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1.
PRRs and NB-LRRs: From Signal Perception to Activation of Plant Innate Immunity.
Noman, A, Aqeel, M, Lou, Y
International journal of molecular sciences. 2019;(8)
Abstract
To ward off pathogens and pests, plants use a sophisticated immune system. They use pattern-recognition receptors (PRRs), as well as nucleotide-binding and leucine-rich repeat (NB-LRR) domains, for detecting nonindigenous molecular signatures from pathogens. Plant PRRs induce local and systemic immunity. Plasma-membrane-localized PRRs are the main components of multiprotein complexes having additional transmembrane and cytosolic kinases. Topical research involving proteins and their interactive partners, along with transcriptional and posttranscriptional regulation, has extended our understanding of R-gene-mediated plant immunity. The unique LRR domain conformation helps in the best utilization of a surface area and essentially mediates protein-protein interactions. Genome-wide analyses of inter- and intraspecies PRRs and NB-LRRs offer innovative information about their working and evolution. We reviewed plant immune responses with relevance to PRRs and NB-LRRs. This article focuses on the significant functional diversity, pathogen-recognition mechanisms, and subcellular compartmentalization of plant PRRs and NB-LRRs. We highlight the potential biotechnological application of PRRs and NB-LRRs to enhance broad-spectrum disease resistance in crops.
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2.
Pistachio nut allergy: An updated overview.
Costa, J, Silva, I, Vicente, AA, Oliveira, MBPP, Mafra, I
Critical reviews in food science and nutrition. 2019;(4):546-562
Abstract
Pistachio nut (Pistacia vera) is highly appreciated for its organoleptic characteristics and potential health benefits. However, this tree nut is also responsible for triggering moderate to severe IgE-mediated reactions in allergic individuals. Currently, pistachio nut allergy has gained some special attention, mainly due to its intrinsic relation with cashew nut allergy. Like for other nuts, the prevalence of pistachio nut allergy seems to be increasing at a global scale. Until now, there are five allergenic proteins officially listed for pistachio nut (Pis v 1, Pis v 2, Pis v 3, Pis v 4 and Pis v 5). Relevant data on their biochemical classification has become available, enabling establishing a correlation with the respective clinical symptoms. The establishment of an effective allergen risk assessment is a key issue for the food industry, policy makers and regulatory agencies. Thus, the availability of fast, specific and sensitive methods to detect trace amounts of allergens in processed foods is crucial. In the specific case of pistachio nut, there are some protein- and DNA-based methods for its detection/quantification in foods, which can aid to verify label information. Accordingly, all relevant research advances on this topic were summarised, updated and critically discussed in this review.
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3.
NMR resonance assignments of the pathogenesis-related peach allergen Pru p 1.0101.
Führer, S, Trimmel, S, Breuker, K, Tollinger, M
Biomolecular NMR assignments. 2019;(1):127-130
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Abstract
In Europe, Northern America, and China a large number of individuals are suffering from peach (Prunus persica) allergy caused by the protein Pru p 1. Immunologic reactions against this 17.5 kDa protein result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1 and subsequent immunologic cross-reactivity of Bet v 1 specific antibodies. Allergic symptoms typically include severe itching, scratching of the throat, and rhino conjunctivitis. So far, experimental structural data for the peach allergen Pru p 1 are not available. In a first step towards the elucidation of the structure of this protein we assigned backbone and side chain 1H, 13C, and 15N chemical shifts of the naturally occurring isoform Pru p 1.0101 by solution NMR spectroscopy. Our chemical shift data indicate that this protein fold consists of seven β-strands separated by two short α-helices and a long C-terminal α-helix, which is in accordance with the reported crystal structure of Bet v 1. Our data provide the basis for determining the three-dimensional solution structure of this protein and to characterize its immunologic cross-reactivity on a structural basis.
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4.
Qualitative assessment of 'highly digestible' protein mutation in hard endosperm sorghum and its functional properties.
Teferra, TF, Amoako, DB, Rooney, WL, Awika, JM
Food chemistry. 2019;:561-569
Abstract
Sorghum mutants with altered protein body structure have improved protein nutritional quality; however, practical methods to accurately track heritability of the trait are lacking. We evaluated suitability of the in vitro pepsin assay, and a new high-resolution field emission electron microscopy (FE-SEM) method to detect the mutation (HD) in hard-endosperm sorghum; and compared the physicochemical properties of experimental HD sorghums to wild type (LD) lines. FE-SEM reliably resolved sorghum protein body structure, allowing for qualitative classification of sorghum as HD or LD. The pepsin assay was less reliable, with significant variations across environments. Nevertheless, HD lines averaged higher protein digestibility (69.4% raw, 57.6% cooked) than LD lines (61.7% raw, 45.6% cooked). The HD lines also had better water solubility and starch pasting profiles than LD lines. FE-SEM, but not pepsin assay, reliably detects HD nutation in sorghum. The HD trait may improve food-use functionality of sorghum.
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5.
The Molecular Mechanisms Underlying Iron Deficiency Responses in Rice.
Li, Q, Chen, L, Yang, A
International journal of molecular sciences. 2019;(1)
Abstract
Iron (Fe) is an essential element required for plant growth and development. Under Fe-deficientconditions, plants have developed two distinct strategies (designated as strategy I and II) to acquire Fe from soil. As a graminaceous species, rice is not a typical strategy II plant, as it not only synthesizes DMA (2'-deoxymugineic acid) in roots to chelate Fe3+ but also acquires Fe2+ through transporters OsIRT1 and OsIRT2. During the synthesis of DMA in rice, there are three sequential enzymatic reactions catalyzed by enzymes NAS (nicotianamine synthase), NAAT (nicotianamine aminotransferase), and DMAS (deoxymugineic acid synthase). Many transporters required for Fe uptake from the rhizosphere and internal translocation have also been identified in rice. In addition, the signaling networks composed of various transcription factors (such as IDEF1, IDEF2, and members of the bHLH (basic helix-loop-helix) family), phytohormones, and signaling molecules are demonstrated to regulate Fe uptake and translocation. This knowledge greatly contributes to our understanding of the molecular mechanisms underlying iron deficiency responses in rice.
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6.
Proteomic Identification of Allergenic Proteins of Morus alba L. Pollenexacerbation.
Çetereisi, D, Karlioglu, N, Gelincik, A, Michelland, S, Önay-Uçar, E, Ertek, B, Akdeniz, N, Erden, S, Çolkoglu, B, Akkemik, Ü, et al
Asian Pacific journal of allergy and immunology. 2019;(4):205-211
Abstract
BACKGROUND Tree pollens are well-known aeroallergens all over the world. Little is known about the allergenicity of Morus alba (white mulberry) pollen. OBJECIVE We aimed to explore the potential allergens of this pollen and its clinical relevance in tree pollen allergic patients living in Istanbul, Turkey. METHODS Twenty three seasonal allergic rhinitis patients with a confirmed tree pollen allergy and 5 healthy control subjects underwent skin prick and nasal provocation tests with M.alba pollen extract. The pollen extract was then resolved by gel electrophoresis, and immunoblotted with sera from patients/control individuals to detect the potential allergenic proteins. The prevalent IgE binding proteins from 1D-gel were analyzed by MALDI-TOF/TOF. RESULTS Eleven out of 23 patients were reactive to the extract with skin prick tests. Seven of those patients also reacted positively to the nasal provocation tests. The most common IgE-binding pollen proteins were detected between 55-100 kDa, and also at molecular weights lower than 30 kDa for some patients. Mass spectrometry analyses revealed that the principal IgE-binding protein was methionine synthase (5-methyltetrahydropteroyltriglutamate homocysteine methyltransferase), which is then proposed as a novel allergen in M.alba pollen. CONCLUSION This study provides the first detailed information for the potential allergens of Morus alba pollen of Istanbul. Methionine synthase with an apparent molecular weight of 80 to 85 kDa has been recognized as one of the allergens in Morus alba pollen for the first time.
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7.
Cell Wall Proteins Play Critical Roles in Plant Adaptation to Phosphorus Deficiency.
Wu, W, Zhu, S, Chen, Q, Lin, Y, Tian, J, Liang, C
International journal of molecular sciences. 2019;(21)
Abstract
Phosphorus is one of the mineral nutrient elements essential for plant growth and development. Low phosphate (Pi) availability in soils adversely affects crop production. To cope with low P stress, remodeling of root morphology and architecture is generally observed in plants, which must be accompanied by root cell wall modifications. It has been documented that cell wall proteins (CWPs) play critical roles in shaping cell walls, transmitting signals, and protecting cells against environmental stresses. However, understanding of the functions of CWPs involved in plant adaptation to P deficiency remains fragmentary. The aim of this review was to summarize advances in identification and functional characterization of CWPs in responses to P deficiency, and to highlight the critical roles of CWPs in mediating root growth, P reutilization, and mobilization in plants.
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8.
Plant-Microbe Symbiosis: What Has Proteomics Taught Us?
Khatabi, B, Gharechahi, J, Ghaffari, MR, Liu, D, Haynes, PA, McKay, MJ, Mirzaei, M, Salekdeh, GH
Proteomics. 2019;(16):e1800105
Abstract
Beneficial microbes have a positive impact on the productivity and fitness of the host plant. A better understanding of the biological impacts and underlying mechanisms by which the host derives these benefits will help to address concerns around global food production and security. The recent development of omics-based technologies has broadened our understanding of the molecular aspects of beneficial plant-microbe symbiosis. Specifically, proteomics has led to the identification and characterization of several novel symbiosis-specific and symbiosis-related proteins and post-translational modifications that play a critical role in mediating symbiotic plant-microbe interactions and have helped assess the underlying molecular aspects of the symbiotic relationship. Integration of proteomic data with other "omics" data can provide valuable information to assess hypotheses regarding the underlying mechanism of symbiosis and help define the factors affecting the outcome of symbiosis. Herein, an update is provided on the current and potential applications of symbiosis-based "omic" approaches to dissect different aspects of symbiotic plant interactions. The application of proteomics, metaproteomics, and secretomics as enabling approaches for the functional analysis of plant-associated microbial communities is also discussed.
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9.
The Function of Inositol Phosphatases in Plant Tolerance to Abiotic Stress.
Jia, Q, Kong, D, Li, Q, Sun, S, Song, J, Zhu, Y, Liang, K, Ke, Q, Lin, W, Huang, J
International journal of molecular sciences. 2019;(16)
Abstract
Inositol signaling is believed to play a crucial role in various aspects of plant growth and adaptation. As an important component in biosynthesis and degradation of myo-inositol and its derivatives, inositol phosphatases could hydrolyze the phosphate of the inositol ring, thus affecting inositol signaling. Until now, more than 30 members of inositol phosphatases have been identified in plants, which are classified intofive families, including inositol polyphosphate 5-phosphatases (5PTases), suppressor of actin (SAC) phosphatases, SAL1 phosphatases, inositol monophosphatase (IMP), and phosphatase and tensin homologue deleted on chromosome 10 (PTEN)-related phosphatases. The current knowledge was revised here in relation to their substrates and function in response to abiotic stress. The potential mechanisms were also concluded with the focus on their activities of inositol phosphatases. The general working model might be that inositol phosphatases would degrade the Ins(1,4,5)P3 or phosphoinositides, subsequently resulting in altering Ca2+ release, abscisic acid (ABA) signaling, vesicle trafficking or other cellular processes.
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10.
Tackling Plant Phosphate Starvation by the Roots.
Crombez, H, Motte, H, Beeckman, T
Developmental cell. 2019;(5):599-615
Abstract
Plant responses to phosphate deprivation encompass a wide range of strategies, varying from altering root system architecture, entering symbiotic interactions to excreting root exudates for phosphorous release, and recycling of internal phosphate. These processes are tightly controlled by a complex network of proteins that are specifically upregulated upon phosphate starvation. Although the different effects of phosphate starvation have been intensely studied, the full extent of its contribution to altered root system architecture remains unclear. In this review, we focus on the effect of phosphate starvation on the developmental processes that shape the plant root system and their underlying molecular pathways.