Aspergillus fumigatus ; SARS-CoV-2 ; HEK293 Cells ; Molecular Docking Simulation ; COVID-19 ; Peptides
Chemische Substanzen	Peptide Hydrolases (EC 3.4.-) ; spike protein, SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Peptides
Sprache	Englisch
Erscheinungsdatum	2024-03-06
Erscheinungsland	England
Dokumenttyp	Journal Article
ZDB-ID	2160640-7
ISSN	1743-422X ; 1743-422X
ISSN (online)	1743-422X
ISSN	1743-422X
DOI	10.1186/s12985-024-02331-z
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Cryptococcal proteases exhibit the potential to activate the latent SARS-CoV-2 spike protein

Nozethu Mjokane / Saheed Sabiu / Olufemi S. Folorunso / Onele M.N. Gcilitshana / Jacobus Albertyn / Carolina H. Pohl / Olihile M. Sebolai

Journal of Infection and Public Health, Vol 17, Iss 2, Pp 263-

2024 Band 270

Abstract: Background: The COVID-19 pandemic has affected more than 650 million people and resulted in over 6.8 million deaths. Notably, the disease could co-manifest with microbial infections, like cryptococcosis, which also presents as a primary lung infection. ... ...

Abstract	Background: The COVID-19 pandemic has affected more than 650 million people and resulted in over 6.8 million deaths. Notably, the disease could co-manifest with microbial infections, like cryptococcosis, which also presents as a primary lung infection. Objective: In this contribution, we sought to determine if cryptococcal supernatant (which contains secreted furin-like proteases) could activate the SARS-CoV-2 spike protein. Methods: Molecular docking of the crystal structures of the SARS-CoV-2 spike protein (target) and selected cryptococcal proteases (ligands) was executed using the high ambiguity driven protein-protein docking (HADDOCK) server, with the furin protease serving as a reference ligand. The furin protease is found in human cells and typically activates the SARS-CoV-2 spike protein.Importantly, in order to provide experimental evidence for enzymatic activity, we also assessed the biochemical efficiency of cryptococcal proteases to initiate viral entry into HEK-293 T cells by SARS-CoV-2 spike pseudotyped Lentivirus. Results: We show that the selected cryptococcal proteases could interact with the spike protein, and some had a better or comparable binding affinity for the spike protein than furin protease following an in silico comparative analysis of the molecular docking parameters. Furthermore, it was noted that the biochemical efficiency of the cryptococcal supernatant to transduce HEK-293 T cells with SARS-CoV-2 pseudovirions was comparable (p > 0.05) to that of recombinant furin. Conclusions: Taken together, these data show that cryptococcal proteases could activate the SARS-CoV-2 spike protein. In practice, it may be critical to determine if patients have an underlying cryptococcal infection, as this microbe could secrete proteases that may further activate the SARS-CoV-2 viral particles, thus undermining COVID-19 intervention measures.
Schlagwörter	Cryptococcal protease ; Furin protease ; HEK-293 T cells ; Protein-protein docking ; SARS-CoV-2 spike protein ; Infectious and parasitic diseases ; RC109-216 ; Public aspects of medicine ; RA1-1270
Thema/Rubrik (Code)	612
Sprache	Englisch
Erscheinungsdatum	2024-02-01T00:00:00Z
Verlag	Elsevier
Dokumenttyp	Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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Artikel: The Possible Role of Microbial Proteases in Facilitating SARS-CoV-2 Brain Invasion.

Mjokane, Nozethu / Folorunso, Olufemi S / Ogundeji, Adepemi O / Sebolai, Olihile M

Biology

2021 Band 10, Heft 10

Abstract: SARS-CoV-2 has been shown to display proclivity towards organs bearing angiotensin-converting enzyme (ACE2) expression cells. Of interest herein is the ability of the virus to exhibit neurotropism. However, there is limited information on how this virus ... ...

Abstract	SARS-CoV-2 has been shown to display proclivity towards organs bearing angiotensin-converting enzyme (ACE2) expression cells. Of interest herein is the ability of the virus to exhibit neurotropism. However, there is limited information on how this virus invades the brain. With this contribution, we explore how, in the context of a microbial co-infection using a cryptococcal co-infection as a model, SARS-CoV-2 could reach the brain. We theorise that the secretion of proteases by disseminated fungal cells might also activate the S2 domain of the viral spike glycoprotein for membrane fusion with brain endothelial cells leading to endocytosis. Understanding this potential invasion mechanism could lead to better SARS-CoV-2 intervention measures, which may also be applicable in instances of co-infection, especially with protease-secreting pathogens.
Sprache	Englisch
Erscheinungsdatum	2021-09-27
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology10100966
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Cryptococcal proteases exhibit the potential to activate the latent SARS-CoV-2 spike protein.

Mjokane, Nozethu / Sabiu, Saheed / Folorunso, Olufemi S / Gcilitshana, Onele M N / Albertyn, Jacobus / Pohl, Carolina H / Sebolai, Olihile M

Journal of infection and public health

2023 Band 17, Heft 2, Seite(n) 263–270

Abstract	Background: The COVID-19 pandemic has affected more than 650 million people and resulted in over 6.8 million deaths. Notably, the disease could co-manifest with microbial infections, like cryptococcosis, which also presents as a primary lung infection. Objective: In this contribution, we sought to determine if cryptococcal supernatant (which contains secreted furin-like proteases) could activate the SARS-CoV-2 spike protein. Methods: Molecular docking of the crystal structures of the SARS-CoV-2 spike protein (target) and selected cryptococcal proteases (ligands) was executed using the high ambiguity driven protein-protein docking (HADDOCK) server, with the furin protease serving as a reference ligand. The furin protease is found in human cells and typically activates the SARS-CoV-2 spike protein. Importantly, in order to provide experimental evidence for enzymatic activity, we also assessed the biochemical efficiency of cryptococcal proteases to initiate viral entry into HEK-293 T cells by SARS-CoV-2 spike pseudotyped Lentivirus. Results: We show that the selected cryptococcal proteases could interact with the spike protein, and some had a better or comparable binding affinity for the spike protein than furin protease following an in silico comparative analysis of the molecular docking parameters. Furthermore, it was noted that the biochemical efficiency of the cryptococcal supernatant to transduce HEK-293 T cells with SARS-CoV-2 pseudovirions was comparable (p > 0.05) to that of recombinant furin. Conclusions: Taken together, these data show that cryptococcal proteases could activate the SARS-CoV-2 spike protein. In practice, it may be critical to determine if patients have an underlying cryptococcal infection, as this microbe could secrete proteases that may further activate the SARS-CoV-2 viral particles, thus undermining COVID-19 intervention measures.
Mesh-Begriff(e)	Humans ; Furin/chemistry ; Furin/metabolism ; COVID-19 ; Spike Glycoprotein, Coronavirus/chemistry ; SARS-CoV-2 ; Peptide Hydrolases/metabolism ; Molecular Docking Simulation ; Pandemics ; HEK293 Cells
Chemische Substanzen	Furin (EC 3.4.21.75) ; spike protein, SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Peptide Hydrolases (EC 3.4.-)
Sprache	Englisch
Erscheinungsdatum	2023-12-14
Erscheinungsland	England
Dokumenttyp	Journal Article
ZDB-ID	2467587-8
ISSN	1876-035X ; 1876-0341
ISSN (online)	1876-035X
ISSN	1876-0341
DOI	10.1016/j.jiph.2023.12.008
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: The Possible Role of Microbial Proteases in Facilitating SARS-CoV-2 Brain Invasion

Mjokane, Nozethu / Folorunso, Olufemi S. / Ogundeji, Adepemi O. / Sebolai, Olihile M.

Biology. 2021 Sept. 27, v. 10, no. 10

2021

Abstract	SARS-CoV-2 has been shown to display proclivity towards organs bearing angiotensin-converting enzyme (ACE2) expression cells. Of interest herein is the ability of the virus to exhibit neurotropism. However, there is limited information on how this virus invades the brain. With this contribution, we explore how, in the context of a microbial co-infection using a cryptococcal co-infection as a model, SARS-CoV-2 could reach the brain. We theorise that the secretion of proteases by disseminated fungal cells might also activate the S2 domain of the viral spike glycoprotein for membrane fusion with brain endothelial cells leading to endocytosis. Understanding this potential invasion mechanism could lead to better SARS-CoV-2 intervention measures, which may also be applicable in instances of co-infection, especially with protease-secreting pathogens.
Schlagwörter	Severe acute respiratory syndrome coronavirus 2 ; brain ; endocytosis ; fungi ; glycoproteins ; membrane fusion ; mixed infection ; models ; peptidyl-dipeptidase A ; proteinases ; secretion ; viruses
Sprache	Englisch
Erscheinungsverlauf	2021-0927
Erscheinungsort	Multidisciplinary Digital Publishing Institute
Dokumenttyp	Artikel
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology10100966
Datenquelle	NAL Katalog (AGRICOLA)

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Artikel ; Online: 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

Cells

2022 Band 11, Heft 3

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 ...

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 (
Mesh-Begriff(e)	Amino Acid Sequence ; Aspartic Acid Proteases/genetics ; Aspartic Acid Proteases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; COVID-19/epidemiology ; COVID-19/prevention & control ; COVID-19/virology ; Cryptococcus neoformans/enzymology ; Cryptococcus neoformans/genetics ; Fluorescent Dyes/chemistry ; Furin/genetics ; Furin/metabolism ; Humans ; Pandemics ; Peptides/chemistry ; Peptides/metabolism ; Proteolysis ; SARS-CoV-2/metabolism ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/metabolism
Chemische Substanzen	Bacterial Proteins ; Fluorescent Dyes ; Peptides ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Aspartic Acid Proteases (EC 3.4.-) ; Furin (EC 3.4.21.75)
Sprache	Englisch
Erscheinungsdatum	2022-01-27
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11030437
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: The Repurposing of Acetylsalicylic Acid as a Photosensitiser to Inactivate the Growth of Cryptococcal Cells.

Ogundeji, Adepemi O / Mjokane, Nozethu / Folorunso, Olufemi S / Pohl, Carolina H / Nyaga, Martin M / Sebolai, Olihile M

Pharmaceuticals (Basel, Switzerland)

2021 Band 14, Heft 5

Abstract: Photodynamic treatment (PDT) is often successful when used against aerobic microbes, given their natural susceptibility to oxidative damage. To this end, the current study aimed to explore the photodynamic action of acetylsalicylic acid (ASA; aspirin, ... ...

Abstract	Photodynamic treatment (PDT) is often successful when used against aerobic microbes, given their natural susceptibility to oxidative damage. To this end, the current study aimed to explore the photodynamic action of acetylsalicylic acid (ASA; aspirin, which is commonly used to treat non-infectious ailments), when administered to respiring cryptococcal cells. The treatment of cryptococcal cells, i.e., exposure to 0.5 or 1 mM of ASA in the presence of ultraviolet light (UVL) for 10 min, resulted in a significant (
Sprache	Englisch
Erscheinungsdatum	2021-04-23
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2193542-7
ISSN	1424-8247
ISSN	1424-8247
DOI	10.3390/ph14050404
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: The first survey of cryptococcal cells in bird droppings across Bloemfontein, South Africa.

Kankam, Gloria / Christians, Byron / Maliehe, Maphori / Mjokane, Nozethu / Ogundeji, Adepemi O / Folorunso, Olufemi S / Pohl, Carolina H / Sebolai, Olihile M

Veterinary world

2021 Band 14, Heft 10, Seite(n) 2739–2744

Abstract: Background and aim: Cryptococcal yeast cells are spread across different ecosystems through bird movement and are deposited in bird guano. These cells may be inhaled by humans and lead to cryptococcal pneumonia. In individuals with reduced immune T-cell ...

Abstract	Background and aim: Cryptococcal yeast cells are spread across different ecosystems through bird movement and are deposited in bird guano. These cells may be inhaled by humans and lead to cryptococcal pneumonia. In individuals with reduced immune T-cell populations, cells may disseminate to the brain and cause the often-deadly cryptococcal meningitis. In this study, we surveyed cryptococcal cells in bird droppings across the city of Bloemfontein, South Africa. Materials and methods: We aseptically collected 120 bird dropping samples from 15 representative city sites. In the laboratory, samples were assessed with regards to location, weighed, and standardized to a mass of 1 g before suspension in 10 mL phosphate buffer saline. Samples were first screened usingCalcofluor-white stain as it is a rapid technique for the detection of fungi via binding to cell wall components such as chitin. After this, positive Calcofluor samples were serologically assayed for the cryptococcal antigen (CrAg). To confirm assay data, CrAg positive samples were then cultured on bird seed agar and resulting colonies were assessed using Indian ink. Results: We determined that 10/15 locations were positive for the CrAg. Pathogenic cells were identified on bird seed agar as brown colonies. When examined using microscopy, brown colony cells exhibited characteristic thick capsules representative of cryptococcal cells. Conclusion: This is the first proximate analysis showing the ecological distribution of cryptococcal cells in Bloemfontein. This is important as associated infections are acquired from the environment. Similarly, given the threat posed by cryptococcal cells to immunocompromised individuals, local authorities must initiate measures curbing the spread of these cells.
Sprache	Englisch
Erscheinungsdatum	2021-10-25
Erscheinungsland	India
Dokumenttyp	Journal Article
ZDB-ID	2456277-4
ISSN	2231-0916 ; 0972-8988
ISSN (online)	2231-0916
ISSN	0972-8988
DOI	10.14202/vetworld.2021.2739-2744
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: The Repurposing of Acetylsalicylic Acid as a Photosensitiser to Inactivate the Growth of Cryptococcal Cells

Adepemi O. Ogundeji / Nozethu Mjokane / Olufemi S. Folorunso / Carolina H. Pohl / Martin M. Nyaga / Olihile M. Sebolai

Pharmaceuticals, Vol 14, Iss 404, p

2021 Band 404

Abstract	Photodynamic treatment (PDT) is often successful when used against aerobic microbes, given their natural susceptibility to oxidative damage. To this end, the current study aimed to explore the photodynamic action of acetylsalicylic acid (ASA; aspirin, which is commonly used to treat non-infectious ailments), when administered to respiring cryptococcal cells. The treatment of cryptococcal cells, i.e., exposure to 0.5 or 1 mM of ASA in the presence of ultraviolet light (UVL) for 10 min, resulted in a significant ( p < 0.05) reduction in the growth of tested cells when compared to non-treated (non-Rx) cells, i.e., no ASA and no UVL. The treated cells were also characterised by diseased mitochondria, which is crucial for the survival of respiring cells, as observed by a significant ( p < 0.05) loss of mitochondrial membrane potential (ΔΨM) and significant ( p < 0.05) accumulation of reactive oxygen species (ROS) when compared to non-Rx cells. Moreover, the photolytic products of acetylsalicylic acid altered the ultrastructural appearance of treated cells as well as limited the expression levels of the capsular-associated gene, CAP64, when compared to non-Rx cells. The results of the study highlight the potential use of ASA as a photosensitiser that is effective for controlling the growth of cryptococcal cells. Potentially, this treatment can also be used as an adjuvant, to complement and support the usage of current anti-microbial agents.
Schlagwörter	acetylsalicylic acid (ASA ; aspirin) ; capsule ; CAP64 ; Cryptococcus ; membrane potential (ΔΨM) ; photodynamic treatment ; Medicine ; R ; Pharmacy and materia medica ; RS1-441
Thema/Rubrik (Code)	630
Sprache	Englisch
Erscheinungsdatum	2021-04-01T00:00:00Z
Verlag	MDPI AG
Dokumenttyp	Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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Artikel ; Online: Cryptococcal Protease(s) and the Activation of SARS-CoV-2 Spike (S) Protein

Nozethu Mjokane / Maphori Maliehe / Olufemi S. Folorunso / Adepemi O. Ogundeji / Onele M. N. Gcilitshana / Jacobus Albertyn / Carolina H. Pohl / Olihile M. Sebolai

Cells, Vol 11, Iss 437, p

2022 Band 437

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, S PRRA R↓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.
Schlagwörter	cryptococcal infection ; Cryptococcus ; Cryptococcus neoformans ; fluorogenic peptide ; furin ; protease ; Biology (General) ; QH301-705.5
Sprache	Englisch
Erscheinungsdatum	2022-01-01T00:00:00Z
Verlag	MDPI AG
Dokumenttyp	Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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