Chitovibrin: a chitin-binding lectin from Vibrio parahemolyticus.
A novel 134 kDa, calcium-independent chitin-binding lectin, 'chitovibrin', is secreted by the marine bacterium Vibrio parahemolyticus, inducible with chitin or chitin-oligomers. Chitovibrin shows no apparent enzymatic activity but exhibits a strong affinity for chitin and chito-oligomers > dp9. The protein has an isoelectric pH of 3.6, shows thermal tolerance, binds chitin with an optimum at pH 6 and is active in 0-4 M NaCl. Chitovibrin appears to be completely different from other reported Vibrio lectins and may function to bind V. parahemolyticus to chitin substrates, or to capture or sequester chito-oligomers. It may be a member of a large group of recently described proteins in Vibrios related to a complex chitinoclastic (chitinivorous) system.
Gildemeister
O S
OS
Department of Biochemistry, Louisiana State University, Baton Rouge.
Zhu
B C
BC
Laine
R A
RA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001665:Binding Sites; D002686:Chitin / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006017:Glycolipids / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D014733:Vibrio / Q000378:metabolism*
D001426:Bacterial Proteins; D006017:Glycolipids; D037102:Lectins; C092849:chitovibrin protein, Vibrio parahemolyticus; D002686:Chitin