Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds
Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium aci...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
da Silva Neto, João Xavier [verfasserIn] Araújo, Nadine Monteiro Salgueiro |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
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| Umfang: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor - Penchovsky, Robert ELSEVIER, 2019, structure, function and interactions, New York, NY [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:143 ; year:2020 ; day:15 ; month:01 ; pages:814-824 ; extent:11 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.ijbiomac.2019.09.142 |
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ELV049047752 |
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| 245 | 1 | 0 | |a Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds |
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| 520 | |a Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. | ||
| 520 | |a Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. | ||
| 700 | 1 | |a da Costa, Helen Paula Silva |4 oth | |
| 700 | 1 | |a Vasconcelos, Ilka Maria |4 oth | |
| 700 | 1 | |a Pereira, Mirella Leite |4 oth | |
| 700 | 1 | |a Oliveira, Jose Tadeu Abreu |4 oth | |
| 700 | 1 | |a Lopes, Tiago Deiveson Pereira |4 oth | |
| 700 | 1 | |a Dias, Lucas Pinheiro |4 oth | |
| 700 | 1 | |a Araújo, Nadine Monteiro Salgueiro |4 oth | |
| 700 | 1 | |a Moura, Luiz Francisco Wemmenson Gonçalves |4 oth | |
| 700 | 1 | |a Van Tilburg, Mauricio Fraga |4 oth | |
| 700 | 1 | |a Guedes, Maria Izabel Florindo |4 oth | |
| 700 | 1 | |a Lopes, Larissa Alves |4 oth | |
| 700 | 1 | |a Morais, Eva Gomes |4 oth | |
| 700 | 1 | |a de Oliveira Bezerra de Sousa, Daniele |4 oth | |
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10.1016/j.ijbiomac.2019.09.142 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000872.pica (DE-627)ELV049047752 (ELSEVIER)S0141-8130(19)36206-3 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl da Silva Neto, João Xavier verfasserin aut Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. da Costa, Helen Paula Silva oth Vasconcelos, Ilka Maria oth Pereira, Mirella Leite oth Oliveira, Jose Tadeu Abreu oth Lopes, Tiago Deiveson Pereira oth Dias, Lucas Pinheiro oth Araújo, Nadine Monteiro Salgueiro oth Moura, Luiz Francisco Wemmenson Gonçalves oth Van Tilburg, Mauricio Fraga oth Guedes, Maria Izabel Florindo oth Lopes, Larissa Alves oth Morais, Eva Gomes oth de Oliveira Bezerra de Sousa, Daniele oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:143 year:2020 day:15 month:01 pages:814-824 extent:11 https://doi.org/10.1016/j.ijbiomac.2019.09.142 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 143 2020 15 0115 814-824 11 |
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10.1016/j.ijbiomac.2019.09.142 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000872.pica (DE-627)ELV049047752 (ELSEVIER)S0141-8130(19)36206-3 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl da Silva Neto, João Xavier verfasserin aut Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. da Costa, Helen Paula Silva oth Vasconcelos, Ilka Maria oth Pereira, Mirella Leite oth Oliveira, Jose Tadeu Abreu oth Lopes, Tiago Deiveson Pereira oth Dias, Lucas Pinheiro oth Araújo, Nadine Monteiro Salgueiro oth Moura, Luiz Francisco Wemmenson Gonçalves oth Van Tilburg, Mauricio Fraga oth Guedes, Maria Izabel Florindo oth Lopes, Larissa Alves oth Morais, Eva Gomes oth de Oliveira Bezerra de Sousa, Daniele oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:143 year:2020 day:15 month:01 pages:814-824 extent:11 https://doi.org/10.1016/j.ijbiomac.2019.09.142 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 143 2020 15 0115 814-824 11 |
| allfields_unstemmed |
10.1016/j.ijbiomac.2019.09.142 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000872.pica (DE-627)ELV049047752 (ELSEVIER)S0141-8130(19)36206-3 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl da Silva Neto, João Xavier verfasserin aut Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. da Costa, Helen Paula Silva oth Vasconcelos, Ilka Maria oth Pereira, Mirella Leite oth Oliveira, Jose Tadeu Abreu oth Lopes, Tiago Deiveson Pereira oth Dias, Lucas Pinheiro oth Araújo, Nadine Monteiro Salgueiro oth Moura, Luiz Francisco Wemmenson Gonçalves oth Van Tilburg, Mauricio Fraga oth Guedes, Maria Izabel Florindo oth Lopes, Larissa Alves oth Morais, Eva Gomes oth de Oliveira Bezerra de Sousa, Daniele oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:143 year:2020 day:15 month:01 pages:814-824 extent:11 https://doi.org/10.1016/j.ijbiomac.2019.09.142 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 143 2020 15 0115 814-824 11 |
| allfieldsGer |
10.1016/j.ijbiomac.2019.09.142 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000872.pica (DE-627)ELV049047752 (ELSEVIER)S0141-8130(19)36206-3 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl da Silva Neto, João Xavier verfasserin aut Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. da Costa, Helen Paula Silva oth Vasconcelos, Ilka Maria oth Pereira, Mirella Leite oth Oliveira, Jose Tadeu Abreu oth Lopes, Tiago Deiveson Pereira oth Dias, Lucas Pinheiro oth Araújo, Nadine Monteiro Salgueiro oth Moura, Luiz Francisco Wemmenson Gonçalves oth Van Tilburg, Mauricio Fraga oth Guedes, Maria Izabel Florindo oth Lopes, Larissa Alves oth Morais, Eva Gomes oth de Oliveira Bezerra de Sousa, Daniele oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:143 year:2020 day:15 month:01 pages:814-824 extent:11 https://doi.org/10.1016/j.ijbiomac.2019.09.142 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 143 2020 15 0115 814-824 11 |
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10.1016/j.ijbiomac.2019.09.142 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000872.pica (DE-627)ELV049047752 (ELSEVIER)S0141-8130(19)36206-3 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl da Silva Neto, João Xavier verfasserin aut Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. da Costa, Helen Paula Silva oth Vasconcelos, Ilka Maria oth Pereira, Mirella Leite oth Oliveira, Jose Tadeu Abreu oth Lopes, Tiago Deiveson Pereira oth Dias, Lucas Pinheiro oth Araújo, Nadine Monteiro Salgueiro oth Moura, Luiz Francisco Wemmenson Gonçalves oth Van Tilburg, Mauricio Fraga oth Guedes, Maria Izabel Florindo oth Lopes, Larissa Alves oth Morais, Eva Gomes oth de Oliveira Bezerra de Sousa, Daniele oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:143 year:2020 day:15 month:01 pages:814-824 extent:11 https://doi.org/10.1016/j.ijbiomac.2019.09.142 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 143 2020 15 0115 814-824 11 |
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da Silva Neto, João Xavier @@aut@@ da Costa, Helen Paula Silva @@oth@@ Vasconcelos, Ilka Maria @@oth@@ Pereira, Mirella Leite @@oth@@ Oliveira, Jose Tadeu Abreu @@oth@@ Lopes, Tiago Deiveson Pereira @@oth@@ Dias, Lucas Pinheiro @@oth@@ Araújo, Nadine Monteiro Salgueiro @@oth@@ Moura, Luiz Francisco Wemmenson Gonçalves @@oth@@ Van Tilburg, Mauricio Fraga @@oth@@ Guedes, Maria Izabel Florindo @@oth@@ Lopes, Larissa Alves @@oth@@ Morais, Eva Gomes @@oth@@ de Oliveira Bezerra de Sousa, Daniele @@oth@@ |
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role of membrane sterol and redox system in the anti-candida activity reported for mo-cbp2, a protein from moringa oleifera seeds |
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Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds |
| abstract |
Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. |
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Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. |
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Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity. |
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Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP2 against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP2 decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP2 also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP2 increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP2 interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H+-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP2 did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP2 as a promising molecule with low toxicity and potent activity. 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