Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen

Merja Niemi; Sirpa Jylhä; Marja-Leena Laukkanen; Hans Söderlund; Soili Mäkinen-Kiljunen; Johanna M. Kallio; Nina Hakulinen; Tari Haahtela; Kristiina Takkinen; Juha Rouvinen

doi:10.1016/j.str.2007.09.012

Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen

Merja Niemi, Sirpa Jylhä, Marja-Leena Laukkanen, Hans Söderlund, Soili Mäkinen-Kiljunen, Johanna M. Kallio, Nina Hakulinen, Tari Haahtela, Kristiina Takkinen, Juha Rouvinen

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

114 Citations (Scopus)

Abstract

Allergies are caused by the immune reaction to commonly harmless proteins, allergens.
This reaction is typified by immunoglobulin E (IgE) antibodies. We report the crystal structure of an IgE Fab fragment in complex with β-lactoglobulin (BLG), one of the major allergens of bovine milk. The solved structure shows how two IgE/Fab molecules bind the dimeric BLG. The epitope of BLG consists of six different short fragments of the polypeptide chain, which are located especially in the β strands, covering a flat area on the allergen surface.
All six CDR (complementary-determining region) loops of the IgE Fab participate in the binding of BLG. The light chain CDR loops are responsible for the binding of the flat β sheet region of BLG.
The IgE epitope is different from common IgG epitopes that are normally located in the exposed loop regions of antigens and observed also in the two recently determined allergen-IgG complexes.

Original language	English
Pages (from-to)	1413-1421
Journal	Structure
Volume	15
Issue number	11
DOIs	https://doi.org/10.1016/j.str.2007.09.012
Publication status	Published - 2007
MoE publication type	A1 Journal article-refereed

Keywords

allergen
allergy
IgE antibody
antibodies
recombinant antibodies
lactoglobulin

Access to Document

10.1016/j.str.2007.09.012

Cite this

@article{f2499d4716694efbb0b2eb72e7e1dc48,

title = "Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen",

abstract = "Allergies are caused by the immune reaction to commonly harmless proteins, allergens. This reaction is typified by immunoglobulin E (IgE) antibodies. We report the crystal structure of an IgE Fab fragment in complex with β-lactoglobulin (BLG), one of the major allergens of bovine milk. The solved structure shows how two IgE/Fab molecules bind the dimeric BLG. The epitope of BLG consists of six different short fragments of the polypeptide chain, which are located especially in the β strands, covering a flat area on the allergen surface. All six CDR (complementary-determining region) loops of the IgE Fab participate in the binding of BLG. The light chain CDR loops are responsible for the binding of the flat β sheet region of BLG. The IgE epitope is different from common IgG epitopes that are normally located in the exposed loop regions of antigens and observed also in the two recently determined allergen-IgG complexes.",

keywords = "allergen, allergy, IgE antibody, antibodies, recombinant antibodies, lactoglobulin",

author = "Merja Niemi and Sirpa Jylh{\"a} and Marja-Leena Laukkanen and Hans S{\"o}derlund and Soili M{\"a}kinen-Kiljunen and Kallio, {Johanna M.} and Nina Hakulinen and Tari Haahtela and Kristiina Takkinen and Juha Rouvinen",

year = "2007",

doi = "10.1016/j.str.2007.09.012",

language = "English",

volume = "15",

pages = "1413--1421",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "11",

}

TY - JOUR

T1 - Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen

AU - Niemi, Merja

AU - Jylhä, Sirpa

AU - Laukkanen, Marja-Leena

AU - Söderlund, Hans

AU - Mäkinen-Kiljunen, Soili

AU - Kallio, Johanna M.

AU - Hakulinen, Nina

AU - Haahtela, Tari

AU - Takkinen, Kristiina

AU - Rouvinen, Juha

PY - 2007

Y1 - 2007

N2 - Allergies are caused by the immune reaction to commonly harmless proteins, allergens. This reaction is typified by immunoglobulin E (IgE) antibodies. We report the crystal structure of an IgE Fab fragment in complex with β-lactoglobulin (BLG), one of the major allergens of bovine milk. The solved structure shows how two IgE/Fab molecules bind the dimeric BLG. The epitope of BLG consists of six different short fragments of the polypeptide chain, which are located especially in the β strands, covering a flat area on the allergen surface. All six CDR (complementary-determining region) loops of the IgE Fab participate in the binding of BLG. The light chain CDR loops are responsible for the binding of the flat β sheet region of BLG. The IgE epitope is different from common IgG epitopes that are normally located in the exposed loop regions of antigens and observed also in the two recently determined allergen-IgG complexes.

AB - Allergies are caused by the immune reaction to commonly harmless proteins, allergens. This reaction is typified by immunoglobulin E (IgE) antibodies. We report the crystal structure of an IgE Fab fragment in complex with β-lactoglobulin (BLG), one of the major allergens of bovine milk. The solved structure shows how two IgE/Fab molecules bind the dimeric BLG. The epitope of BLG consists of six different short fragments of the polypeptide chain, which are located especially in the β strands, covering a flat area on the allergen surface. All six CDR (complementary-determining region) loops of the IgE Fab participate in the binding of BLG. The light chain CDR loops are responsible for the binding of the flat β sheet region of BLG. The IgE epitope is different from common IgG epitopes that are normally located in the exposed loop regions of antigens and observed also in the two recently determined allergen-IgG complexes.

KW - allergen

KW - allergy

KW - IgE antibody

KW - antibodies

KW - recombinant antibodies

KW - lactoglobulin

U2 - 10.1016/j.str.2007.09.012

DO - 10.1016/j.str.2007.09.012

M3 - Article

SN - 0969-2126

VL - 15

SP - 1413

EP - 1421

JO - Structure

JF - Structure

IS - 11

ER -

Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen

Abstract

Keywords

Access to Document

Fingerprint

Cite this