Abstract
The binding of fibronectin and fibronectin fragments to the enterotoxigenic strain E. coli B34289c was studied. E. coli cells bound to two distinct sites of fibronectin, one being the N-terminal domain, which also contains the binding sites for staphylococci and streptococci, and the other located within the central heparin binding region. In addition, the N-terininal and the heparin binding domain mediated the attachment of bacteria in a solid phase binding assay. E. coli cells expressed two classes of receptors, the first, a 17 kDa protein, recognized by the N-terminal fragment and the second, having a mol. mass of 55 kDa, which interacts with the internal heparin binding domain. Bacterial receptors, which bind the N-terminal end of fibronectin, may be structurally related.
| Original language | English |
|---|---|
| Pages (from-to) | 111-114 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 290 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - Sep 23 1991 |
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Keywords
- Bacterium
- Fibronectin
- Fibronectin fragment
- Receptor
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Cell Biology
- Genetics
- Structural Biology
Cite this
Binding sites in fibronectin for an enterotoxigenic strain of E. coli B342289c. / Visai, Livia; Bozzini, Silvia; Petersen, Torben E.; Speciale, Livianna; Speziale, Pietro.
In: FEBS Letters, Vol. 290, No. 1-2, 23.09.1991, p. 111-114.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding sites in fibronectin for an enterotoxigenic strain of E. coli B342289c
AU - Visai, Livia
AU - Bozzini, Silvia
AU - Petersen, Torben E.
AU - Speciale, Livianna
AU - Speziale, Pietro
PY - 1991/9/23
Y1 - 1991/9/23
N2 - The binding of fibronectin and fibronectin fragments to the enterotoxigenic strain E. coli B34289c was studied. E. coli cells bound to two distinct sites of fibronectin, one being the N-terminal domain, which also contains the binding sites for staphylococci and streptococci, and the other located within the central heparin binding region. In addition, the N-terininal and the heparin binding domain mediated the attachment of bacteria in a solid phase binding assay. E. coli cells expressed two classes of receptors, the first, a 17 kDa protein, recognized by the N-terminal fragment and the second, having a mol. mass of 55 kDa, which interacts with the internal heparin binding domain. Bacterial receptors, which bind the N-terminal end of fibronectin, may be structurally related.
AB - The binding of fibronectin and fibronectin fragments to the enterotoxigenic strain E. coli B34289c was studied. E. coli cells bound to two distinct sites of fibronectin, one being the N-terminal domain, which also contains the binding sites for staphylococci and streptococci, and the other located within the central heparin binding region. In addition, the N-terininal and the heparin binding domain mediated the attachment of bacteria in a solid phase binding assay. E. coli cells expressed two classes of receptors, the first, a 17 kDa protein, recognized by the N-terminal fragment and the second, having a mol. mass of 55 kDa, which interacts with the internal heparin binding domain. Bacterial receptors, which bind the N-terminal end of fibronectin, may be structurally related.
KW - Bacterium
KW - Fibronectin
KW - Fibronectin fragment
KW - Receptor
UR - http://www.scopus.com/inward/record.url?scp=0025850470&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025850470&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(91)81238-4
DO - 10.1016/0014-5793(91)81238-4
M3 - Article
C2 - 1915860
AN - SCOPUS:0025850470
VL - 290
SP - 111
EP - 114
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -