Interaction of Salmonella telaviv with Maclura pomifera lectin

Infection and Immunity
|January 1, 1985
PubMed

Insights

The Maclura pomifera lectin specifically interacts with Salmonella telaviv, suggesting a unique binding mechanism. This interaction is mediated by galactose or N-acetyl-D-galactosamine in the bacterial O polysaccharide structure.

Area of Science:

  • Microbiology
  • Biochemistry
  • Immunology

Background:

  • Lectins are proteins with specific carbohydrate-binding properties.
  • Salmonella species possess diverse lipopolysaccharide (LPS) structures, including O polysaccharides.
  • Understanding lectin-carbohydrate interactions is crucial for diagnostics and therapeutics.

Purpose of the Study:

  • To investigate the interaction between purified lectins and specific Salmonella serovars.
  • To characterize the molecular basis of lectin binding to Salmonella telaviv.

Main Methods:

  • Screening of 15 purified lectins against Salmonella telaviv, Salmonella tranoroa, and Salmonella illinois.
  • Agglutination assays to assess bacterial cell binding by Maclura pomifera lectin.
  • Precipitation assays using purified S. telaviv lipopolysaccharide and O polysaccharide.
  • Quantitative inhibition assays with specific sugars (methyl-alpha-D-galactopyranoside, N-acetyl-D-galactosamine).

Main Results:

  • A specific interaction was observed exclusively between Maclura pomifera lectin and Salmonella telaviv.
  • M. pomifera lectin agglutinated S. telaviv suspensions and precipitated with its LPS and O polysaccharide.
  • Methyl-alpha-D-galactopyranoside and N-acetyl-D-galactosamine potently inhibited the precipitation, indicating their role in the interaction.

Conclusions:

  • The Maclura pomifera lectin exhibits specific binding to Salmonella telaviv.
  • The interaction is mediated by D-galactose or N-acetyl-D-galactosamine residues within the S. telaviv O polysaccharide.
  • This finding highlights a potential lectin-based method for identifying or characterizing S. telaviv.

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