<i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein
The spirochete, <i>Borrelia burgdorferi</i>, has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host. Some of these proteins also serve different roles in infection and dissemination of the spirochete in the mammalian ho...
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| Format: | Article |
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MDPI AG
2021-02-01
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| Series: | Pathogens |
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| Online Access: | https://www.mdpi.com/2076-0817/10/2/226 |
| _version_ | 1797396039528873984 |
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| author | Thomas Cafiero Alvaro Toledo |
| author_facet | Thomas Cafiero Alvaro Toledo |
| author_sort | Thomas Cafiero |
| collection | DOAJ |
| description | The spirochete, <i>Borrelia burgdorferi</i>, has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host. Some of these proteins also serve different roles in infection and dissemination of the spirochete in the mammalian host. In this spirochete, a number of proteins have been associated with binding to plasminogen or components of the extracellular matrix, which is important for tissue colonization and dissemination. GroEL is a cytoplasmic chaperone protein that has previously been associated with the outer membrane of <i>Borrelia.</i> A His-tag purified <i>B. burgdorferi</i> GroEL was used to generate a polyclonal rabbit antibody showing that GroEL also localizes in the outer membrane and is surface exposed. GroEL binds plasminogen in a lysine dependent manner. GroEL may be part of the protein repertoire that <i>Borrelia</i> successfully uses to establish infection and disseminate in the host. Importantly, this chaperone is readily recognized by sera from experimentally infected mice and rabbits. In summary, GroEL is an immunogenic protein that in addition to its chaperon role it may contribute to pathogenesis of the spirochete by binding to plasminogen and components of the extra cellular matrix. |
| first_indexed | 2024-03-09T00:45:32Z |
| format | Article |
| id | doaj.art-475e38fa40d347789ab08a67dc2727c4 |
| institution | Directory Open Access Journal |
| issn | 2076-0817 |
| language | English |
| last_indexed | 2024-03-09T00:45:32Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pathogens |
| spelling | doaj.art-475e38fa40d347789ab08a67dc2727c42023-12-11T17:32:47ZengMDPI AGPathogens2076-08172021-02-0110222610.3390/pathogens10020226<i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional ProteinThomas Cafiero0Alvaro Toledo1Department of Entomology, Rutgers University, New Brunswick, NJ 08901, USADepartment of Entomology, Rutgers University, New Brunswick, NJ 08901, USAThe spirochete, <i>Borrelia burgdorferi</i>, has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host. Some of these proteins also serve different roles in infection and dissemination of the spirochete in the mammalian host. In this spirochete, a number of proteins have been associated with binding to plasminogen or components of the extracellular matrix, which is important for tissue colonization and dissemination. GroEL is a cytoplasmic chaperone protein that has previously been associated with the outer membrane of <i>Borrelia.</i> A His-tag purified <i>B. burgdorferi</i> GroEL was used to generate a polyclonal rabbit antibody showing that GroEL also localizes in the outer membrane and is surface exposed. GroEL binds plasminogen in a lysine dependent manner. GroEL may be part of the protein repertoire that <i>Borrelia</i> successfully uses to establish infection and disseminate in the host. Importantly, this chaperone is readily recognized by sera from experimentally infected mice and rabbits. In summary, GroEL is an immunogenic protein that in addition to its chaperon role it may contribute to pathogenesis of the spirochete by binding to plasminogen and components of the extra cellular matrix.https://www.mdpi.com/2076-0817/10/2/226<i>Borrelia burgdorferi</i>Lyme diseaseGroELMoonlight protein |
| spellingShingle | Thomas Cafiero Alvaro Toledo <i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein Pathogens <i>Borrelia burgdorferi</i> Lyme disease GroEL Moonlight protein |
| title | <i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein |
| title_full | <i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein |
| title_fullStr | <i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein |
| title_full_unstemmed | <i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein |
| title_short | <i>Borrelia burgdorferi</i> Surface Exposed GroEL Is a Multifunctional Protein |
| title_sort | i borrelia burgdorferi i surface exposed groel is a multifunctional protein |
| topic | <i>Borrelia burgdorferi</i> Lyme disease GroEL Moonlight protein |
| url | https://www.mdpi.com/2076-0817/10/2/226 |
| work_keys_str_mv | AT thomascafiero iborreliaburgdorferiisurfaceexposedgroelisamultifunctionalprotein AT alvarotoledo iborreliaburgdorferiisurfaceexposedgroelisamultifunctionalprotein |