Purification and characterization of a protein cryoprotective for Vibrio cholerae extracted from the prawn shell surface.
A substance cryoprotective for Vibrio cholerae on the prawn shell surface was purified by ammonium sulfate precipitation and gel filtration. It was a protein of 81 kDa and called cryoprotective protein (CPP). The cryoprotective activity of this protein for V. cholerae was sensitive to heat at 100 C and trypsin treatment. In the presence of Mg ion the protein can bind to the bacterial cell surface. V. cholerae can adhere to the shell surface of the prawn. The number of adhered bacteria was reduced by treating the shell with anti-CPP serum, heat or by trypsin. The presence of Mg ion promoted the adherence. These results suggest that the CPP could serve as an adherence site for V. cholerae on the shell surface.
Faming
D
D
Department of Bacteriology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
Shimodori
S
S
Moriya
T
T
Iwanaga
S
S
Amako
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001422:Bacterial Adhesion / Q000502:physiology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003451:Cryoprotective Agents / Q000737:chemistry* / Q000302:isolation & purification*; D033364:Decapoda / Q000737:chemistry* / Q000382:microbiology; D007106:Immune Sera; D015151:Immunoblotting; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification* / Q000502:physiology; D014734:Vibrio cholerae / Q000502:physiology*
D003451:Cryoprotective Agents; D007106:Immune Sera; D011506:Proteins