Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus
Bap (biofilm-associated protein) is a 254-kDa staphylococcal surface protein implicated in formation of biofilms by staphylococci isolated from chronic mastitis infections. The presence of potential EF-hand motifs in the amino acid sequence of Bap prompted us to investigate the effect of calcium on...
| Autores principales: | , , , , |
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| Formato: | article |
| Lenguaje: | Inglés |
| Publicado: |
2017
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| Acceso en línea: | http://hdl.handle.net/20.500.11939/4450 |
| _version_ | 1855032122670055424 |
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| author | Arrizubieta, M. J. Toledo-Arana, Alejandro Amorena, B. Penadés, José R. Lasa, Inigo |
| author_browse | Amorena, B. Arrizubieta, M. J. Lasa, Inigo Penadés, José R. Toledo-Arana, Alejandro |
| author_facet | Arrizubieta, M. J. Toledo-Arana, Alejandro Amorena, B. Penadés, José R. Lasa, Inigo |
| author_sort | Arrizubieta, M. J. |
| collection | ReDivia |
| description | Bap (biofilm-associated protein) is a 254-kDa staphylococcal surface protein implicated in formation of biofilms by staphylococci isolated from chronic mastitis infections. The presence of potential EF-hand motifs in the amino acid sequence of Bap prompted us to investigate the effect of calcium on the multicellular behavior of Bap-expressing staphylococci. We found that addition of millimolar amounts of calcium to the growth media inhibited intercellular adhesion of and biofilm formation by Bap-positive strain V329. Addition of manganese, but not addition of magnesium, also inhibited biofilm formation, whereas bacterial aggregation in liquid media was greatly enhanced by metal-chelating agents. In contrast, calcium or chelating agents had virtually no effect on the aggregation of Bap-deficient strain M556. The biofilm elicited by insertion of bap into the chromosome of a biofilm-negative strain exhibited a similar dependence on the calcium concentration, indicating that the observed calcium inhibition was an inherent property of the Bap-mediated biofilms. Site-directed mutagenesis of two of the putative EF-hand domains resulted in a mutant strain that was capable of forming a biofilm but whose biofilm was not inhibited by calcium. Our results indicate that Bap binds Ca2+ with low affinity and that Ca2+ binding renders the protein noncompetent for biofilm formation and for intercellular adhesion. The fact that calcium inhibition of Bap-mediated multicellular behavior takes place in vitro at concentrations similar to those found in milk serum supports the possibility that this inhibition is relevant to the pathogenesis and/or epidemiology of the bacteria in the mastitis process. |
| format | article |
| id | ReDivia4450 |
| institution | Instituto Valenciano de Investigaciones Agrarias (IVIA) |
| language | Inglés |
| publishDate | 2017 |
| publishDateRange | 2017 |
| publishDateSort | 2017 |
| record_format | dspace |
| spelling | ReDivia44502025-04-25T14:43:34Z Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus Arrizubieta, M. J. Toledo-Arana, Alejandro Amorena, B. Penadés, José R. Lasa, Inigo Bap (biofilm-associated protein) is a 254-kDa staphylococcal surface protein implicated in formation of biofilms by staphylococci isolated from chronic mastitis infections. The presence of potential EF-hand motifs in the amino acid sequence of Bap prompted us to investigate the effect of calcium on the multicellular behavior of Bap-expressing staphylococci. We found that addition of millimolar amounts of calcium to the growth media inhibited intercellular adhesion of and biofilm formation by Bap-positive strain V329. Addition of manganese, but not addition of magnesium, also inhibited biofilm formation, whereas bacterial aggregation in liquid media was greatly enhanced by metal-chelating agents. In contrast, calcium or chelating agents had virtually no effect on the aggregation of Bap-deficient strain M556. The biofilm elicited by insertion of bap into the chromosome of a biofilm-negative strain exhibited a similar dependence on the calcium concentration, indicating that the observed calcium inhibition was an inherent property of the Bap-mediated biofilms. Site-directed mutagenesis of two of the putative EF-hand domains resulted in a mutant strain that was capable of forming a biofilm but whose biofilm was not inhibited by calcium. Our results indicate that Bap binds Ca2+ with low affinity and that Ca2+ binding renders the protein noncompetent for biofilm formation and for intercellular adhesion. The fact that calcium inhibition of Bap-mediated multicellular behavior takes place in vitro at concentrations similar to those found in milk serum supports the possibility that this inhibition is relevant to the pathogenesis and/or epidemiology of the bacteria in the mastitis process. 2017-06-01T10:10:10Z 2017-06-01T10:10:10Z 2004 NOV 2004 article Arrizubieta, M.J., Toledo-Arana, A., Amorena, B., Penades, J.R., Lasa, I. (2004). Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus. Journal of Bacteriology, 186(22), 7490-7498. 0021-9193 http://hdl.handle.net/20.500.11939/4450 10.1128/JB.186.22.7490-7498.2004 en openAccess Impreso |
| spellingShingle | Arrizubieta, M. J. Toledo-Arana, Alejandro Amorena, B. Penadés, José R. Lasa, Inigo Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus |
| title | Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus |
| title_full | Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus |
| title_fullStr | Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus |
| title_full_unstemmed | Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus |
| title_short | Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus |
| title_sort | calcium inhibits bap dependent multicellular behavior in staphylococcus aureus |
| url | http://hdl.handle.net/20.500.11939/4450 |
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