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

doi:10.1111/j.1444-2906.2005.01047.x

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 journal › Article › peer-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 language	English
Pages (from-to)	931-940
Number of pages	10
Journal	Fisheries Science
Volume	71
Issue number	4
DOIs	https://doi.org/10.1111/j.1444-2906.2005.01047.x
Publication status	Published - 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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10.1111/j.1444-2906.2005.01047.x

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@article{48e0773c04544f75a49e388fb1cdb387,

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

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.",

keywords = "Acorn barnacle, Biomineralization, C-type lectin, Glycopeptidase F, Glycoprotein, Lectin, N-linked sugar chain",

author = "Hiroki Matsubara and Shizuya Kabuto and Naoko Nakahara and Tomohisa Ogawa and Koji Muramoto and Mitsuru Jimbo and Hisao Kamiya",

note = "Funding Information: This work was supported by Grants-in-Aid for Scientific Research (13556031) from the Ministry of Education, Science, Sports and Culture of Japan.",

year = "2005",

month = aug,

doi = "10.1111/j.1444-2906.2005.01047.x",

language = "English",

volume = "71",

pages = "931--940",

journal = "Fisheries Science",

issn = "0919-9268",

publisher = "Springer Japan",

number = "4",

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T1 - Structure and possible function of N-glycans of an invertebrate C-type lectin from the acorn barnacle Megabalanus rosa

AU - Matsubara, Hiroki

AU - Kabuto, Shizuya

AU - Nakahara, Naoko

AU - Ogawa, Tomohisa

AU - Muramoto, Koji

AU - Jimbo, Mitsuru

AU - Kamiya, Hisao

N1 - Funding Information: This work was supported by Grants-in-Aid for Scientific Research (13556031) from the Ministry of Education, Science, Sports and Culture of Japan.

PY - 2005/8

Y1 - 2005/8

N2 - 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.

AB - 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.

KW - Acorn barnacle

KW - Biomineralization

KW - C-type lectin

KW - Glycopeptidase F

KW - Glycoprotein

KW - Lectin

KW - N-linked sugar chain

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DO - 10.1111/j.1444-2906.2005.01047.x

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VL - 71

SP - 931

EP - 940

JO - Fisheries Science

JF - Fisheries Science

SN - 0919-9268

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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