Structure and possible function of N-glycans of an invertebrate C-type lectin from the acorn barnacle Megabalanus rosa

Hiroki Matsubara, Shizuya Kabuto, Naoko Nakahara, Tomohisa Ogawa, Koji Muramoto, Mitsuru Jimbo, Hisao Kamiya

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

A C-type lectin (BRA-2) isolated from the acorn barnacle Megabalanus rosa, which was a glycoprotein having an N-linked sugar chain, was deglycosylated by N-glycopeptidase F. The structure of the released sugar chains was determined by a 2-D mapping method after derivatization with a fluorescent reagent, 2-aminopyridine, to be Manα1-6(Manα1-3)Manβ1-4GlcNAcβ1- 4(Fucα1-6)GlcNAc and Manα1-6(GlcNAcβ1-2Manα1-3) Manβ1-4GlcNAcβ1-4(Fucα1-6)GlcNAc. The structures were confirmed by matrix-assisted laser desorption ionization mass spectrometry and a comparison with authentic sugar chains by high-pressure liquid chromatography. Various properties of BRA-2 were examined before and after deglycosylation. The susceptibility of BRA-2 to protease digestion was increased by deglycosylation. However, the inhibitory activity toward calcium carbonate crystallization as well as the hemagglutinating activity of deglycosylated BRA-2 was significantly decreased. These results suggest that the sugar chains of BRA-2 are important to both its structural stability and its function.

Original languageEnglish
Pages (from-to)931-940
Number of pages10
JournalFisheries Science
Volume71
Issue number4
DOIs
Publication statusPublished - 2005 Aug

Keywords

  • Acorn barnacle
  • Biomineralization
  • C-type lectin
  • Glycopeptidase F
  • Glycoprotein
  • Lectin
  • N-linked sugar chain

ASJC Scopus subject areas

  • Aquatic Science

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