ArticleBiophysical journal2008
Part II: diffraction from two-dimensional cholera toxin crystals bound to their receptors in a lipid monolayer.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 14 citations in OpenAlex.
- Binding of Cholera Toxin B-Subunit to a Ganglioside GM1-Functionalized PEG-Tethered Lipid Membrane.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- The glycolipid GM1 reshapes asymmetric biomembranes and giant vesicles by curvature generation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Part I: an x-ray scattering study of cholera toxin penetration and induced phase transformations in lipid membranes.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of cholera toxin (CTAB(5)) bound to its putative ganglioside receptor, galactosyl-N-acetylgalactosaminyl (N-acetyl-neuraminyl) galactosylglucosylceramide (GM(1)), in a lipid monolayer at the air-water interface has been studied utilizing grazing incidence x-ray diffraction. Cholera toxin is one of very few proteins to be crystallized in two dimensions and characterized in a fully hydrated state. The observed grazing incidence x-ray diffraction Bragg peaks indicated cholera toxin was ordered in a hexagonal lattice and the order extended 600-800 A. The pentameric binding portion of cholera toxin (CTB(5)) improved in-plane ordering over the full toxin (CTAB(5)) especially at low pH. Disulfide bond reduction (activation of the full toxin) also increased the protein layer ordering. These findings are consistent with A-subunit flexibility and motion, which cause packing inefficiencies and greater disorder of the protein layer. Corroborative out-of-plane diffraction (Bragg rod) analysis indicated that the scattering units in the cholera layer with CTAB(5) shortened after disulfide bond reduction of the A subunit. These studies, together with Part I results, revealed key changes in the structure of the cholera toxin-lipid system under different pH conditions.
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