+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

An antibody that inhibits the binding of diphtheria toxin to cells revealed the association of a 27-kDa membrane protein with the diphtheria toxin receptor



An antibody that inhibits the binding of diphtheria toxin to cells revealed the association of a 27-kDa membrane protein with the diphtheria toxin receptor



Journal of Biological Chemistry 266(30): 20463



A monoclonal antibody that blocks the binding of diphtheria toxin to Vero cells was isolated by immunizing mice with Vero cell membrane. The antibody inhibits the binding of diphtheria toxin and also CRM197, a mutant form of diphtheria toxin, to Vero cells, and consequently inhibits the cytotoxicity of diphtheria toxin. This antibody does not directly react with the receptor molecule of diphtheria toxin (DTR14.5). Immunoprecipitation and immunoblotting studies revealed that this antibody binds to a novel membrane protein of 27 kDa (DRAP27). When diphtheria toxin receptor was passed through an affinity column made with this antibody, the receptor was trapped only in the presence of DRAP27. These results indicate that DRAP27 and DTR14.5 closely associate in Vero cell membrane and that the inhibition of the binding of diphtheria toxin to the receptor is due to the binding of the antibody to the DRAP27 molecule. Binding studies using 125I-labeled antibody showed that there are many more molecules of DRAP27 on the cell surface than diphtheria toxin-binding sites. However, there is a correlation between the sensitivity of a cell line to diphtheria toxin and the number of DRAP27 molecules on the cell surface, suggesting that DRAP27 is involved in the entry of diphtheria toxin into the target cell.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 039239359

Download citation: RISBibTeXText

PMID: 1939101


Related references

Identification of diphtheria toxin receptor and a non protein diphtheria toxin binding molecule in vero cell membrane. Journal of Cell Biology 107(2): 511-520, 1988

Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity. Embo Journal 13(10): 2322-2330, 1994

Heparin-binding EGF-like growth factor, which acts as diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity. The EMBO Journal 13: 22-30, 1994

Identification of diphtheria toxin receptor and a nonproteinous diphtheria toxin-binding molecule in Vero cell membrane. Journal of Cell Biology 107(2): 511-519, 1988

Identification of Diphtheria Toxin Receptor and a Nonproteinous Diphtheria Toxin-Binding Molecule in Vero Cell Membrane. The Journal of Cell Biology 107(2): 511-519, 1988

Diphtheria toxin receptor and a nonproteinaceous diphtheria toxin binding molecule in cell membrane. Zentralblatt fuer Bakteriologie Suppl. 19: 241-248, 1990

Co-expression of diphtheria toxin receptor and DRAP27 in mouse L cells DRAP27 elevates the number of diphtheria toxin receptors on the cell surface but not changes the binding affinity for the toxin. Freer, J , Aitken, R , Alouf, J E , Boulnois, G FEMS Symposium; Bacterial protein toxins 519-520, 1994

Diphtheria toxin receptor. Identification of specific diphtheria toxin-binding proteins on the surface of Vero and BS-C-1 cells. Journal of Biological Chemistry 262(27): 13246-13253, 1987

Construction of a diphtheria toxin A fragment-C180 peptide fusion protein which elicits a neutralizing antibody response against diphtheria toxin and pertussis toxin. Infection and Immunity 60(12): 5071-5077, 1992

The 27-kD Diphtheria Toxin Receptor-Associated Protein (Drap27) from Vero Cells Is the Monkey Homologue of Human Cd9 Antigen: Expression of Drap27 Elevates the Number of Diphtheria Toxin Receptors on Toxin-Sensitive Cells. The Journal of Cell Biology 118(6): 1389-1399, 1992

The 27 kd diphtheria toxin receptor associated protein drap27 from vero cells is the monkey homologue of human cd9 antigen expression of drap27 elevates the number of diphtheria toxin receptors on toxin sensitive cells. Journal of Cell Biology 118(6): 1389-1399, 1992

Role of the heparin-binding domain on the binding of diphtheria toxin to the diphtheria toxin receptor/membrane-anchored heparin-binding EGF-like growth factor. Cell Structure and Function 21(6): 614, 1996

Diphtheria toxin receptor binding domain substitution with interleukin-2: genetic construction and properties of a diphtheria toxin-related interleukin-2 fusion protein. Protein Engineering 1(6): 493-498, 1987

Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity. Journal of Biological Chemistry 270(3): 1015-1019, 1995

Localization of a critical diphtheria toxin-binding domain to the C-terminus of the mature heparin-binding EGF-like growth factor region of the diphtheria toxin receptor. Biochemical and Biophysical Research Communications 206(2): 710-717, 1995