Mutational analysis of immunoglobulin E‐binding epitopes of β‐casein and β‐lactoglobulin showed a heterogeneous pattern of critical amino acids between individual patients and pooled sera

Cocco, Renata Rodrigues; Järvinen, Kirsi-Marjut; Han, Ning; Beyer, Kirsten; Sampson, Hugh A.

doi:10.1111/j.1365-2222.2007.02712.x

Cited by 42 publications

(39 citation statements)

References 20 publications

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“…Aggregation has earlier been suggested to be the reason for the sustained allergenic capacity of digestion products of allergens, which in theory were too small to contain two epitopes and thereby not big enough to cross-link two IgE molecules bound to the surface of mast cells or basophils [11,16,26]. The finding that IgE epitopes on BLG survive digestion is in accordance with previous studies stating that the major IgE epitopes reported in the literature by Järvinen et al [6] and Cocco et al [5] corresponded to areas of BLG where peptides did resist simulated gastro-duodenal digestion [22]. This is in agreement with the current study and could support the presence of major linear B cell epitopes on BLG.…”

Section: Discussionsupporting

confidence: 82%

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The Sensitising Capacity of Intact β-Lactoglobulin Is Reduced by Co-Administration with Digested β-Lactoglobulin

Bøgh

Barkholt

Madsen

2012

Int Arch Allergy Immunol

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Background: It is generally believed that protein hydrolysis in the gastrointestinal tract decreases the allergenicity of food allergens. However, it remains unknown if specific properties of digestion products determine whether a sensitisation or tolerogenic immune response will develop. We sought to examine the sensitising capacity of the cow’s milk allergen β-lactoglobulin (BLG) and digestion products thereof in a Brown Norway (BN) rat model. Methods: Intact BLG was digested in an in vitro model simulating the gastro-duodenal digestion process and subsequently fractionated by gel permeation chromatography. BN rats were dosed with either PBS, 200 µg of intact BLG, 30 µg of intact BLG, 200 µg of partially digested BLG, 200 µg of digested BLG, or with 200 µg of a fraction of large complexes or a fraction of small complexes. Sera from BN rats were analysed for specific antibodies and avidity was measured. Results: BLG partly resisted the digestion process. However, the BLG molecules that did not survive the digestion process were rapidly broken down to peptides of sizes less than M_r 4,500. Specific antibody responses revealed that both 200 and 30 µg of intact BLG had immunogenic as well as sensitising capacity, while digested BLG could not induce any specific antibodies. Most importantly, while intact BLG showed a significant sensitising capacity when administered alone, this sensitising capacity was significantly reduced when co-administered with digested BLG. Conclusions: Co-immunisation of intact BLG with digested BLG reduces the sensitising capacity of intact BLG, which could result from tolerogenic mechanisms induced by the digestion products.

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Section: Discussionsupporting

confidence: 82%

“…Numerous studies have been performed with the aim of identifying BLG-specific epitopes. They indicate that many conformational as well as many linear epitopes exist, covering most of the molecule [5,6,7]. …”

Section: Introductionmentioning

confidence: 99%

The Sensitising Capacity of Intact β-Lactoglobulin Is Reduced by Co-Administration with Digested β-Lactoglobulin

Bøgh

Barkholt

Madsen

2012

Int Arch Allergy Immunol

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“…3B). Although alanine scanning is usually performed to determine the binding epitope, conversion to other amino acids has been utilized in some reports (33)(34)(35) when alanine might be included in the epitope. Therefore, we further changed Ala42 and Ala46 to other amino acids such as Ser and Val (Fig.…”

Section: Immunohistochemical Analysis Using Lpmab-13mentioning

confidence: 99%

Establishment of Mouse Monoclonal Antibody LpMab-13 Against Human Podoplanin

OgasawaraSatoshi

Kaneko

HonmaRyusuke

et al. 2016

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy

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Podoplanin (PDPN)/Aggrus is a type-I transmembrane sialoglycoprotein, which possesses a platelet aggregation-stimulating (PLAG) domain. The O-glycosylation on Thr52 of human PDPN (hPDPN) is critical for the interaction of hPDPN with C-type lectin-like receptor-2 (CLEC-2), resulting in platelet aggregation. Many anti-hPDPN monoclonal antibodies (MAbs) against PLAG domains and non-PLAG domains have been established; however, mouse anti-PLAG2/3 MAb, the epitope of which is consistent with rat anti-PLAG2/3 MAb NZ-1, has not been established. NZ-1 inhibits the hPDPN-CLEC-2 interaction and is also useful for anti-PA tag MAb. We recently established CasMab technology to produce MAbs against membranous proteins. Herein, we produced a novel anti-hPDPN MAb, LpMab-13, which binds to PLAG2/3 domains. LpMab-13 recognized endogenous hPDPN of cancer cells, including glioblastoma, oral cancer, lung cancer, and malignant mesothelioma, and normal cells such as lymphatic endothelial cells and podocytes of kidney in Western blot, flow cytometry, and immunohistochemistry. LpMab-13 recognized glycan-deficient hPDPN in flow cytometry, indicating that the interaction between LpMab-13 and hPDPN is independent of its glycosylation. The minimum epitope of LpMab-13 was identified as Ala42-Asp49 of hPDPN using Western blot and flow cytometry. The combination of different epitope-possessing MAbs could be advantageous for the hPDPN-targeting diagnosis and therapy.

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“…Terms & Introduction b-Lactoglobulin (BLG) is a major food allergen, contributing significantly to the overall allergenicity of bovine milk (Besler, Eigenmann, & Schwartz, 2002). Sequential and conformational epitopes may play an important role in the allergenicity of this protein (Cocco, Jarvinen, Han, Beyer, & Sampson, 2007). Immunological investigations of BLG have reported six different IgE-binding regions (epitopes) of the protein that were linked with allergic reaction (Niemi et al, 2007).…”

Section: Allergenic Changes In β-Lactoglobulin Induced By Microwave Imentioning

confidence: 99%

Allergenic changes in β-lactoglobulin induced by microwave irradiation under different pH conditions

Zellal

Kaddouri

Grar

et al. 2011

Food and Agricultural Immunology

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Mutational analysis of immunoglobulin E‐binding epitopes of β‐casein and β‐lactoglobulin showed a heterogeneous pattern of critical amino acids between individual patients and pooled sera

Cited by 42 publications

References 20 publications

The Sensitising Capacity of Intact β-Lactoglobulin Is Reduced by Co-Administration with Digested β-Lactoglobulin

The Sensitising Capacity of Intact β-Lactoglobulin Is Reduced by Co-Administration with Digested β-Lactoglobulin

Establishment of Mouse Monoclonal Antibody LpMab-13 Against Human Podoplanin

Allergenic changes in β-lactoglobulin induced by microwave irradiation under different pH conditions

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