The Potential ofBetv1Homologues, a Nuclear Multigene Family, as Phylogenetic Markers in Flowering Plants

Wen, Jun; Vanek-Krebitz, M; Hoffmann‐Sommergruber, Karin; Scheiner, Otto; Breiteneder, Heimo

doi:10.1006/mpev.1997.0447

Cited by 78 publications

(55 citation statements)

References 61 publications

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“…A search against the Pfam database resulted in high confident annotations for both proteins, matching against the Bet v I allergen protein family. In fact, members of the Bet v I allergen protein family are storage proteins that occur across dicotyledonous plants (41) and have been shown to be cytokinin-binding proteins (42). Together, the expression patterns observed, as well as annotations provided through protein family memberships, suggest biological roles impacting multiple aspects of plant development, including cell growth and sink and source relationships.…”

Section: Resultsmentioning

confidence: 97%

Putting the Pieces Together: High-performance LC-MS/MS Provides Network-, Pathway-, and Protein-level Perspectives in Populus

Abraham

Giannone

Adams

et al. 2013

Molecular & Cellular Proteomics

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High-performance mass spectrometry (MS)-based proteomics enabled the construction of a detailed proteome atlas for Populus, a woody perennial plant model organism. Optimization of experimental procedures and implementation of current state-of-the-art instrumentation afforded the most detailed look into the predicted proteome space of Populus, offering varying proteome perspectives: (1) network-wide, (2) pathway-specific, and (3) protein-level viewpoints. Together, enhanced protein retrieval through a detergent-based lysis approach and maximized peptide sampling via the dual-pressure linear ion trap mass spectrometer (LTQ Velos), have resulted in the identification of 63,056 tryptic peptides. The technological advancements, specifically spectral-acquisition and sequencing speed, afforded the deepest look into the Populus proteome, with peptide abundances spanning 6 orders of magnitude and mapping to ϳ25% of the predicted proteome space. In total, tryptic peptides mapped to 11,689 protein assignments across four organ-types: mature (fully expanded, leaf plastichronic index (LPI) 10 -12) leaf, young (juvenile, LPI 4 -6) leaf, root, and stem. To resolve protein ambiguity, identified proteins were grouped by sequence similarity (> 90%), thereby reducing the protein assignments into 7538 protein groups. In addition, this large-scale data set features the first systemswide survey of protein expression across different Populus organs. As a demonstration of the precision and comprehensiveness of the semiquantitative analysis, we were able to contrast two stages of leaf development, mature versus young leaf. Statistical comparison through ANOVA analysis revealed 1432 protein groups that exhibited statistically significant (p < 0.01) differences in protein abundance. Experimental validation of the metabolic circuitry expected in mature leaf (characterized by photosynthesis and carbon fixation) compared with young leaf (characterized by rapid growth and moderate photosynthetic activities) strongly testifies to the credibility of the approach. Mass spectrometry (MS)-based proteomics has experienced tremendous growth in recent years, leading to the establishment of numerous protocols, platforms, and workflows for the characterization of protein expression at the genome level (1). Although these advancements have facilitated comprehensive proteomic investigations of simple bacterial isolates and microbial communities, the application of MS-based proteomics for plants and other higher eukaryotes remains underdeveloped. Recently, large-scale proteomic studies have been directed at characterization of Populus, a woody perennial model organism. With the recent release and subsequent curation of the P. trichocarpa genome (2), these large-scale MS-based proteomic investigations offer the potential to introduce new biological insights into woody perennial plant biology (3,4,5). For example, we have recently demonstrated the ability to measure ϳ17% of the Populus proteome by coupling multidimensional liquid chromatography (MudPIT) 1 w...

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Section: Resultsmentioning

confidence: 97%

Putting the Pieces Together: High-performance LC-MS/MS Provides Network-, Pathway-, and Protein-level Perspectives in Populus

Abraham

Giannone

Adams

et al. 2013

Molecular & Cellular Proteomics

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“…Proteins from ginseng have been shown to display ribonuclease activity [73], but for other members no or rather weak activity was found [74]. It is noteworthy that all these proteins are encoded by multiple genes (designated Ypr10 according to van Loon and van Strien [3]), forming a monophyletic group and representing potential phylogenetic markers within or among closely related families in flowering plants [75]. The widespread occurrence and the conservation of these proteins within the plant kingdom indicates an important role.…”

Section: Pr-10 Intracellular Proteins With Unknown Enzymatic Functionmentioning

confidence: 99%

Plant Allergens and Pathogenesis-Related Proteins

Hoffmann‐Sommergruber

2000

Int Arch Allergy Immunol

170

114

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In the recent past a great number of proteins causing type 1 allergic reactions in humans have been isolated and characterised. The main sources containing allergens are plants, mites, fungal spores and insects. Plant-derived allergens may either be taken in from the upper respiratory tract or they are present in a vast range of plant food causing food allergic reactions. Compared to the enormous amount of different plant proteins only a small number out of them are identified as a an allergen at present. Looking at the allergen encoding sequences, relationships by sequence similarity can be found quite frequently to a restricted number of plant protein families. Predominantly, these protein families are seed storage proteins, structural proteins and proteins involved in the defence-related system – pathogenesis-related proteins. In the following, a short overview of a number of pathogenesis-related protein families is presented in relation to the already known homologous plant allergens.

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“…This family is classified by sequence similarity into three sub-families: pathogenesis-related (PR)-10, Bet v 1 major allergen, and ripening-related (RRP) proteins (Ivanciuc et al, 2009). PR-10 includes a majority of allergens in those three sub-families (Wen et al, 1997). Bet v 1 is the major birch pollen allergen.…”

Section: Bioinformatics Analysis and Classification Of The Test Food mentioning

confidence: 99%

Food proteins from different allergen families sensitize Balb/c mice to family-specific immune responses

Wang

Sun

Zhou

et al. 2013

Journal of Immunotoxicology

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The classification of food allergens based on the structure and function of proteins contributes to the study of the relationship between bioinformatics and potential allergenicity of allergens. Food allergens always share sequence similarity with the allergens in the same allergen families. For that reason, food proteins from different allergen families may induce different patterns of immune responses in animal models. Female Balb/c mice (3-4-weeks-old) were sensitized with food proteins once per week for 4 weeks, and then challenged 2 weeks later (on Day 42 of study). Blood was collected (to obtain serum levels of histamine and protein-specific IgG 1 and IgE antibodies) and measures of vascular permeability were performed 20 min after the challenge. Five food proteins (11S globulin, OVA [ovalbumin], HAS [human serum albumin] and LRP [lysine-responsive storage protein] of different allergen families, and Cry 1Ab/Ac [crystal protein]) were used to assess patterns of immune responses for each allergen family and then bioinformatics and digestive stability in simulated gastric fluid were employed to assess the overall utility of the Balb/c. The assay results indicated that, in this model, histamine and protein-specific IgE antibody levels and vascular permeability could be used to identify allergenicity of 11S globulin, OVA, and PAP (potato acid phosphatase) only. However, the results of the protein-specific IgG 1 measures could only distinguish allergic food proteins with negative control. Based on bioinformatic analyses, the five different food proteins clearly induced distinct patterns of immune responses in the Balb/c model.

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The Potential ofBetv1Homologues, a Nuclear Multigene Family, as Phylogenetic Markers in Flowering Plants

Cited by 78 publications

References 61 publications

Putting the Pieces Together: High-performance LC-MS/MS Provides Network-, Pathway-, and Protein-level Perspectives in Populus

Putting the Pieces Together: High-performance LC-MS/MS Provides Network-, Pathway-, and Protein-level Perspectives in Populus

Plant Allergens and Pathogenesis-Related Proteins

Food proteins from different allergen families sensitize Balb/c mice to family-specific immune responses

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