g(m1)-ganglioside and stichoposide

g(m1)-ganglioside has been researched along with stichoposide* in 2 studies

Reviews

1 review(s) available for g(m1)-ganglioside and stichoposide

Article	Year
Heat-labile enterotoxin: beyond G(m1) binding. Toxins, 2010, Volume: 2, Issue:6 Enterotoxigenic Escherichia coli (ETEC) is a significant source of morbidity and mortality worldwide. One major virulence factor released by ETEC is the heat-labile enterotoxin LT, which is structurally and functionally similar to cholera toxin. LT consists of five B subunits carrying a single catalytically active A subunit. LTB binds the monosialoganglioside G(M1), the toxin's host receptor, but interactions with A-type blood sugars and E. coli lipopolysaccharide have also been identified within the past decade. Here, we review the regulation, assembly, and binding properties of the LT B-subunit pentamer and discuss the possible roles of its numerous molecular interactions. Topics: Animals; Bacterial Toxins; Enterotoxins; Escherichia coli Proteins; G(M1) Ganglioside; Glycosides; Humans; Lipopolysaccharides; Protein Binding; Triterpenes	2010

Article

Year

Heat-labile enterotoxin: beyond G(m1) binding.

Toxins, 2010, Volume: 2, Issue:6

Enterotoxigenic Escherichia coli (ETEC) is a significant source of morbidity and mortality worldwide. One major virulence factor released by ETEC is the heat-labile enterotoxin LT, which is structurally and functionally similar to cholera toxin. LT consists of five B subunits carrying a single catalytically active A subunit. LTB binds the monosialoganglioside G(M1), the toxin's host receptor, but interactions with A-type blood sugars and E. coli lipopolysaccharide have also been identified within the past decade. Here, we review the regulation, assembly, and binding properties of the LT B-subunit pentamer and discuss the possible roles of its numerous molecular interactions.

Topics: Animals; Bacterial Toxins; Enterotoxins; Escherichia coli Proteins; G(M1) Ganglioside; Glycosides; Humans; Lipopolysaccharides; Protein Binding; Triterpenes

2010

Other Studies

1 other study(ies) available for g(m1)-ganglioside and stichoposide

Article	Year
Molecular genetic analysis of ganglioside GD1b-binding activity of Escherichia coli type IIa heat-labile enterotoxin by use of random and site-directed mutagenesis. Infection and immunity, 1992, Volume: 60, Issue:1 Mutagenesis of the B-subunit gene of Escherichia coli heat-labile enterotoxin LT-IIa was performed in vitro with sodium bisulfite. Mutants were screened initially by radial passive immune hemolysis assays for loss of binding to erythrocytes. Mutant B polypeptides were characterized for immunoreactivity; for binding to gangliosides GD1b, GD1a, and GM1; for formation of holotoxin; and for biological activity. Mutant alleles that determined altered binding specificities were sequenced. Three such mutant alleles encoded Thr-to-Ile substitutions at residues 13, 14, and 34 in the mature B polypeptide of LT-IIa. Each mutant protein failed to bind to ganglioside GD1b, although the Ile-14 mutant retained the ability to bind to ganglioside GM1. Site-specific mutagenesis was used to construct mutants with various amino acid substitutions at residue 13, 14, or 34. Only those mutant proteins with Ser substituted for Thr at position 13, 14, or 34 retained the ability to bind to ganglioside GD1b, thereby suggesting a role for the hydroxyl group of Thr or Ser in ganglioside GD1b binding. Topics: Amino Acid Sequence; Animals; Bacterial Toxins; Biological Assay; Enterotoxins; Escherichia coli; Escherichia coli Proteins; G(M1) Ganglioside; Gangliosides; Glycosides; Hemolysis; In Vitro Techniques; Molecular Sequence Data; Mutagenesis; Oligonucleotide Probes; Plasmids; Radioimmunoassay; Sulfites; Triterpenes	1992

Article

Year

Molecular genetic analysis of ganglioside GD1b-binding activity of Escherichia coli type IIa heat-labile enterotoxin by use of random and site-directed mutagenesis.

Infection and immunity, 1992, Volume: 60, Issue:1

Mutagenesis of the B-subunit gene of Escherichia coli heat-labile enterotoxin LT-IIa was performed in vitro with sodium bisulfite. Mutants were screened initially by radial passive immune hemolysis assays for loss of binding to erythrocytes. Mutant B polypeptides were characterized for immunoreactivity; for binding to gangliosides GD1b, GD1a, and GM1; for formation of holotoxin; and for biological activity. Mutant alleles that determined altered binding specificities were sequenced. Three such mutant alleles encoded Thr-to-Ile substitutions at residues 13, 14, and 34 in the mature B polypeptide of LT-IIa. Each mutant protein failed to bind to ganglioside GD1b, although the Ile-14 mutant retained the ability to bind to ganglioside GM1. Site-specific mutagenesis was used to construct mutants with various amino acid substitutions at residue 13, 14, or 34. Only those mutant proteins with Ser substituted for Thr at position 13, 14, or 34 retained the ability to bind to ganglioside GD1b, thereby suggesting a role for the hydroxyl group of Thr or Ser in ganglioside GD1b binding.

Topics: Amino Acid Sequence; Animals; Bacterial Toxins; Biological Assay; Enterotoxins; Escherichia coli; Escherichia coli Proteins; G(M1) Ganglioside; Gangliosides; Glycosides; Hemolysis; In Vitro Techniques; Molecular Sequence Data; Mutagenesis; Oligonucleotide Probes; Plasmids; Radioimmunoassay; Sulfites; Triterpenes

1992