Identification and functionality prediction of pathogenesis‐related protein 1 from legume family

Tellis, Meenakshi; Mathur, Monika; Gurjar, Gayatri; Kadoo, Narendra Y.; Gupta, Vidya S.

doi:10.1002/prot.25361

Cited by 10 publications

(7 citation statements)

References 48 publications

(44 reference statements)

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“…A notable exception to this trend was the strong overexpression of the PATHOGENESIS-RELATED protein 1 (PR-1) family member PHAVU_006G196900g. PR-1 proteins represent common markers of the late, salicylic acid-driven pathogenic response [ 46 ]. Similarly, besides a WRKY transcription factor (PHAVU_004G105800g), a protein belonging to the ENHANCED DISEASE SUSCEPTIBILITY TO ERYSIPHE ORONTII family (PHAVU_010G011700g) and three disease resistance proteins (PHAVU_010G028700g, PHAVU_010G027300g and PHAVU_010G028800g), very few genes related to this functional category were found significantly down-regulated in nifA nodules compared to P. phymatum wild-type nodules.…”

Section: Resultsmentioning

confidence: 99%

Metabolomics and Dual RNA-Sequencing on Root Nodules Revealed New Cellular Functions Controlled by Paraburkholderia phymatum NifA

et al. 2021

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Paraburkholderia phymatum STM815 is a nitrogen-fixing endosymbiont that nodulate the agriculturally important Phaseolus vulgaris and several other host plants. We previously showed that the nodules induced by a STM815 mutant of the gene encoding the master regulator of nitrogen fixation NifA showed no nitrogenase activity (Fix−) and increased in number compared to P. vulgaris plants infected with the wild-type strain. To further investigate the role of NifA during symbiosis, nodules from P. phymatum wild-type and nifA mutants were collected and analyzed by metabolomics and dual RNA-Sequencing, allowing us to investigate both host and symbiont transcriptome. Using this approach, several metabolites’ changes could be assigned to bacterial or plant responses. While the amount of the C4-dicarboxylic acid succinate and of several amino acids was lower in Fix− nodules, the level of indole-acetamide (IAM) and brassinosteroids increased. Transcriptome analysis identified P. phymatum genes involved in transport of C4-dicarboxylic acids, carbon metabolism, auxin metabolism and stress response to be differentially expressed in absence of NifA. Furthermore, P. vulgaris genes involved in autoregulation of nodulation (AON) are repressed in nodules in absence of NifA potentially explaining the hypernodulation phenotype of the nifA mutant. These results and additional validation experiments suggest that P. phymatum STM815 NifA is not only important to control expression of nitrogenase and related enzymes but is also involved in regulating its own auxin production and stress response. Finally, our data indicate that P. vulgaris does sanction the nifA nodules by depleting the local carbon allocation rather than by mounting a strong systemic immune response to the Fix− rhizobia.

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Section: Resultsmentioning

confidence: 99%

Metabolomics and Dual RNA-Sequencing on Root Nodules Revealed New Cellular Functions Controlled by Paraburkholderia phymatum NifA

et al. 2021

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“…Several allergens have been identified as members of the pathogenesis-related (PR) protein families, PR-2 (ß-1-3 Glucanases), PR-3 and PR-4 (Chitinase), PR-5 (Thaumatin-like), PR-8 (Chitinase), PR-10 (Bet v 1-like), PR-14 (nsLTPs) ( 1 , 2 ), and from the PR-1 family ( 3 ). The PR proteins of the same family are known to have highly-homologous sequences and similar functions ( 4 ).…”

Section: Introductionmentioning

confidence: 99%

“…The classification of PR-1 proteins is not consistent. On one hand, PR-1 proteins were classified as either cysteine-rich secretory proteins (CRISP) or antigen 5 (Ag5) type proteins ( 4 ). These proteins either belong to sperm coating protein (SCP)-like extracellular protein family, PR-1 protein family, or allergen V5/Tpx-1-related protein family ( 4 ), as part of the SCP/TAPS (Tpx-1/Ag5/PR-1/Sc7) protein superfamily ( 5 , 6 ).…”

Section: Introductionmentioning

confidence: 99%

“…On one hand, PR-1 proteins were classified as either cysteine-rich secretory proteins (CRISP) or antigen 5 (Ag5) type proteins ( 4 ). These proteins either belong to sperm coating protein (SCP)-like extracellular protein family, PR-1 protein family, or allergen V5/Tpx-1-related protein family ( 4 ), as part of the SCP/TAPS (Tpx-1/Ag5/PR-1/Sc7) protein superfamily ( 5 , 6 ). In another classification, PR-1 proteins are described as members of a CAP protein superfamily, encompassing the Cysteine-rich secretory proteins in vertebrates, Antigen 5 in insects, and PR-1 in plants ( 7 – 9 ).…”

Section: Introductionmentioning

confidence: 99%

“…PR-1 expression is induced by salicylic acid signaling, but the molecular mechanism to achieve disease resistance is not known ( 8 ). Domain analysis indicated that most PR-1 proteins have a conserved α βα sandwich folded CAP domain of 150 amino acids ( 4 , 9 ). The CAP domain comprises the whole PR-1 protein and contains four conserved signature motifs (CAP1-4), with six specific cysteine residues encompassing 3 disulfide bonds ( Figure 1A ) ( 10 ) and is attributed to ion-, fatty acid, and sterol-binding capacity ( 8 , 9 , 13 ).…”

Section: Introductionmentioning

confidence: 99%

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Allergenic Properties and Molecular Characteristics of PR-1 Proteins

et al. 2022

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Only a small fraction of proteins in plants and animals are classified as allergens. The allergenic properties are frequently attributed to certain functional characteristics of the proteins, such as a role in the plant defense against biotic and abiotic stress, to achieve the systematic acquired resistance. In line with this, eight members out of 17 functional pathogenesis-related (PR) protein families have been characterized as allergens. The present review summarizes the molecular features and allergenic significance of allergens of the PR-1 family. Not many allergens have been identified as belonging to this protein family, with most of them having a pollen origin, like mugwort or Bermuda grass. Molecular and structural features of allergenic PR-1 proteins are discussed and attributed to their IgE-reactive properties, clinical manifestation, and cross-reactivity among different foods and inhalants.

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