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Infection and Immunity, October 1999, p. 5332-5337, Vol. 67, No. 10
Department of Bacterial Infections,
Received 9 April 1999/Returned for modification 7 June
1999/Accepted 15 July 1999
El Tor hemolysin (ETH), a pore-forming toxin secreted by
Vibrio cholerae O1 biotype El Tor and most Vibrio
cholerae non-O1 isolates, is able to lyse erythrocytes and other
mammalian cells. To study the receptor for this toxin or the related
molecule(s) on erythrocyte, we first isolated a monoclonal antibody,
B1, against human erythrocyte membrane, which not only blocks the
binding of ETH to human erythrocyte but also inhibits the hemolytic
activity of ETH. Biochemical characterization and immunoblotting
revealed that this antibody recognized an epitope on the extracellular domain of glycophorin B, a sialoglycoprotein of erythrocyte membrane. Erythrocytes lacking glycophorin B but not glycophorin A were less
sensitive to the toxin than were normal human erythrocytes. These
results indicate that glycophorin B is a receptor for ETH or at least
an associated molecule of the receptor for ETH on human erythrocytes.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Analysis of Receptor for Vibrio cholerae
El Tor Hemolysin with a Monoclonal Antibody That Recognizes Glycophorin
B of Human Erythrocyte Membrane
*
Corresponding author. Mailing address: Department of
Bacterial Infections, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan. Phone: 81-6-6879-8276. Fax: 81-6-6879-8277. E-mail:
honda{at}biken.osaka-u.ac.jp.
Infection and Immunity, October 1999, p. 5332-5337, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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