TY - JOUR
T1 - Glycosphingolipids are not pivotal receptors for Subtilase cytotoxin in vivo
T2 - Sensitivity analysis with glycosylation-defective mutant mice
AU - Kondo, Yuji
AU - Tokuda, Noriyo
AU - Fan, Xiayan
AU - Yamashita, Tatsuyuki
AU - Honke, Koichi
AU - Takematsu, Hiroshi
AU - Togayachi, Akira
AU - Ohta, Michio
AU - Kotzusumi, Yasunori
AU - Narimatsu, Hisashi
AU - Tajima, Orie
AU - Furukaw, Keiko
AU - Furukawa, Koichi
N1 - Funding Information:
We thank Dr. J.C. Paton at School of Molecular and Biomedical Science, University of Adelaide (Australia) for kindly providing us with Subtilase toxin SubAB and its mutant SubA A272 B. We thank Dr. A. Suzuki at Tokai University for valuable discussion. We also thank Ms. Y. Nakayasu and T. Mizuno for technical assistance. This study was supported by a Grant-in-Aid for Scientific Research on Priority Areas (19041030) from the Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT).
PY - 2009/1/9
Y1 - 2009/1/9
N2 - Certain glycosphingolipids play important roles as cellular receptor for bacterial toxins with high specificity and strong affinity. In particular AB5 toxins exhibit typical modes of cell attachment with B5 and invasion and biological effects in cells with A subunit. Subtilase cytotoxin (SubAB) is the prototype of a recently discovered AB5 cytotoxin family produced by certain strains of Shiga toxigenic Escherichia coli, and shows highly specific serine protease activity toward endoplasmic reticulum chaperone Bip. Since this toxin bound to a mimic of ganglioside GM2, GM2 has been considered to be possible receptor for SubAB. Using six kinds of glycosylation-defective knockout mice lacking certain group of glycosphingolipids, sensitivity to SubAB in vivo was analyzed. Consequently, all mutant mice died at around 70 h after intraperitoneal injection of 10 μg (or 7.5 μg) of SubAB as well as wild type mice. These results indicated none of glycolipids are not pivotal receptor for SubAB in the body.
AB - Certain glycosphingolipids play important roles as cellular receptor for bacterial toxins with high specificity and strong affinity. In particular AB5 toxins exhibit typical modes of cell attachment with B5 and invasion and biological effects in cells with A subunit. Subtilase cytotoxin (SubAB) is the prototype of a recently discovered AB5 cytotoxin family produced by certain strains of Shiga toxigenic Escherichia coli, and shows highly specific serine protease activity toward endoplasmic reticulum chaperone Bip. Since this toxin bound to a mimic of ganglioside GM2, GM2 has been considered to be possible receptor for SubAB. Using six kinds of glycosylation-defective knockout mice lacking certain group of glycosphingolipids, sensitivity to SubAB in vivo was analyzed. Consequently, all mutant mice died at around 70 h after intraperitoneal injection of 10 μg (or 7.5 μg) of SubAB as well as wild type mice. These results indicated none of glycolipids are not pivotal receptor for SubAB in the body.
UR - http://www.scopus.com/inward/record.url?scp=57049137092&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=57049137092&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2008.10.163
DO - 10.1016/j.bbrc.2008.10.163
M3 - Article
C2 - 18996356
AN - SCOPUS:57049137092
SN - 0006-291X
VL - 378
SP - 179
EP - 181
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -