The biofilm matrix of <i>Campylobacter jejuni</i> determined by fluorescence lectin-binding analysis

<i>Campylobacter jejuni</i> 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 <i>N</i>-acetylgalactosamine. Several lectins interacted with <i>N</i>-acetylglucosamine and sialic acid, probably originated from the capsular polysaccharides, lipooligosaccharides and <i>N</i>-glycans of <i>C. jejuni</i>. In addition, glycoconjugates containing mannose and fucose were detected within the biofilm, which have not previously been found in the <i>C. jejuni</i> 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 <i>C. jejuni.</i>