Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6
<i>Candida albicans</i> and other closely related pathogenic yeast-like fungi carry on their surface numerous loosely adsorbed “moonlighting proteins”—proteins that play evolutionarily conserved intracellular functions but also appear on the cell surface and exhibit additional functions,...
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2024-01-01
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| author | Aneta Bednarek Dorota Satala Marcin Zawrotniak Angela H. Nobbs Maria Rapala-Kozik Andrzej Kozik |
| author_facet | Aneta Bednarek Dorota Satala Marcin Zawrotniak Angela H. Nobbs Maria Rapala-Kozik Andrzej Kozik |
| author_sort | Aneta Bednarek |
| collection | DOAJ |
| description | <i>Candida albicans</i> and other closely related pathogenic yeast-like fungi carry on their surface numerous loosely adsorbed “moonlighting proteins”—proteins that play evolutionarily conserved intracellular functions but also appear on the cell surface and exhibit additional functions, e.g., contributing to attachment to host tissues. In the current work, we characterized this “moonlighting” role for glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) of <i>C. albicans</i> and <i>Nakaseomyces glabratus</i>. GAPDH was directly visualized on the cell surface of both species and shown to play a significant part in the total capacity of fungal cells to bind two selected human host proteins—vitronectin and plasminogen. Using purified proteins, both host proteins were found to tightly interact with GAPDH, with dissociation constants in an order of 10<sup>−8</sup> M, as determined by bio-layer interferometry and surface plasmon resonance measurements. It was also shown that exogenous GAPDH tightly adheres to the surface of candidal cells, suggesting that the cell surface location of this moonlighting protein may partly result from the readsorption of its soluble form, which may be present at an infection site (e.g., due to release from dying fungal cells). The major dedicated adhesins, covalently bound to the cell wall—agglutinin-like sequence protein 3 (Als3) and epithelial adhesin 6 (Epa6)—were suggested to serve as the docking platforms for GAPDH in <i>C. albicans</i> and <i>N. glabratus</i>, respectively. |
| first_indexed | 2024-03-08T09:53:32Z |
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| language | English |
| last_indexed | 2024-03-08T09:53:32Z |
| publishDate | 2024-01-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-1755cee4220040699b00175bcf1814902024-01-29T13:56:19ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-01-01252101310.3390/ijms25021013Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6Aneta Bednarek0Dorota Satala1Marcin Zawrotniak2Angela H. Nobbs3Maria Rapala-Kozik4Andrzej Kozik5Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, PolandDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, PolandDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, PolandBristol Dental School Research Laboratories, University of Bristol, Dorothy Hodgkin Building, Whitson Street, Bristol BS1 3NY, UKDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, PolandDepartment of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland<i>Candida albicans</i> and other closely related pathogenic yeast-like fungi carry on their surface numerous loosely adsorbed “moonlighting proteins”—proteins that play evolutionarily conserved intracellular functions but also appear on the cell surface and exhibit additional functions, e.g., contributing to attachment to host tissues. In the current work, we characterized this “moonlighting” role for glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) of <i>C. albicans</i> and <i>Nakaseomyces glabratus</i>. GAPDH was directly visualized on the cell surface of both species and shown to play a significant part in the total capacity of fungal cells to bind two selected human host proteins—vitronectin and plasminogen. Using purified proteins, both host proteins were found to tightly interact with GAPDH, with dissociation constants in an order of 10<sup>−8</sup> M, as determined by bio-layer interferometry and surface plasmon resonance measurements. It was also shown that exogenous GAPDH tightly adheres to the surface of candidal cells, suggesting that the cell surface location of this moonlighting protein may partly result from the readsorption of its soluble form, which may be present at an infection site (e.g., due to release from dying fungal cells). The major dedicated adhesins, covalently bound to the cell wall—agglutinin-like sequence protein 3 (Als3) and epithelial adhesin 6 (Epa6)—were suggested to serve as the docking platforms for GAPDH in <i>C. albicans</i> and <i>N. glabratus</i>, respectively.https://www.mdpi.com/1422-0067/25/2/1013<i>Candida albicans</i><i>Nakaseomyces glabratus</i>moonlighting proteinsglyceraldehyde 3-phosphate dehydrogenasevitronectinplasminogen |
| spellingShingle | Aneta Bednarek Dorota Satala Marcin Zawrotniak Angela H. Nobbs Maria Rapala-Kozik Andrzej Kozik Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6 International Journal of Molecular Sciences <i>Candida albicans</i> <i>Nakaseomyces glabratus</i> moonlighting proteins glyceraldehyde 3-phosphate dehydrogenase vitronectin plasminogen |
| title | Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6 |
| title_full | Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6 |
| title_fullStr | Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6 |
| title_full_unstemmed | Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6 |
| title_short | Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface of <i>Candida albicans</i> and <i>Nakaseomyces glabratus</i> Cells—A Moonlighting Protein That Binds Human Vitronectin and Plasminogen and Can Adsorb to Pathogenic Fungal Cells via Major Adhesins Als3 and Epa6 |
| title_sort | glyceraldehyde 3 phosphate dehydrogenase on the surface of i candida albicans i and i nakaseomyces glabratus i cells a moonlighting protein that binds human vitronectin and plasminogen and can adsorb to pathogenic fungal cells via major adhesins als3 and epa6 |
| topic | <i>Candida albicans</i> <i>Nakaseomyces glabratus</i> moonlighting proteins glyceraldehyde 3-phosphate dehydrogenase vitronectin plasminogen |
| url | https://www.mdpi.com/1422-0067/25/2/1013 |
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