Sandbox Reserved 1628
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{{Sandbox_Reserved_BHall_F20}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_F20}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
- | == | + | ==Epithelial Adhesin 1A== |
- | <StructureSection load='4af9' size='340' side='right' caption=' | + | <StructureSection load='4af9' size='340' side='right' caption='EpaA in a complex with Galb1-3Glc' scene=''> |
- | + | Adhesins, commonly found on the surface of bacteria, aid in binding or adhering the bacteria to other cells. This is normally the beginning of an infection as the bacteria can bind to a host cell and potentially start a cascade of events within the host cell that leads to the bacteria invading<ref>PMID:9973330</ref>. Various bacteria have various types of adhesin proteins, but this page looks specifically at epithelial adhesins, particularly one found in ''Candida glabrata'' which causes infections most often in immunosuppressed patients<ref>PMID:9880475</ref> and can lead to deadly bloodstream infections. | |
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Revision as of 00:43, 8 December 2020
This Sandbox is Reserved from 09/18/2020 through 03/20/2021 for use in CHEM 351 Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, IA. This reservation includes Sandbox Reserved 1628 through Sandbox Reserved 1642. |
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Epithelial Adhesin 1A
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References
- ↑ Soto GE, Hultgren SJ. Bacterial adhesins: common themes and variations in architecture and assembly. J Bacteriol. 1999 Feb;181(4):1059-71. doi: 10.1128/JB.181.4.1059-1071.1999. PMID:9973330 doi:http://dx.doi.org/10.1128/JB.181.4.1059-1071.1999
- ↑ Fidel PL Jr, Vazquez JA, Sobel JD. Candida glabrata: review of epidemiology, pathogenesis, and clinical disease with comparison to C. albicans. Clin Microbiol Rev. 1999 Jan;12(1):80-96. PMID:9880475
- ↑ Hoffmann D, Diderrich R, Reithofer V, Friederichs S, Kock M, Essen LO, Mosch HU. Functional reprogramming of Candida glabrata epithelial adhesins: the role of conserved and variable structural motifs in ligand binding. J Biol Chem. 2020 Jul 15. pii: RA120.013968. doi: 10.1074/jbc.RA120.013968. PMID:32669365 doi:http://dx.doi.org/10.1074/jbc.RA120.013968