Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance
Abstract
The present study determines the affinity of cholera toxin for the ganglioside series GM1, GM2, GM3, GD1A, GD1B, GT1B, asialo GM1, globotriosyl ceramide, and lactosyl ceramide using real time biospecific interaction analysis (surface plasmon resonance, SPR). SPR shows that cholera toxin preferably binds to gangliosides in the following sequence: GM1 > GM2 > GD1A > GM3 > GT1B > GD1B > asialo-GM1. The measured binding affinity of cholera toxin for the ganglioside sequence ranges from 4.61 {times} 10{sup {minus}12} M for GM1 to 1.88 {times} 10{sup {minus}10} M for asialo GM1. The picomolar values obtained by surface plasmon resonance are similar to K{sub d} values determined with whole-cell binding assays. Both whole-cell assays ans SPR measurements on synthetic membranes are higher than free solution measurements by several orders of magnitude. This difference may be caused by the effects of avidity and charged lipid head-groups, which may play a major role in the binding between cholera toxin, the receptor, and the membrane surface. The primary difference between free solution binding studies and surface plasmon resonance studies is that the latter technique is performed on surfaces resembling the cell membrane. Surface plasmon resonance has the further advantage of measuring apparent kinetic associationmore »
- Authors:
-
- Univ. of California, Berkeley, CA (United States)
- Publication Date:
- OSTI Identifier:
- 518242
- DOE Contract Number:
- AC03-76SF00098
- Resource Type:
- Journal Article
- Journal Name:
- Biochemistry (Eaton)
- Additional Journal Information:
- Journal Volume: 35; Journal Issue: 20; Other Information: PBD: 21 May 1996
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 55 BIOLOGY AND MEDICINE, BASIC STUDIES; MEMBRANES; SURFACE PROPERTIES; TOXINS; AFFINITY; CHOLERA; DISSOCIATION; GANGLIOSIDES; SPECIFICITY; MOLECULAR STRUCTURE
Citation Formats
Kuziemko, G M, Stroh, M, Stevens, R C, and Lawrence Berkeley National Lab., CA. Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. United States: N. p., 1996.
Web. doi:10.1021/bi952314i.
Kuziemko, G M, Stroh, M, Stevens, R C, & Lawrence Berkeley National Lab., CA. Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. United States. https://doi.org/10.1021/bi952314i
Kuziemko, G M, Stroh, M, Stevens, R C, and Lawrence Berkeley National Lab., CA. 1996.
"Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance". United States. https://doi.org/10.1021/bi952314i.
@article{osti_518242,
title = {Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance},
author = {Kuziemko, G M and Stroh, M and Stevens, R C and Lawrence Berkeley National Lab., CA},
abstractNote = {The present study determines the affinity of cholera toxin for the ganglioside series GM1, GM2, GM3, GD1A, GD1B, GT1B, asialo GM1, globotriosyl ceramide, and lactosyl ceramide using real time biospecific interaction analysis (surface plasmon resonance, SPR). SPR shows that cholera toxin preferably binds to gangliosides in the following sequence: GM1 > GM2 > GD1A > GM3 > GT1B > GD1B > asialo-GM1. The measured binding affinity of cholera toxin for the ganglioside sequence ranges from 4.61 {times} 10{sup {minus}12} M for GM1 to 1.88 {times} 10{sup {minus}10} M for asialo GM1. The picomolar values obtained by surface plasmon resonance are similar to K{sub d} values determined with whole-cell binding assays. Both whole-cell assays ans SPR measurements on synthetic membranes are higher than free solution measurements by several orders of magnitude. This difference may be caused by the effects of avidity and charged lipid head-groups, which may play a major role in the binding between cholera toxin, the receptor, and the membrane surface. The primary difference between free solution binding studies and surface plasmon resonance studies is that the latter technique is performed on surfaces resembling the cell membrane. Surface plasmon resonance has the further advantage of measuring apparent kinetic association and dissociation rates in real time, providing direct information about binding events at the membrane surface. 34 refs., 8 figs., 2 tabs.},
doi = {10.1021/bi952314i},
url = {https://www.osti.gov/biblio/518242},
journal = {Biochemistry (Eaton)},
number = 20,
volume = 35,
place = {United States},
year = {Tue May 21 00:00:00 EDT 1996},
month = {Tue May 21 00:00:00 EDT 1996}
}