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Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells
Year:
1998
Source of publication :
Journal of Infectious Diseases
Authors :
Sela, Shlomo
;
.
Volume :
178
Co-Authors:
Jadoun, J.
Ozeri, V.
Burstein, E.
Skutelsky, E.
Hanski, E.
Sela, S., Dept. of Human Microbiology, Sackler School of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel
Facilitators :
From page:
147
To page:
148
(
Total pages:
2
)
Abstract:
It was recently reported that strains of Streptococcus pyogenes are capable of inducing entry of the bacterium into epithelial cells; however, nothing is known regarding the gene(s) and the underlying mechanism(s) involved. Using isogenic mutants of S. pyogenes JRS4 strain that are defective in the expression of each of the surface proteins F1 and M6, it was demonstrated that both are required for efficient internalization. Expression of F1 on the surface of a poorly invading S. pyogenes strain significantly enhances its internalization efficiency. Protein F1-mediated internalization is inhibited by UR, the nonrepetitive fibronectin-binding domain of this protein, and to a lesser extent, by the repetitive fibronectin-binding domain, RD2. Polyclonal anti-human fibronectin antibodies completely abolish F1-mediated internalization; increasing fibronectin concentrations result in a significant enhancement of bacterial uptake. The findings shown here suggest that protein F1 mediates streptococcal internalization and that the M6 protein is required for more efficient entry of the bacterium.
Note:
Related Files :
Bacterial Outer Membrane Proteins
epithelium cell
human cell
Plasmid
unclassified drug
Show More
Related Content
More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
24147
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:05
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Scientific Publication
Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells
178
Jadoun, J.
Ozeri, V.
Burstein, E.
Skutelsky, E.
Hanski, E.
Sela, S., Dept. of Human Microbiology, Sackler School of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel
Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells
It was recently reported that strains of Streptococcus pyogenes are capable of inducing entry of the bacterium into epithelial cells; however, nothing is known regarding the gene(s) and the underlying mechanism(s) involved. Using isogenic mutants of S. pyogenes JRS4 strain that are defective in the expression of each of the surface proteins F1 and M6, it was demonstrated that both are required for efficient internalization. Expression of F1 on the surface of a poorly invading S. pyogenes strain significantly enhances its internalization efficiency. Protein F1-mediated internalization is inhibited by UR, the nonrepetitive fibronectin-binding domain of this protein, and to a lesser extent, by the repetitive fibronectin-binding domain, RD2. Polyclonal anti-human fibronectin antibodies completely abolish F1-mediated internalization; increasing fibronectin concentrations result in a significant enhancement of bacterial uptake. The findings shown here suggest that protein F1 mediates streptococcal internalization and that the M6 protein is required for more efficient entry of the bacterium.
Scientific Publication
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