In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile

Rivca L Valk-Weeber; Cecile Deelman-Driessen; Lubbert Dijkhuizen; Talitha Eshuis-de Ruiter; Sander van Leeuwen

doi:10.1021/acs.jafc.0c00959

In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile

Rivca L Valk-Weeber, Cecile Deelman-Driessen, Lubbert Dijkhuizen, Talitha Eshuis-de Ruiter, Sander van Leeuwen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

The N-linked glycoprofile of bovine whey is the combined result of individual protein glycoprofiles. In this work, we provide in-depth structural information on the glycan structures of known whey glycoproteins, namely lactoferrin, lactoperoxidase, α-lactalbumin, immunoglobulin-G (IgG) and glycosylation dependent cellular adhesion molecule 1 (GlyCAM-1, PP3). The majority (~95%) of N-glycans present in the overall whey glycoprofile were attributed to three proteins; Lactoferrin, IgG and GlyCAM-1. We identified specific signature glycans for these main proteins; Lactoferrin contributes oligomannose-type glycans, while IgG carries fucosylated di-antennary glycans with Gal-β(1,4)GlcNAc (LacNAc) motifs. GlyCAM-1 is the sole whey glycoprotein carrying tri- and tetra-antennary structures, with a high degree of fucosylation and sialylation. Signature glycans can be used to recognize individual proteins in the overall whey glycoprofile, as well as for protein concentration estimations. Application of the whey glycoprofile analysis to colostrum samples revealed dynamic protein concentration changes for IgG, lactoferrin and GlyCAM-1 over time.

Original language	English
Article number	acs.jafc.0c00959
Pages (from-to)	6544-6553
Number of pages	10
Journal	Journal of Agricultural and Food Chemistry
Volume	68
Issue number	24
Early online date	2020
DOIs	https://doi.org/10.1021/acs.jafc.0c00959
Publication status	Published - 17-Jun-2020

Keywords

GlyCAM-1
PP3
colostrum
milk
protein glycosylation
whey

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title = "In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile",

abstract = "The N-linked glycoprofile of bovine whey is the combined result of individual protein glycoprofiles. In this work, we provide in-depth structural information on the glycan structures of known whey glycoproteins, namely lactoferrin, lactoperoxidase, α-lactalbumin, immunoglobulin-G (IgG) and glycosylation dependent cellular adhesion molecule 1 (GlyCAM-1, PP3). The majority (~95%) of N-glycans present in the overall whey glycoprofile were attributed to three proteins; Lactoferrin, IgG and GlyCAM-1. We identified specific signature glycans for these main proteins; Lactoferrin contributes oligomannose-type glycans, while IgG carries fucosylated di-antennary glycans with Gal-β(1,4)GlcNAc (LacNAc) motifs. GlyCAM-1 is the sole whey glycoprotein carrying tri- and tetra-antennary structures, with a high degree of fucosylation and sialylation. Signature glycans can be used to recognize individual proteins in the overall whey glycoprofile, as well as for protein concentration estimations. Application of the whey glycoprofile analysis to colostrum samples revealed dynamic protein concentration changes for IgG, lactoferrin and GlyCAM-1 over time.",

keywords = "GlyCAM-1, PP3, colostrum, milk, protein glycosylation, whey",

author = "Valk-Weeber, {Rivca L} and Cecile Deelman-Driessen and Lubbert Dijkhuizen and {Eshuis-de Ruiter}, Talitha and {van Leeuwen}, Sander",

year = "2020",

month = jun,

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doi = "10.1021/acs.jafc.0c00959",

language = "English",

volume = "68",

pages = "6544--6553",

journal = "Journal of Agricultural and Food Chemistry",

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publisher = "AMER CHEMICAL SOC",

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}

In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile. / Valk-Weeber, Rivca L; Deelman-Driessen, Cecile ; Dijkhuizen, Lubbert et al.
In: Journal of Agricultural and Food Chemistry, Vol. 68, No. 24, acs.jafc.0c00959, 17.06.2020, p. 6544-6553.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile

AU - Valk-Weeber, Rivca L

AU - Deelman-Driessen, Cecile

AU - Dijkhuizen, Lubbert

AU - Eshuis-de Ruiter, Talitha

AU - van Leeuwen, Sander

PY - 2020/6/17

Y1 - 2020/6/17

N2 - The N-linked glycoprofile of bovine whey is the combined result of individual protein glycoprofiles. In this work, we provide in-depth structural information on the glycan structures of known whey glycoproteins, namely lactoferrin, lactoperoxidase, α-lactalbumin, immunoglobulin-G (IgG) and glycosylation dependent cellular adhesion molecule 1 (GlyCAM-1, PP3). The majority (~95%) of N-glycans present in the overall whey glycoprofile were attributed to three proteins; Lactoferrin, IgG and GlyCAM-1. We identified specific signature glycans for these main proteins; Lactoferrin contributes oligomannose-type glycans, while IgG carries fucosylated di-antennary glycans with Gal-β(1,4)GlcNAc (LacNAc) motifs. GlyCAM-1 is the sole whey glycoprotein carrying tri- and tetra-antennary structures, with a high degree of fucosylation and sialylation. Signature glycans can be used to recognize individual proteins in the overall whey glycoprofile, as well as for protein concentration estimations. Application of the whey glycoprofile analysis to colostrum samples revealed dynamic protein concentration changes for IgG, lactoferrin and GlyCAM-1 over time.

AB - The N-linked glycoprofile of bovine whey is the combined result of individual protein glycoprofiles. In this work, we provide in-depth structural information on the glycan structures of known whey glycoproteins, namely lactoferrin, lactoperoxidase, α-lactalbumin, immunoglobulin-G (IgG) and glycosylation dependent cellular adhesion molecule 1 (GlyCAM-1, PP3). The majority (~95%) of N-glycans present in the overall whey glycoprofile were attributed to three proteins; Lactoferrin, IgG and GlyCAM-1. We identified specific signature glycans for these main proteins; Lactoferrin contributes oligomannose-type glycans, while IgG carries fucosylated di-antennary glycans with Gal-β(1,4)GlcNAc (LacNAc) motifs. GlyCAM-1 is the sole whey glycoprotein carrying tri- and tetra-antennary structures, with a high degree of fucosylation and sialylation. Signature glycans can be used to recognize individual proteins in the overall whey glycoprofile, as well as for protein concentration estimations. Application of the whey glycoprofile analysis to colostrum samples revealed dynamic protein concentration changes for IgG, lactoferrin and GlyCAM-1 over time.

KW - GlyCAM-1

KW - PP3

KW - colostrum

KW - milk

KW - protein glycosylation

KW - whey

U2 - 10.1021/acs.jafc.0c00959

DO - 10.1021/acs.jafc.0c00959

M3 - Article

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SN - 0021-8561

VL - 68

SP - 6544

EP - 6553

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 24

M1 - acs.jafc.0c00959

ER -

In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile

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