Kevin Schey
Last active: 3/24/2020

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

Xue QG, Itoh N, Schey KL, Li YL, Cooper RK, La Peyre JF
Cell Mol Life Sci. 2007 64 (1): 82-95

PMID: 17160350 · DOI:10.1007/s00018-006-6386-y

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.

MeSH Terms (11)

Amino Acid Sequence Animals Base Sequence Crassostrea DNA, Complementary Evolution, Molecular Gene Expression Regulation, Enzymologic Molecular Sequence Data Muramidase Phylogeny Sequence Alignment

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