Glycoconjugate Journal

, Volume 11, Issue 6, pp 518–526 | Cite as

Chitovibrin: a chitin-binding lectin fromVibrio parahemolyticus

  • Otto S. Gildemeister
  • Betty C. R. Zhu
  • Roger A. Laine
Lectin Papers


A novel 134 kDa, calcium-independent chitin-binding lectin, ‘chitovibrin’, is secreted by the marine bacteriumVibrio 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 0–4m NaCl. Chitovibrin appears to be completely different from other reported Vibrio lectins and may function to bindV. 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.


chitin-binding lectin ‘chitovibrin’ Vibrio parahemolyticus 





sodium dodecyl sulphate-polyacrylamide gel electrophoresis


phosphotransferase system


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Copyright information

© Chapman & Hall 1994

Authors and Affiliations

  • Otto S. Gildemeister
    • 1
  • Betty C. R. Zhu
    • 1
  • Roger A. Laine
    • 1
  1. 1.Department of Biochemistry, Department of ChemistryLouisiana State University and The Louisiana Agricultural CenterBaton RougeUSA

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