is the only culturable vibrio associated with the chitinaceous carapace of the copepod (Fisher 1860) living in Ligurian coastal rock pools (Tyrrhenian Sea). The characteristics of the interaction between chitin particles and were studied by analysing strains isolated both from the copepod surface and from rock-pool water. The highest degree of attachment to chitin was observed at 20°, in the presence of 3% NaCI. Bacterial treatment with -acetylglucosamine and pronase E caused a reduction in attachment of 52-62% and 77-94%, respectively. Chitin pretreatment with either wheat germ agglutinin or membrane proteins (MPs) from caused a reduction in attachment, of 50-57% and 53-70%, respectively. No inhibition was observed when bacteria were pretreated with D-glucose, D-fucose or D-fructose, or when chitin was pretreated with concanavalin A and DH5α MPs. MPs able to bind chitin were isolated and analysed by SDS-PAGE. Four chitin-binding proteins were visualized in all tested strains (53, 35, 20 and 14 kDa); these peptides may efficiently mediate attachment to chitin-containing substrates.


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