Novel matrix proteins of Pteria penguin pearl oyster shell nacre homologous to the jacalin-related β-prism fold lectins.

ABSTRACT: Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of α and γ subunits, and PPL2B is a homo-dimer of β subunit, all of which surprisingly shared sequence homology with the jacalin-related plant lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclu

SUBMITTER: Naganuma T 

PROVIDER: S-EPMC4223035 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature