A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes

Cell Mol Life Sci. 2007 Jan;64(1):82-95. doi: 10.1007/s00018-006-6386-y.

Abstract

A new lysozyme (cv-lysozyme 2) with a MALDI molecular mass of 12 984.6 Da was purified from crystalline styles and digestive glands of eastern oysters (Crassostrea virginica) and its cDNA sequenced. Quantitative real time RT-PCR detected cv-lysozyme 2 gene expression primarily in digestive gland tissues, and in situ hybridization located cv-lysozyme 2 gene expression in basophil cells of digestive tubules. Cv-lysozyme 2 showed high amino acid sequence similarity to other bivalve mollusk lysozymes, including cv-lysozyme 1, a lysozyme recently purified from C. virginica plasma. Differences between cv-lysozyme 2 and cv-lysozyme 1 molecular characteristics, enzymatic properties, antibacterial activities, distribution in the oyster body and site of gene expression indicate that the main role of cv-lysozyme 2 is in digestion. While showing that a bivalve mollusk employs different lysozymes for different functions, findings in this study suggest adaptive evolution of i type lysozymes for nutrition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Crassostrea / enzymology*
  • Crassostrea / metabolism
  • DNA, Complementary
  • Evolution, Molecular*
  • Gene Expression Regulation, Enzymologic
  • Molecular Sequence Data
  • Muramidase / chemistry*
  • Muramidase / genetics*
  • Muramidase / isolation & purification
  • Muramidase / metabolism
  • Phylogeny
  • Sequence Alignment

Substances

  • DNA, Complementary
  • Muramidase