Glycan binding profiling of jacalin-related lectins from the Pteria Penguin pearl shell

Tomohisa Ogawa, Rie Sato, Takako Naganuma, Kayeu Liu, Agness Ethel Lakudzala, Koji Muramoto, Makoto Osada, Kyosuke Yoshimi, Keiko Hiemori, Jun Hirabayashi, Hiroaki Tateno

Research output: Contribution to journalArticlepeer-review

Abstract

We determined the primary structures of jacalin-related lectins termed PPL3s (PPL3A, 3B, and 3C, which are dimers consisting of sequence variants α + α, a α β, β + β, respectively) and PPL4, which is heterodimer consisting of α + β subunits, isolated from mantle secretory fluid of Pteria penguin (Mabe) pearl shell. Their carbohydrate-binding properties were analyzed, in addition to that of PPL2A, which was previously reported as a matrix protein. PPL3s and PPL4 shared only 35-50% homology to PPL2A, respectively; they exhibited significantly different carbohydrate-binding specificities based on the multiple glycan binding profiling data sets from frontal affinity chromatography analysis. The carbohydrate-binding specificity of PPL3s was similar to that of PPL2A, except only for Man3Fuc1Xyl1GlcNAc2 oligosaccharide, while PPL4 showed different carbohydrate-binding specificity compared with PPL2A and PPL3s. PPL2A and PPL3s mainly recognize agalactosylatedand galactosylated-type glycans. On the other hand, PPL4 binds to high-mannose-and hybrid-type N-linked glycans but not agalactosylated- and galactosylated-type glycans.

Original languageEnglish
Article number4629
JournalInternational journal of molecular sciences
Volume20
Issue number18
DOIs
Publication statusPublished - 2019 Sep 2

Keywords

  • Biomineralization
  • Chitin
  • Glycan binding profiling
  • Lectin
  • Pearl shell

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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