The biofilm matrix of Campylobacter jejuni determined by fluorescence lectin-binding analysis

Biofouling. 2016;32(5):597-608. doi: 10.1080/08927014.2016.1169402.

Abstract

Campylobacter jejuni is responsible for the most common bacterial foodborne gastroenteritis. Despite its fastidious growth, it can survive harsh conditions through biofilm formation. In this work, fluorescence lectin-binding analysis was used to determine the glycoconjugates present in the biofilm matrix of two well-described strains. Screening of 72 lectins revealed strain-specific patterns with six lectins interacting with the biofilm matrix of both strains. The most common sugar moiety contained galactose and N-acetylgalactosamine. Several lectins interacted with N-acetylglucosamine and sialic acid, probably originated from the capsular polysaccharides, lipooligosaccharides and N-glycans of C. jejuni. In addition, glycoconjugates containing mannose and fucose were detected within the biofilm, which have not previously been found in the C. jejuni envelope. Detection of thioflavin T and curcumin highlighted the presence of amyloids in the cell envelope without association with specific cell appendages. The lectins ECA, GS-I, HMA and LEA constitute a reliable cocktail to detect the biofilm matrix of C. jejuni.

Keywords: CLSM; Campylobacter jejuni; FLBA; amyloids; biofilm matrix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biofilms*
  • Campylobacter jejuni / physiology*
  • Fluorescence
  • Glycoconjugates / analysis
  • Lectins / metabolism*
  • Lipopolysaccharides / analysis
  • Polysaccharides, Bacterial / analysis

Substances

  • Glycoconjugates
  • Lectins
  • Lipopolysaccharides
  • Polysaccharides, Bacterial
  • lipid-linked oligosaccharides