title: A general role for surface membrane proteins in attachment to chitin particles and copepods of environmental and clinical vibrios.
abstract: OBJECTIVE
  To investigate the role of surface membrane proteins (MP) to promote attachment to chitin particles and copepods of different environmental and clinical vibrios.
  
  
  RESULTS
  The role of surface MP to promote attachment to chitin particles and the copepod Tigriopus fulvus was investigated in several environmental and clinical Vibrio strains by inhibition test methods. Attachment to both substrates was significantly inhibited by homologous MP treatment in all strains and percentages of inhibition were comparable with the ones observed with N-acetyl glucosamine (GlcNAc). Sarkosyl-insoluble MP extracted from tested strains were added to chitin particles either in the presence or in the absence of GlcNAc and the fraction bound to chitin in both conditions was visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Chitin-binding proteins (CBP) defined as Sarkosyl-insoluble MP that bound chitin in the absence of GlcNAc but did not in the presence of the sugar were isolated in all strains.
  
  
  CONCLUSIONS
  CBP are common in both environmental and clinical Vibrio strains and they have an important general role in mediating cell interactions with chitin-containing surfaces.
  
  
  CONCLUSIONS
  The role of CBP should be taken into account when investigating environmental persistence of aquatic vibrios.
authors.affiliation: Department of Biology (DIBIO), University of Genoa, Genoa, Italy. luigi.vezzulli@unige.it
authors.forename: L
authors.initials: L
authors.lastname: Vezzulli
authors.forename: E
authors.initials: E
authors.lastname: Pezzati
authors.forename: B
authors.initials: B
authors.lastname: Repetto
authors.forename: M
authors.initials: M
authors.lastname: Stauder
authors.forename: G
authors.initials: G
authors.lastname: Giusto
authors.forename: C
authors.initials: C
authors.lastname: Pruzzo
mesh_terms: D000117:Acetylglucosamine / Q000502:physiology; D000818:Animals; D001422:Bacterial Adhesion / Q000187:drug effects; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002241:Carbohydrates / Q000502:physiology; D002686:Chitin / Q000378:metabolism*; D033342:Copepoda / Q000382:microbiology*; D006801:Humans; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D014733:Vibrio / Q000737:chemistry / Q000378:metabolism* / Q000472:pathogenicity; D014735:Vibrio Infections / Q000382:microbiology*
chemical_list: D001426:Bacterial Proteins; D002241:Carbohydrates; D008565:Membrane Proteins; D002686:Chitin; D000117:Acetylglucosamine