Diphtheria toxin-binding glycoproteins on hamster cells: candidates for diphtheria toxin receptors

Diphtheria toxin-binding glycoproteins of high molecular weight (greater than 100,000) were identified on the surface of lymph node and thymus cells from hamsters, a diphtheria toxin-sensitive species. These diphtheria toxin-binding glycoproteins also interacted with CRM197 protein, which possesses toxin-blocking activity, but not with diphtheria toxoid, fragment A of diphtheria toxin, or cholera toxin, all of which lack toxin-blocking activity. These observations are consistent with the hypothesis that the detected diphtheria toxin-binding glycoproteins are involved in intoxication of cells by this toxin and possibly serve as the plasma membrane receptors for diphtheria toxin.

[1]  R. Proia,et al.  Immunoprecipitation and partial characterization of diphtheria toxin-binding glycoproteins from surface of guinea pig cells. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[2]  M. Hollenberg,et al.  Isolation of the human placenta receptor for epidermal growth factor-urogastrone , 1979, Nature.

[3]  S. Leppla,et al.  Association of diphtheria toxin with Vero cells. Demonstration of a receptor. , 1978, The Journal of biological chemistry.

[4]  C. F. Fox,et al.  Molecular mechanism of mitogen action: processing of receptor induced by epidermal growth factor. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[5]  M. Simon,et al.  Diphtheria toxin has the properties of a lectin. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[6]  P. Cuatrecasas,et al.  Purification and properties of insulin receptors from rat liver membranes. , 1977, Biochemical and Biophysical Research Communications - BBRC.

[7]  M. Pandian,et al.  Labeling of bovine corpus luteal plasma membrane human chorionic gonadotropin or luteinizing hormone (hCG/LH) receptor and its purification and properties. , 1977, Archives of biochemistry and biophysics.

[8]  A. M. Pappenheimer Diphtheria toxin. , 1952, Annual review of biochemistry.

[9]  J. Zanen,et al.  Competitive antagonists of the action of diphtheria toxin in HeLa cells , 1976, FEBS letters.

[10]  C. Ward,et al.  Size and chemical composition of influenza virus hemagglutinin chains , 1976, FEBS letters.

[11]  D. Hart Evidence for the non-protein nature of the receptor for the enterotoxin in Vibrio cholerae on murine lymphoid cells , 1975, Infection and immunity.

[12]  R. Collier Diphtheria toxin: mode of action and structure , 1975, Bacteriological reviews.

[13]  P. Cuatrecasas Membrane receptors. , 1974, Annual review of biochemistry.

[14]  K. Catt,et al.  Characteristics of a soluble gonadotropin receptor from the rat testis. , 1973, The Journal of biological chemistry.

[15]  T. Uchida,et al.  An immunological study of the diphtheria toxin molecule. , 1972, Immunochemistry.

[16]  M. Crumpton,et al.  Isolation of glycoproteins from pig lymphocyte plasma membrane using Lens culinaris phytohemagglutinin. , 1972, Biochemical and biophysical research communications.

[17]  V. Marchesi,et al.  Human erythrocyte membrane glycoprotein: a re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis. , 1971, Biochemical and biophysical research communications.

[18]  J V Maizel,et al.  Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. , 1967, Biochemical and biophysical research communications.

[19]  L. Olitzki,et al.  Neurotoxic symptoms produced in the Syrian hamster, Cricetus auratus by diphtherial toxin. , 1948, Journal of immunology.