Study of HBP35 Secretion and Glycosylation in Porphyromonas gingivalis
Author Information
Author(s): Shoji Mikio, Sato Keiko, Yukitake Hideharu, Kondo Yoshio, Narita Yuka, Kadowaki Tomoko, Naito Mariko, Nakayama Koji
Primary Institution: Nagasaki University Graduate School of Biomedical Sciences
Hypothesis
HBP35 is translocated to the cell surface via the Por secretion system and is glycosylated with A-LPS.
Conclusion
HBP35 is secreted via the PorSS and glycosylated on the cell surface, with the C-terminal 22 amino acids being crucial for this process.
Supporting Evidence
- HBP35 is translocated to the cell surface via the PorSS.
- The C-terminal 22 amino acids of HBP35 are required for its cell surface localization.
- Glycosylation of HBP35 occurs after the removal of its C-terminal domain.
Takeaway
The study shows that a protein called HBP35 in a type of bacteria is moved to the surface and modified in a specific way, which is important for how the bacteria work.
Methodology
The study involved immunoblot analysis, deletion analysis, and GFP fusion studies to investigate the secretion and glycosylation mechanisms.
Digital Object Identifier (DOI)
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