Identification of Ligustrum lucidum pollen allergens using a proteomics approach

Mani, Blessy Maruthukunnel; Huerta‐Ocampo, José Ángel; García-Sánchez, José Rubén; Barrera-Pacheco, Alberto; Rosa, Ana; Teran, Luis M.

doi:10.1016/j.bbrc.2015.11.033

Cited by 19 publications

(25 citation statements)

References 20 publications

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“…In recent years, proteomic technologies have been increasingly employed in the field of allergy, allowing the identification of new allergens by using two-dimensional gel electrophoresis (2-DE) coupled with mass spectrometry (MS) [ 13 , 14 ]. For instance, Akagawa et al [ 15 ] identified flour wheat allergens (serine protease inhibitors (serpin), α-amylase inhibitor, ç-gliadin and low-molecular-weight (LMW) glutenin) and their sequentially homologous proteins as major IgE (Immunoglobulin E)-binding proteins using the allergenomic approach.…”

Section: Introductionmentioning

confidence: 99%

“…For instance, Akagawa et al [ 15 ] identified flour wheat allergens (serine protease inhibitors (serpin), α-amylase inhibitor, ç-gliadin and low-molecular-weight (LMW) glutenin) and their sequentially homologous proteins as major IgE (Immunoglobulin E)-binding proteins using the allergenomic approach. Mani et al [ 14 ] first identified seven IgE-reactive proteins from L . lucidum pollen by 2-DE immunoblotting and MS. Cocos nucifera (Coconut) pollen proteins were analyzed and within them were identified 12 allergenic proteins by 2-DE, immunoblotted with coconut pollen sensitive patient sera followed by mass spectrometry of IgE-reactive proteins [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

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Proteomic Analysis and Identification of Possible Allergenic Proteins in Mature Pollen of Populus tomentosa

Rui

Zhang

Fan

et al. 2018

IJMS

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Pollen grains from Populus tomentosa, a widely cultivated tree in northern area of China, are considered to be an important aeroallergen causing severe allergic diseases. To gain insight into their allergenic components, mature Populus tomentosa pollen proteins were analyzed by two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF/TOF MS). A total of 412 spots from mature pollen were resolved on pH 4–7 immobilized pH gradient (IPG) strips and 159 distinct proteins were identified from 242 spots analyzed. The identified proteins were categorized based on their functional role in the pollen, which included proteins involved in energy regulation, protein fate, protein synthesis and processing, metabolism, defense/stress responses, development and other functional categories. Moreover, among the identified proteins, 27 proteins were identified as putative allergens using the Structural Database of Allergenic Proteins (SDAP) tool and Allergen Online. The expression patterns of these putative allergen genes indicate that several of these genes are highly expressed in pollen. The identified putative allergens have the potential to improve specific diagnosis and can be used to develop vaccines for immunotherapy against poplar pollen allergy.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis and Identification of Possible Allergenic Proteins in Mature Pollen of Populus tomentosa

Rui

Zhang

Fan

et al. 2018

IJMS

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“…Indeed, enolase is an allergenic protein which has been identified in other plants including Ailanthus altissima, Ligustrum, Cynodon dactylon (Bermuda grass), Ambrosia, latex (Hev b 9) and coconut. [19][20][21][22][23][24][25][26] Interestingly, both enolases share a 68% of sequence identity, but not a single peptide identified by mass spectrometry. Enolase 1 exhibited high identity with enolases from other plant allergenic sources including Bermuda grass (88.31%), ambrosia (90.99%) and latex (Hebv 9, 91.46%).…”

Section: Discussionmentioning

confidence: 99%

Proteomic identification of allergenic proteins in red oak (Quercus rubra) pollen

Huerta‐Ocampo

Valenzuela-Corral

Robles–Burgueño

et al. 2020

World Allergy Organization Journal

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Background: Red oak pollen is an important cause of allergic respiratory disease and it is widely distributed in North America and central Europe. To date, however, red oak pollen allergens have not been identified. Here, we describe the allergenic protein profile from red oak pollen. Methods: Total proteins were extracted from red oak pollen using a modified phenolic extraction method, and, subsequently, proteins were separated by two-dimensional gel electrophoresis (2DE) for both total protein stain (Coomassie Blue) and immunoblotting. A pool of 8 sera from red oak sensitive patients was used to analyze blotted proteins. Protein spots were analyzed by Mass Spectrometry. Results: Electrophoretic pattern of total soluble proteins showed higher intensity bands in the regions of 26-40 and 47-52 kDa. Two dimensional immunoblots using pool sera from patients revealed four allergenic proteins spots with molecular masses in the range from 50 to 55 kDa. Mass spectrometry analysis identified 8 proteins including Enolase 1 and Enolase 1 chloroplastic, Xylose isomerase (X1 isoform), mitochondrial Aldehyde dehydrogenase, UTP-Glusose-1phosphate uridylyltransferase, Betaxylosidase/alpha-L-arabinofuranosidase and alpha-and beta subunits of ATP synthase. Conclusions: This study has identified for first time 8 IgE binding proteins from red oak pollen. These findings will pave the way towards the development of new diagnostic and therapeutic modalities for red oak allergy.

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“…It is responsible for ATP synthesis and also participates as a novel plant cell death regulator protein. It was reported as an allergen from Cannabis sativa [ 32 ], Ligustrum lucidum [ 33 ] pollen grains and cow dander [ 34 ].…”

Section: Discussionmentioning

confidence: 99%

Clinical and immuno-proteomic approach on Lantana camara pollen allergy—a major health hazard

Ghosal

Saha

Bhattacharya

2016

Allergy Asthma Clin Immunol

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BackgroundThe incidence of allergic diseases is increasing gradually and is a global burden affecting the socio-economic quality of life. Identification of allergens is the first step towards paving the way for therapeutic interventions against atopic diseases. Our previous investigation figured out that total pollen load correlated significantly with the rise of respiratory allergy in a subtropical city in India. The most dominant pollen responsible for IgE sensitivity in most patients emerged to be from Lantana camara (LC) an obnoxious weed growing in and around suburban areas of West Bengal. In this study, we identified allergenic components from this shrub using an immunoproteomic approach.MethodsDetermination of dominant pollen species was done using aerobiological sampling during two consecutive years and correlated with hospitalization and skin prick test. Serum was collected from LC positive patients and checked for in vitro allergenicity using ELISA and Histamine assay. Total proteome was profiled in SDS–PAGE, 2D PAGE and immunoblotted to detect IgE binding proteins which were further identified using mass spectrometry.ResultsLantana camara pollen emerged as a significant contributor from the correlation study with hospital admission of the respiratory allergy sufferers and its extract demonstrated an elevated IgE response in ELISA and histamine release assay tests. Five IgE reactive bands/zones were observed in 1D blot which resolved to 12 allergo-reactive spots in the 2D blot. Mass spectrometric analysis identified nine spots that grouped into four diverse proteins. Pathogenesis-related Thaumatin-like protein was found to be one of the major allergens in Lantana camara.ConclusionsThis is to our knowledge the first attempt to identify allergens from Lantana camara using a proteomic approach. The allergens identified thereof can be used to prepare hypoallergenic vaccine candidates and design immunotherapy trials against LC pollen and other aeroallergen carriers which are cross-reactive and harbor similar proteins.Electronic supplementary materialThe online version of this article (doi:10.1186/s13223-016-0135-z) contains supplementary material, which is available to authorized users.

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Identification of Ligustrum lucidum pollen allergens using a proteomics approach

Cited by 19 publications

References 20 publications

Proteomic Analysis and Identification of Possible Allergenic Proteins in Mature Pollen of Populus tomentosa

Proteomic Analysis and Identification of Possible Allergenic Proteins in Mature Pollen of Populus tomentosa

Proteomic identification of allergenic proteins in red oak (Quercus rubra) pollen

Clinical and immuno-proteomic approach on Lantana camara pollen allergy—a major health hazard

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