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פותח על ידי קלירמאש פתרונות בע"מ -
Recognitory bacterial surface lectins which mediate its mannose‐specific adherence to eukaryotic cells
Year:
1984
Source of publication :
Biology of the Cell
Authors :
אשדת, יובל
;
.
Volume :
51
Co-Authors:
Eshdat, Y.
Sharon, N.
Facilitators :
From page:
259
To page:
266
(
Total pages:
8
)
Abstract:
Cell surface protein were found to play a role in the sugar‐specific molecular mechanism by which bacteria adhere to mammalian cells. We have demonstrated that at least three different types of lectin‐like proteins mediate the mannose‐sensitive adherence of gram negative bacteria to epithelial cells. One group of such lectins was shown in our study to be associated with the bacterial flagellum. Flagella isolated from Escherichia coli 7343 and Serratia marcescens 8347 exhibited mannose‐sensitive agglutination of yeast cells; however, the flagella of the two bacteria differ in the molecular structure of their protein subunits. Another class of lectins comprises the bacterial fimbriae (also known as type 1 pili), which were previously shown to facilitate the mannose‐sensitive adherence of various bacteria to mammalian cells. Fimbriae isolated from E. coli 346 were reversibly dissociated by saturated guanidine hydrochloride to their protein subunits. The dissociated subunits retained in part their mannose‐binding ability, and were reassembled into fimbriae‐like structures by removal of the denaturant under specific conditions. Mannose‐sensitive yeast agglutinating activity of E. coli 2699, as well as of its isolated outer membranes devoid of fimbriae or flagella, was abolished by pretreatment with trypsin. It is therefore believed that the mannose‐sensitive adherence of these bacteria is mediated also by lectin‐like proteins associated directly with the outer membrane. 1984 Société Française des Microscopies and Société Biologie Cellulaire de France
Note:
Related Files :
Animal
bacteria
Cell Adhesion
cell membrane
fungi
Histology
human cell
עוד תגיות
תוכן קשור
More details
DOI :
10.1111/j.1768-322X.1984.tb00307.x
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19513
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:29
Scientific Publication
Recognitory bacterial surface lectins which mediate its mannose‐specific adherence to eukaryotic cells
51
Eshdat, Y.
Sharon, N.
Recognitory bacterial surface lectins which mediate its mannose‐specific adherence to eukaryotic cells
Cell surface protein were found to play a role in the sugar‐specific molecular mechanism by which bacteria adhere to mammalian cells. We have demonstrated that at least three different types of lectin‐like proteins mediate the mannose‐sensitive adherence of gram negative bacteria to epithelial cells. One group of such lectins was shown in our study to be associated with the bacterial flagellum. Flagella isolated from Escherichia coli 7343 and Serratia marcescens 8347 exhibited mannose‐sensitive agglutination of yeast cells; however, the flagella of the two bacteria differ in the molecular structure of their protein subunits. Another class of lectins comprises the bacterial fimbriae (also known as type 1 pili), which were previously shown to facilitate the mannose‐sensitive adherence of various bacteria to mammalian cells. Fimbriae isolated from E. coli 346 were reversibly dissociated by saturated guanidine hydrochloride to their protein subunits. The dissociated subunits retained in part their mannose‐binding ability, and were reassembled into fimbriae‐like structures by removal of the denaturant under specific conditions. Mannose‐sensitive yeast agglutinating activity of E. coli 2699, as well as of its isolated outer membranes devoid of fimbriae or flagella, was abolished by pretreatment with trypsin. It is therefore believed that the mannose‐sensitive adherence of these bacteria is mediated also by lectin‐like proteins associated directly with the outer membrane. 1984 Société Française des Microscopies and Société Biologie Cellulaire de France
Scientific Publication
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