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Updated: Jul 6, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Requirements for surface expression and function of adhesin P1 from Streptococcus mutans
Paula J Crowley1, Trevor B Seifert, Ryutaro Isoda
1Department of Oral Biology, University of Florida, Gainesville, FL 32610, USA.
Streptococcus mutans adhesin P1 translocation requires specific structural features and cellular factors like RopA and DnaK. Its maturation and secretion involve complex protein-folding and turnover pathways, including HtrA protease activity.
Area of Science:
- Microbiology
- Molecular Biology
- Protein Biochemistry
Background:
- Streptococcus mutans adhesin P1 is crucial for bacterial adhesion and biofilm formation.
- Understanding P1's translocation and maturation is key to developing strategies against dental caries.
Purpose of the Study:
- To define the requirements for successful translocation and functional maturation of Streptococcus mutans adhesin P1.
- To characterize conformational epitopes of P1 for use as monitoring tools.
- To investigate the roles of cellular factors in P1 processing.
Main Methods:
- Monoclonal antibody characterization
- Analysis of protein structure-function relationships
- Investigating protein-folding and secretion machinery interactions
Main Results:
- P1 localization depends on intramolecular A-P region interaction and cellular factors RopA and DnaK.
- Absence of RopA prevents P1 functional maturation; limited DnaK delays translocation.
- HtrA protease activity is involved in P1 turnover, with substrate-dependent function.
Conclusions:
- Successful P1 translocation and maturation are complex processes influenced by P1 structure and host cell factors.
- Cellular components like RopA, DnaK, and HtrA play critical roles in P1 processing.
- HtrA exhibits adaptable chaperone/protease activity based on P1 structure and cellular conditions.
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