Diversified biomineralization roles of pteria penguin pearl shell lectins as matrix proteins

Tomohisa Ogawa, Rie Sato, Takako Naganuma, Kayeu Liu, Saho Sato, Shizuka Sakaue, Makoto Osada, Kyosuke Yoshimi, Koji Muramoto

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation.

Original languageEnglish
Article number1081
Pages (from-to)1-12
Number of pages12
JournalInternational Journal of Molecular Sciences
Issue number3
Publication statusPublished - 2021 Feb 1


  • Biomineralization
  • Carbohydrate
  • Chitin
  • Lectin
  • Pearl shell


Dive into the research topics of 'Diversified biomineralization roles of pteria penguin pearl shell lectins as matrix proteins'. Together they form a unique fingerprint.

Cite this