Sandbox Reserved 1561
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
== Function(s) and Biological Relevance == | == Function(s) and Biological Relevance == | ||
| - | Bap1 (Biofilm-Associated protein 1) is an extracellular matrix protein from the bacterium Vibrio cholerae that aids in biofilm architecture and adhesion affinity to living surfaces. <scene name='82/823085/6mlt_cartoon_view/2'>6MLT Cartoon View</scene> Bap1 is also responsible for the biofilm resistance to aqueous environments, acid conditions, antibiotics and the human immune system making the V. cholerae biofilm very versatile and difficult to eradicate. Vibrio cholerae biofilms are made up of Vibrio polysaccharides, nucleic acids and matrix proteins RBmA, RbmC, and Bap1. V. cholerae biofilms are linked to increased transmission, virulence and resistance to various environments, which resulted in pandemic cholera. The biofilm resistance and adhesion affinity promote survival in a multitude of environments including mammalian stomachs. The increased resistance and adhesion affinity increase the virulence of the bacterium resulting in a greater probability of contraction, infection and disease. = Broader Implications == | + | Bap1 (Biofilm-Associated protein 1) is an extracellular matrix protein from the bacterium Vibrio cholerae that aids in biofilm architecture and adhesion affinity to living surfaces. <scene name='82/823085/6mlt_cartoon_view/2'>6MLT Cartoon View</scene> Bap1 is also responsible for the biofilm resistance to aqueous environments, acid conditions, antibiotics and the human immune system making the V. cholerae biofilm very versatile and difficult to eradicate. Vibrio cholerae biofilms are made up of Vibrio polysaccharides, nucleic acids and matrix proteins RBmA, RbmC, and Bap1. V. cholerae biofilms are linked to increased transmission, virulence and resistance to various environments, which resulted in pandemic cholera. The biofilm resistance and adhesion affinity promote survival in a multitude of environments including mammalian stomachs. The increased resistance and adhesion affinity increase the virulence of the bacterium resulting in a greater probability of contraction, infection and disease. |
| + | = Broader Implications == | ||
== Structural highlights and structure-function relationships == | == Structural highlights and structure-function relationships == | ||
Revision as of 18:36, 1 December 2019
| This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575. |
To get started:
More help: Help:Editing |
Bap1 from Vibrio cholera plays a crucial role in biofilm binding affinity
| |||||||||||
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
