Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A
Abstract Background Staphylococcus aureus secretes a variety of proteins including virulence factors that cause diseases. PrsA, encoded by many Gram-positive bacteria, is a membrane-anchored lipoprotein that functions as a foldase to assist in post-translocational folding and helps maintain the stab...
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| Format: | Article |
| Language: | English |
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BMC
2024-04-01
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| Series: | BMC Microbiology |
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| Online Access: | https://doi.org/10.1186/s12866-024-03268-7 |
| _version_ | 1797220035443294208 |
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| author | Mei-Hui Lin Chao-Chin Liu Chiao-Wen Lu Jwu-Ching Shu |
| author_facet | Mei-Hui Lin Chao-Chin Liu Chiao-Wen Lu Jwu-Ching Shu |
| author_sort | Mei-Hui Lin |
| collection | DOAJ |
| description | Abstract Background Staphylococcus aureus secretes a variety of proteins including virulence factors that cause diseases. PrsA, encoded by many Gram-positive bacteria, is a membrane-anchored lipoprotein that functions as a foldase to assist in post-translocational folding and helps maintain the stability of secreted proteins. Our earlier proteomic studies found that PrsA is required for the secretion of protein A, an immunoglobulin-binding protein that contributes to host immune evasion. This study aims to investigate how PrsA influences protein A secretion. Results We found that in comparison with the parental strain HG001, the prsA-deletion mutant HG001ΔprsA secreted less protein A. Deleting prsA also decreased the stability of exported protein A. Pulldown assays indicated that PrsA interacts with protein A in vivo. The domains in PrsA that interact with protein A are mapped to both the N- and C-terminal regions (NC domains). Additionally, the NC domains are essential for promoting PrsA dimerization. Furthermore, an immunoglobulin-binding assay revealed that, compared to the parental strain HG001, fewer immunoglobulins bound to the surface of the mutant strain HG001ΔprsA. Conclusions This study demonstrates that PrsA is critical for the folding and secretion of protein A. The information derived from this study provides a better understanding of virulent protein export pathways that are crucial to the pathogenicity of S. aureus. |
| first_indexed | 2024-04-24T12:43:08Z |
| format | Article |
| id | doaj.art-e954c8f969ed45978437ae204fe695b4 |
| institution | Directory Open Access Journal |
| issn | 1471-2180 |
| language | English |
| last_indexed | 2024-04-24T12:43:08Z |
| publishDate | 2024-04-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Microbiology |
| spelling | doaj.art-e954c8f969ed45978437ae204fe695b42024-04-07T11:10:25ZengBMCBMC Microbiology1471-21802024-04-0124111010.1186/s12866-024-03268-7Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein AMei-Hui Lin0Chao-Chin Liu1Chiao-Wen Lu2Jwu-Ching Shu3Graduate Institute of Medical Biotechnology and Laboratory Science, College of Medicine, Chang Gung UniversityGraduate Institute of Medical Biotechnology and Laboratory Science, College of Medicine, Chang Gung UniversityGraduate Institute of Medical Biotechnology and Laboratory Science, College of Medicine, Chang Gung UniversityGraduate Institute of Medical Biotechnology and Laboratory Science, College of Medicine, Chang Gung UniversityAbstract Background Staphylococcus aureus secretes a variety of proteins including virulence factors that cause diseases. PrsA, encoded by many Gram-positive bacteria, is a membrane-anchored lipoprotein that functions as a foldase to assist in post-translocational folding and helps maintain the stability of secreted proteins. Our earlier proteomic studies found that PrsA is required for the secretion of protein A, an immunoglobulin-binding protein that contributes to host immune evasion. This study aims to investigate how PrsA influences protein A secretion. Results We found that in comparison with the parental strain HG001, the prsA-deletion mutant HG001ΔprsA secreted less protein A. Deleting prsA also decreased the stability of exported protein A. Pulldown assays indicated that PrsA interacts with protein A in vivo. The domains in PrsA that interact with protein A are mapped to both the N- and C-terminal regions (NC domains). Additionally, the NC domains are essential for promoting PrsA dimerization. Furthermore, an immunoglobulin-binding assay revealed that, compared to the parental strain HG001, fewer immunoglobulins bound to the surface of the mutant strain HG001ΔprsA. Conclusions This study demonstrates that PrsA is critical for the folding and secretion of protein A. The information derived from this study provides a better understanding of virulent protein export pathways that are crucial to the pathogenicity of S. aureus.https://doi.org/10.1186/s12866-024-03268-7Staphylococcus aureusFoldasePrsAProtein A |
| spellingShingle | Mei-Hui Lin Chao-Chin Liu Chiao-Wen Lu Jwu-Ching Shu Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A BMC Microbiology Staphylococcus aureus Foldase PrsA Protein A |
| title | Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A |
| title_full | Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A |
| title_fullStr | Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A |
| title_full_unstemmed | Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A |
| title_short | Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A |
| title_sort | staphylococcus aureus foldase prsa contributes to the folding and secretion of protein a |
| topic | Staphylococcus aureus Foldase PrsA Protein A |
| url | https://doi.org/10.1186/s12866-024-03268-7 |
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