Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host
A central aspect of <i>Brucella</i> pathogenicity is its ability to invade, survive, and replicate in diverse phagocytic and non-phagocytic cell types, leading to chronic infections and chronic inflammatory phenomena. Adhesion to the target cell is a critical first step in the invasion p...
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MDPI AG
2020-11-01
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| Series: | Pathogens |
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| Online Access: | https://www.mdpi.com/2076-0817/9/11/942 |
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| author | Magalí G. Bialer Gabriela Sycz Florencia Muñoz González Mariana C. Ferrero Pablo C. Baldi Angeles Zorreguieta |
| author_facet | Magalí G. Bialer Gabriela Sycz Florencia Muñoz González Mariana C. Ferrero Pablo C. Baldi Angeles Zorreguieta |
| author_sort | Magalí G. Bialer |
| collection | DOAJ |
| description | A central aspect of <i>Brucella</i> pathogenicity is its ability to invade, survive, and replicate in diverse phagocytic and non-phagocytic cell types, leading to chronic infections and chronic inflammatory phenomena. Adhesion to the target cell is a critical first step in the invasion process. Several <i>Brucella</i> adhesins have been shown to mediate adhesion to cells, extracellular matrix components (ECM), or both. These include the sialic acid-binding proteins SP29 and SP41 (binding to erythrocytes and epithelial cells, respectively), the BigA and BigB proteins that contain an Ig-like domain (binding to cell adhesion molecules in epithelial cells), the monomeric autotransporters BmaA, BmaB, and BmaC (binding to ECM components, epithelial cells, osteoblasts, synoviocytes, and trophoblasts), the trimeric autotransporters BtaE and BtaF (binding to ECM components and epithelial cells) and Bp26 (binding to ECM components). An in vivo role has also been shown for the trimeric autotransporters, as deletion mutants display decreased colonization after oral and/or respiratory infection in mice, and it has also been suggested for BigA and BigB. Several adhesins have shown unipolar localization, suggesting that <i>Brucella</i> would express an adhesive pole. Adhesin-based vaccines may be useful to prevent brucellosis, as intranasal immunization in mice with BtaF conferred high levels of protection against oral challenge with <i>B. suis</i>. |
| first_indexed | 2024-03-10T14:54:03Z |
| format | Article |
| id | doaj.art-95cc8a2e66f243e583c10f45821e5dcf |
| institution | Directory Open Access Journal |
| issn | 2076-0817 |
| language | English |
| last_indexed | 2024-03-10T14:54:03Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pathogens |
| spelling | doaj.art-95cc8a2e66f243e583c10f45821e5dcf2023-11-20T20:43:05ZengMDPI AGPathogens2076-08172020-11-0191194210.3390/pathogens9110942Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the HostMagalí G. Bialer0Gabriela Sycz1Florencia Muñoz González2Mariana C. Ferrero3Pablo C. Baldi4Angeles Zorreguieta5Fundación Instituto Leloir (FIL), IIBBA (CONICET-FIL), Buenos Aires 1405, ArgentinaFundación Instituto Leloir (FIL), IIBBA (CONICET-FIL), Buenos Aires 1405, ArgentinaCátedra de Inmunología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires 1113, ArgentinaCátedra de Inmunología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires 1113, ArgentinaCátedra de Inmunología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires 1113, ArgentinaFundación Instituto Leloir (FIL), IIBBA (CONICET-FIL), Buenos Aires 1405, ArgentinaA central aspect of <i>Brucella</i> pathogenicity is its ability to invade, survive, and replicate in diverse phagocytic and non-phagocytic cell types, leading to chronic infections and chronic inflammatory phenomena. Adhesion to the target cell is a critical first step in the invasion process. Several <i>Brucella</i> adhesins have been shown to mediate adhesion to cells, extracellular matrix components (ECM), or both. These include the sialic acid-binding proteins SP29 and SP41 (binding to erythrocytes and epithelial cells, respectively), the BigA and BigB proteins that contain an Ig-like domain (binding to cell adhesion molecules in epithelial cells), the monomeric autotransporters BmaA, BmaB, and BmaC (binding to ECM components, epithelial cells, osteoblasts, synoviocytes, and trophoblasts), the trimeric autotransporters BtaE and BtaF (binding to ECM components and epithelial cells) and Bp26 (binding to ECM components). An in vivo role has also been shown for the trimeric autotransporters, as deletion mutants display decreased colonization after oral and/or respiratory infection in mice, and it has also been suggested for BigA and BigB. Several adhesins have shown unipolar localization, suggesting that <i>Brucella</i> would express an adhesive pole. Adhesin-based vaccines may be useful to prevent brucellosis, as intranasal immunization in mice with BtaF conferred high levels of protection against oral challenge with <i>B. suis</i>.https://www.mdpi.com/2076-0817/9/11/942<i>Brucella</i>adhesinsIg-like domainmonomeric autotransporterstrimeric autotransportersextracellular matrix |
| spellingShingle | Magalí G. Bialer Gabriela Sycz Florencia Muñoz González Mariana C. Ferrero Pablo C. Baldi Angeles Zorreguieta Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host Pathogens <i>Brucella</i> adhesins Ig-like domain monomeric autotransporters trimeric autotransporters extracellular matrix |
| title | Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host |
| title_full | Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host |
| title_fullStr | Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host |
| title_full_unstemmed | Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host |
| title_short | Adhesins of <i>Brucella</i>: Their Roles in the Interaction with the Host |
| title_sort | adhesins of i brucella i their roles in the interaction with the host |
| topic | <i>Brucella</i> adhesins Ig-like domain monomeric autotransporters trimeric autotransporters extracellular matrix |
| url | https://www.mdpi.com/2076-0817/9/11/942 |
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