Three in one: Identification, expression and enzymatic activity of lysozymes in amphioxus

Dev Comp Immunol. 2014 Oct;46(2):508-17. doi: 10.1016/j.dci.2014.06.007. Epub 2014 Jun 23.

Abstract

The lysozymes identified so far in animals belong to the g-type, c-type, and i-type. Vertebrate animals possess only the former two types, i.e., g- and c-types, while all the three types have been reported in invertebrates. Here we demonstrate that (1) three cDNAs that encode g-, c-, and i-type lysozymes, respectively, were identified in a single species of the amphioxus Branchiostoma japonicum; (2) all the 3-type genes displayed distinct tissue-specific expression pattern; (3) recombinant g-, c-, and i-type lysozymes all exhibited enzymatic activities; and (4) native g-, c-, and i-type lysozymes were identified in the different tissues of amphioxus. Collectively, these results suggest the presence of all the 3-type lysozymes in a single animal species, first such data ever reported. The presence of biologically active i-type lysozyme in amphioxus also suggests that i-type lysozyme gene is retained at least in Protochordata, contrasting to the previous proposal that i-type lysozyme gene has been lost in a common ancestor of all chordates.

Keywords: Amphioxus; C-type lysozyme; G-type lysozyme; I-type lysozyme; Protochordate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalytic Domain
  • Gene Expression
  • Hydrogen-Ion Concentration
  • Lancelets / enzymology*
  • Lancelets / genetics
  • Models, Molecular
  • Muramidase / biosynthesis
  • Muramidase / chemistry
  • Muramidase / genetics*
  • Organ Specificity
  • Phylogeny
  • Protein Structure, Secondary

Substances

  • Muramidase