The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin
<i>Streptococcus pneumoniae</i> causes otitis media, sinusitis, and serious diseases such as pneumonia and bacteremia. However, the in vivo dynamics of <i>S. pneumoniae</i> infections and disease severity are not fully understood. In this study, we investigated pneumococcal p...
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| Format: | Article |
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MDPI AG
2023-12-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/11/12/2969 |
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| author | Yoshihito Yasui Satoru Hirayama Takumi Hiyoshi Toshihito Isono Hisanori Domon Tomoki Maekawa Koichi Tabeta Yutaka Terao |
| author_facet | Yoshihito Yasui Satoru Hirayama Takumi Hiyoshi Toshihito Isono Hisanori Domon Tomoki Maekawa Koichi Tabeta Yutaka Terao |
| author_sort | Yoshihito Yasui |
| collection | DOAJ |
| description | <i>Streptococcus pneumoniae</i> causes otitis media, sinusitis, and serious diseases such as pneumonia and bacteremia. However, the in vivo dynamics of <i>S. pneumoniae</i> infections and disease severity are not fully understood. In this study, we investigated pneumococcal proteins detected in the bronchoalveolar lavage fluid of an <i>S. pneumoniae</i>-infected mouse, which were assumed to be expressed during infection. Analysis of three proteins with unknown infection-related functions revealed that recombinant Fe-S cluster assembly ATP-binding protein (SufC) binds to the host plasminogen and promotes its conversion into plasmin. SufC was detected in the bacterial cell-surface protein fraction, but it had no extracellular secretory signal. This study suggests that <i>S. pneumoniae</i> releases SufC extracellularly through LytA-dependent autolysis, binding to the bacterial cell surface and host plasminogen and promoting its conversion into plasmin. The recruitment of plasmin by <i>S. pneumoniae</i> is considered useful for bacterial survival and spread, and SufC is suggested to facilitate this process. |
| first_indexed | 2024-03-08T20:30:37Z |
| format | Article |
| id | doaj.art-188916d16dc5469192031a3db61a9578 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-08T20:30:37Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-188916d16dc5469192031a3db61a95782023-12-22T14:26:15ZengMDPI AGMicroorganisms2076-26072023-12-011112296910.3390/microorganisms11122969The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into PlasminYoshihito Yasui0Satoru Hirayama1Takumi Hiyoshi2Toshihito Isono3Hisanori Domon4Tomoki Maekawa5Koichi Tabeta6Yutaka Terao7Division of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Periodontology, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, JapanDivision of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8514, Japan<i>Streptococcus pneumoniae</i> causes otitis media, sinusitis, and serious diseases such as pneumonia and bacteremia. However, the in vivo dynamics of <i>S. pneumoniae</i> infections and disease severity are not fully understood. In this study, we investigated pneumococcal proteins detected in the bronchoalveolar lavage fluid of an <i>S. pneumoniae</i>-infected mouse, which were assumed to be expressed during infection. Analysis of three proteins with unknown infection-related functions revealed that recombinant Fe-S cluster assembly ATP-binding protein (SufC) binds to the host plasminogen and promotes its conversion into plasmin. SufC was detected in the bacterial cell-surface protein fraction, but it had no extracellular secretory signal. This study suggests that <i>S. pneumoniae</i> releases SufC extracellularly through LytA-dependent autolysis, binding to the bacterial cell surface and host plasminogen and promoting its conversion into plasmin. The recruitment of plasmin by <i>S. pneumoniae</i> is considered useful for bacterial survival and spread, and SufC is suggested to facilitate this process.https://www.mdpi.com/2076-2607/11/12/2969<i>Streptococcus pneumoniae</i>plasminogenplasminautolysinSufC |
| spellingShingle | Yoshihito Yasui Satoru Hirayama Takumi Hiyoshi Toshihito Isono Hisanori Domon Tomoki Maekawa Koichi Tabeta Yutaka Terao The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin Microorganisms <i>Streptococcus pneumoniae</i> plasminogen plasmin autolysin SufC |
| title | The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin |
| title_full | The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin |
| title_fullStr | The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin |
| title_full_unstemmed | The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin |
| title_short | The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin |
| title_sort | pneumococcal protein sufc binds to host plasminogen and promotes its conversion into plasmin |
| topic | <i>Streptococcus pneumoniae</i> plasminogen plasmin autolysin SufC |
| url | https://www.mdpi.com/2076-2607/11/12/2969 |
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