Allergenic Properties and Molecular Characteristics of PR-1 Proteins

Wangorsch, Andrea; Scheurer, Stephan; Blanca, Miguel; Blanca‐López, Natalia; Somoza, María Luisa; Martín‐Pedraza, Laura

doi:10.3389/falgy.2022.824717

Cited by 16 publications

(8 citation statements)

References 65 publications

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“…They are among the most strongly expressed and abundant PR proteins and can account for up to 2% of total leaf proteins in tobacco (Lu et al, 2011 ; Niderman et al, 1995 ; van Loon & van Kammen, 1970 ; van Loon & van Strien, 1999 ). Some PR1 family members from tomato, potato, oilseed rape, and maize have IgE‐sensitizing capacity and thus act as plant allergens (Wangorsch et al, 2022 ). Most PR1 family members contain only a CAP domain and relatively short C‐ and N‐terminal extensions, indicating that the CAP domain determines their function in plant pathogen defence.…”

Section: Plants Recognize Pathogens and Mount An Immune Responsementioning

confidence: 99%

The function of plant PR1 and other members of the CAP protein superfamily in plant–pathogen interactions

Han

Xiong

Schneiter

et al. 2023

Molecular Plant Pathology

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The pathogenesis‐related (PR) proteins of plants have originally been identified as proteins that are strongly induced upon biotic and abiotic stress. These proteins fall into 17 distinct classes (PR1–PR17). The mode of action of most of these PR proteins has been well characterized, except for PR1, which belongs to a widespread superfamily of proteins that share a common CAP domain. Proteins of this family are not only expressed in plants but also in humans and in many different pathogens, including phytopathogenic nematodes and fungi. These proteins are associated with a diverse range of physiological functions. However, their precise mode of action has remained elusive. The importance of these proteins in immune defence is illustrated by the fact that PR1 overexpression in plants results in increased resistance against pathogens. However, PR1‐like CAP proteins are also produced by pathogens and deletion of these genes results in reduced virulence, suggesting that CAP proteins can exert both defensive and offensive functions. Recent progress has revealed that plant PR1 is proteolytically cleaved to release a C‐terminal CAPE1 peptide, which is sufficient to activate an immune response. The release of this signalling peptide is blocked by pathogenic effectors to evade immune defence. Moreover, plant PR1 forms complexes with other PR family members, including PR5, also known as thaumatin, and PR14, a lipid transfer protein, to enhance the host's immune response. Here, we discuss possible functions of PR1 proteins and their interactors, particularly in light of the fact that these proteins can bind lipids, which have important immune signalling functions.

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Section: Plants Recognize Pathogens and Mount An Immune Responsementioning

confidence: 99%

The function of plant PR1 and other members of the CAP protein superfamily in plant–pathogen interactions

Han

Xiong

Schneiter

et al. 2023

Molecular Plant Pathology

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“…Among the 31 selected effector candidates, an interesting finding is that effector candidate Mycgr3109710 localizes to the nucleus and labels mobile cytosolic bodies that are predominantly located at the cell periphery when expressed in Nicotiana . This effector candidate is annotated as a member of the Allergen V5/Tpx-1 related group, which are cysteine-rich secretory proteins (Crips) including proteins of the PR-1 family and potent allergens (Wangorsch et al, 2022). Protein feature analysis using InterProScan revealed cystine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) and sperm-coating protein (SCP) domains in Mycgr3109710, indicating its association with the homologous PR-1-like superfamily.…”

Section: Discussionmentioning

confidence: 99%

Mechanisms of infection and response of the fungal wheat pathogenZymoseptoria triticiduring compatible, incompatible and non-host interactions

Gomez-Gutierrez,

Million,

Jaiswal

et al. 2023

Preprint

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Zymoseptoria triticiincites Septoria tritici blotch, a disease causing significant annual yield losses in wheat. To investigate infection phase-specific gene expression in the pathogen we analyzed gene expression during infection of susceptible (Taichung 29) and resistant (Veranopolis and Israel 493) wheat cultivars, plus the non-host species barley at 1, 3, 6, 10, 17 and 23 days post-inoculation (DPI). There were dramatic differences in pathogen gene expression at 10 DPI in the compatible compared to both incompatible interactions. The largest differences in pathogen gene expression occurred at 3 DPI in both compatible and incompatible interactions compared to the non-host interaction. Thirty-one putative effectors had early expression in the compatible interaction. Subsequent subcellular localization studies usingAgrobacterium-mediated transient expression inNicotiana benthamianarevealed that most candidate effectors localized to the nucleus and cytosol, and two localized to mobile cytosolic bodies, suggesting involvement in intracellular signaling or host gene regulation. Mycgr3109710, which localized to cytosolic bodies, belongs to the non-plant PR-1-like protein family implicated in virulence in other pathogens. Comparison of pathogen gene expression in resistant and susceptible hosts, in which an initial colonization is established, versus in the non-host species, allowed us to identify genes involved in establishing infection. Comparison of the compatible and incompatible interactions identified pathogen genes involved in transition from biotrophic to necrotrophic growth at 10 DPI. In addition, we contribute to the understanding of candidate effectors that are activated early during infection and might be involved in the initial plant immunity suppression.

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“…An in-depth characterisation of the wasp venom proteome and transcriptome revealed that it is rich in various types of hyperallergic components, including arginine kinase, CAP, hyaluronidase, maltase, and phospholipase ( Figure 2 ; Supplentary Table S3 ), which have been previously reported from several hymenopterans ( Bilo et al, 2005 ; Hoffman et al, 2005 ; Hemmer and Wantke, 2020 ). The CAP superfamily of proteins that constituted nearly one-fourth of the wasp venom proteome (∼26%), are well-known for their role in inhibiting various ion-channels, modulation of vascular permeability and eliciting IgE-mediated immune reactions ( Tadokoro et al, 2020 ; Wangorsch et al, 2022 ). Similarly, hymenopteran PLA 1 s, which constitute 21.86% of the V. affinis venom, are shown to be hyperallergic ( Sookrung et al, 2014 ).…”

Section: Discussionmentioning

confidence: 99%

Stings on wings: Proteotranscriptomic and biochemical profiling of the lesser banded hornet (Vespa affinis) venom

Sunagar

Khochare

Jaglan

et al. 2022

Front. Mol. Biosci.

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Distinct animal lineages have convergently recruited venoms as weaponry for prey capture, anti-predator defence, conspecific competition, or a combination thereof. Most studies, however, have been primarily confined to a narrow taxonomic breadth. The venoms of cone snails, snakes, spiders and scorpions remain particularly well-investigated. Much less explored are the venoms of wasps (Order: Hymenoptera) that are infamous for causing excruciating and throbbing pain, justifying their apex position on Schmidt’s pain index, including some that are rated four on four. For example, the lesser banded wasp (V. affinis) is clinically important yet has only been the subject of a few studies, despite being commonly found across tropical and subtropical Asia. Stings from these wasps, especially from multiple individuals of a nest, often lead to clinically severe manifestations, including mastocytosis, myasthenia gravis, optic neuropathy, and life-threatening pathologies such as myocardial infarction and organ failure. However, their venom composition and activity remain unexplored in the Indian subcontinent. Here, we report the proteomic composition, transcriptomic profile, and biochemical and pharmacological activities of V. affinis venom from southern India. Our findings suggest that wasp venoms are rich in diverse toxins that facilitate antipredator defence. Biochemical and pharmacological assessments reveal that these toxins can exhibit significantly higher activities than their homologues in medically important snakes. Their ability to exert potent effects on diverse molecular targets makes them a treasure trove for discovering life-saving therapeutics. Fascinatingly, wasp venoms, being evolutionarily ancient, exhibit a greater degree of compositional and sequence conservation across very distant populations/species, which contrasts with the patterns of venom evolution observed in evolutionarily younger lineages, such as advanced snakes and cone snails.

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Allergenic Properties and Molecular Characteristics of PR-1 Proteins

Cited by 16 publications

References 65 publications

The function of plant PR1 and other members of the CAP protein superfamily in plant–pathogen interactions

The function of plant PR1 and other members of the CAP protein superfamily in plant–pathogen interactions

Mechanisms of infection and response of the fungal wheat pathogenZymoseptoria triticiduring compatible, incompatible and non-host interactions

Stings on wings: Proteotranscriptomic and biochemical profiling of the lesser banded hornet (Vespa affinis) venom

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