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• W2021837034 abstract "Abstract Background : The Gram-negative bacterium Porphyromonas gingivalis is considered as the etiologic agent of chronic periodontitis. P. gingivalis secretes C-terminal domain (CTD) proteins. CTD proteins pass through the outer membrane via the Por secretion system, undergo post-translational glycosylation by attaching deacylated anionic-lipopolysaccharide (A-LPS), and anchor the outer cell membrane and/or to the extracellular vesicles. These secretion and modification steps vary depending on the different CTD proteins but, in all cases, the CTDs of mature CTD proteins, except for the CTD signal peptidase, are removed. Since CTD proteins such as gingipains are known virulence factors of P. gingivalis , the mechanism of secretion and modification of CTD proteins needs to be elucidated. Highlight : Recent genetic studies have identified the genes essential for the secretion and modification of CTD proteins. Of particular interest is the functional role of each component; however, this issue is not easy to address. Recently, reports on PG0026 and PG27/LptO in the modification system have been published. PG0026 has been proposed as the CTD signal peptidase, while PG27 is an outer membrane protein consisting of a beta-barrel structure, and is bifunctional in the deacylation of A-LPS as LptO and in anchoring PG0026 and HagA to the cell surface. Conclusion : These findings describe the assembly and function of PG27/LptO, PG0026, and HagA." @default.
• W2021837034 created "2016-06-24" @default.
• W2021837034 creator A5013025234 @default.
• W2021837034 creator A5076294672 @default.
• W2021837034 date "2014-11-01" @default.
• W2021837034 modified "2023-09-27" @default.
• W2021837034 title "Assembly and function of PG27/LptO, PG0026, and HagA in the secretion and modification system of C-terminal domain proteins" @default.
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• W2021837034 doi "https://doi.org/10.1016/j.job.2014.07.001" @default.
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