Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?
Bacterial proteins exhibiting two or more unrelated functions, referred to as moonlighting proteins, are suggested to contribute to full virulence manifestation in pathogens. An expanding number of published studies have revealed the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH)...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2020-03-01
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| Series: | Frontiers in Cellular and Infection Microbiology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fcimb.2020.00089/full |
| _version_ | 1818922026694344704 |
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| author | Monika Kopeckova Ivona Pavkova Jiri Stulik |
| author_facet | Monika Kopeckova Ivona Pavkova Jiri Stulik |
| author_sort | Monika Kopeckova |
| collection | DOAJ |
| description | Bacterial proteins exhibiting two or more unrelated functions, referred to as moonlighting proteins, are suggested to contribute to full virulence manifestation in pathogens. An expanding number of published studies have revealed the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to be a multitasking protein with virulence impact in a number of pathogenic bacteria. This protein can be detected on the bacterial surface or outside the bacterial cell, where it interacts with host proteins. In this way, GAPDH is able to modulate various pathogenic processes. Moreover, it has been shown to be involved in non-enzymatic processes inside the bacterial cell. In this mini review, we summarize main findings concerning the multiple localization and protein interactions of GAPDH derived from bacterial pathogens of humans. We also briefly discuss problems associated with using GAPDH as a vaccine antigen and endeavor to inspire further research to fill gaps in the existing knowledge. |
| first_indexed | 2024-12-20T01:47:00Z |
| format | Article |
| id | doaj.art-8a3a0e5380584678ad236a4c0d612c6d |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-12-20T01:47:00Z |
| publishDate | 2020-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-8a3a0e5380584678ad236a4c0d612c6d2022-12-21T19:57:43ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882020-03-011010.3389/fcimb.2020.00089519858Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?Monika KopeckovaIvona PavkovaJiri StulikBacterial proteins exhibiting two or more unrelated functions, referred to as moonlighting proteins, are suggested to contribute to full virulence manifestation in pathogens. An expanding number of published studies have revealed the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to be a multitasking protein with virulence impact in a number of pathogenic bacteria. This protein can be detected on the bacterial surface or outside the bacterial cell, where it interacts with host proteins. In this way, GAPDH is able to modulate various pathogenic processes. Moreover, it has been shown to be involved in non-enzymatic processes inside the bacterial cell. In this mini review, we summarize main findings concerning the multiple localization and protein interactions of GAPDH derived from bacterial pathogens of humans. We also briefly discuss problems associated with using GAPDH as a vaccine antigen and endeavor to inspire further research to fill gaps in the existing knowledge.https://www.frontiersin.org/article/10.3389/fcimb.2020.00089/fullglyceraldehyde-3-phosphate dehydrogenasepathogenic bacteriaprotein-protein interaction (PPI)moonlighting proteinslocalization |
| spellingShingle | Monika Kopeckova Ivona Pavkova Jiri Stulik Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality? Frontiers in Cellular and Infection Microbiology glyceraldehyde-3-phosphate dehydrogenase pathogenic bacteria protein-protein interaction (PPI) moonlighting proteins localization |
| title | Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality? |
| title_full | Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality? |
| title_fullStr | Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality? |
| title_full_unstemmed | Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality? |
| title_short | Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality? |
| title_sort | diverse localization and protein binding abilities of glyceraldehyde 3 phosphate dehydrogenase in pathogenic bacteria the key to its multifunctionality |
| topic | glyceraldehyde-3-phosphate dehydrogenase pathogenic bacteria protein-protein interaction (PPI) moonlighting proteins localization |
| url | https://www.frontiersin.org/article/10.3389/fcimb.2020.00089/full |
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