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Phytochemistry Sep 2015Plants have evolved to synthesize a variety of noxious compounds to cope with unfavorable circumstances, among which a large group of toxic proteins that play a critical... (Review)
Review
Plants have evolved to synthesize a variety of noxious compounds to cope with unfavorable circumstances, among which a large group of toxic proteins that play a critical role in plant defense against predators and microbes. Up to now, a wide range of harmful proteins have been discovered in different plants, including lectins, ribosome-inactivating proteins, protease inhibitors, ureases, arcelins, antimicrobial peptides and pore-forming toxins. To fulfill their role in plant defense, these proteins exhibit various degrees of toxicity towards animals, insects, bacteria or fungi. Numerous studies have been carried out to investigate the toxic effects and mode of action of these plant proteins in order to explore their possible applications. Indeed, because of their biological activities, toxic plant proteins are also considered as potentially useful tools in crop protection and in biomedical applications, such as cancer treatment. Genes encoding toxic plant proteins have been introduced into crop genomes using genetic engineering technology in order to increase the plant's resistance against pathogens and diseases. Despite the availability of ample information on toxic plant proteins, very few publications have attempted to summarize the research progress made during the last decades. This review focuses on the diversity of toxic plant proteins in view of their toxicity as well as their mode of action. Furthermore, an outlook towards the biological role(s) of these proteins and their potential applications is discussed.
Topics: Animals; Humans; Plant Proteins; Plants
PubMed: 26057229
DOI: 10.1016/j.phytochem.2015.05.020 -
Toxins Apr 2024The control of crop diseases caused by fungi remains a major problem and there is a need to find effective fungicides that are environmentally friendly. Plants are an... (Review)
Review
The control of crop diseases caused by fungi remains a major problem and there is a need to find effective fungicides that are environmentally friendly. Plants are an excellent source for this purpose because they have developed defense mechanisms to cope with fungal infections. Among the plant proteins that play a role in defense are ribosome-inactivating proteins (RIPs), enzymes obtained mainly from angiosperms that, in addition to inactivating ribosomes, have been studied as antiviral, fungicidal, and insecticidal proteins. In this review, we summarize and discuss the potential use of RIPs (and other proteins with similar activity) as antifungal agents, with special emphasis on RIP/fungus specificity, possible mechanisms of antifungal action, and the use of RIP genes to obtain fungus-resistant transgenic plants. It also highlights the fact that these proteins also have antiviral and insecticidal activity, which makes them very versatile tools for crop protection.
Topics: Ribosome Inactivating Proteins; Antifungal Agents; Plant Proteins; Fungi; Plant Diseases; Plants, Genetically Modified; Animals; Fungicides, Industrial
PubMed: 38668617
DOI: 10.3390/toxins16040192 -
International Journal of Molecular... May 2023Plants are colonized by various fungi with both pathogenic and beneficial lifestyles. One type of colonization strategy is through the secretion of effector proteins... (Review)
Review
Plants are colonized by various fungi with both pathogenic and beneficial lifestyles. One type of colonization strategy is through the secretion of effector proteins that alter the plant's physiology to accommodate the fungus. The oldest plant symbionts, the arbuscular mycorrhizal fungi (AMF), may exploit effectors to their benefit. Genome analysis coupled with transcriptomic studies in different AMFs has intensified research on the effector function, evolution, and diversification of AMF. However, of the current 338 predicted effector proteins from the AM fungus , only five have been characterized, of which merely two have been studied in detail to understand which plant proteins they associate with to affect the host physiology. Here, we review the most recent findings in AMF effector research and discuss the techniques used for the functional characterization of effector proteins, from their in silico prediction to their mode of action, with an emphasis on high-throughput approaches for the identification of plant targets of the effectors through which they manipulate their hosts.
Topics: Mycorrhizae; Plants; Plant Proteins; Plant Roots
PubMed: 37298075
DOI: 10.3390/ijms24119125 -
Peptides Aug 2021Hypertension is a risk factor for arteriosclerosis development and is recognized as a silent killer. Certain processed food materials, digested by protease or through... (Review)
Review
Hypertension is a risk factor for arteriosclerosis development and is recognized as a silent killer. Certain processed food materials, digested by protease or through the use of fermentation, have shown exertion of hypotensive effects in human clinical or animal studies, and hypotensive peptides were isolated from them. This review discusses the hypotensive peptides derived from plant proteins, such as grain, soy, vegetables, and seaweeds, and their hypotensive mechanisms. Although angiotensin I-converting enzyme (ACE) inhibition is often noted as one of the mechanisms that may exert antihypertensive effects, ACE inhibitory activity measured by in vitro studies is not associated with the actual hypotensive effect. Thus, this review only highlights the peptide hypotensive effect determined by in vivo studies. This review also discusses the tendency of the amino acid sequence of ACE-inhibitory hypotensive peptides and the possible additional effects of hypotensive peptides independent of ACE inhibition.
Topics: Animals; Humans; Hypotension; Peptide Fragments; Plant Proteins
PubMed: 34023396
DOI: 10.1016/j.peptides.2021.170573 -
Pflugers Archiv : European Journal of... Sep 2020The carbohydrate D-glucose is the main source of energy in living organisms. In contrast to animals, as well as most fungi, bacteria, and archaea, plants are capable to... (Review)
Review
The carbohydrate D-glucose is the main source of energy in living organisms. In contrast to animals, as well as most fungi, bacteria, and archaea, plants are capable to synthesize a surplus of sugars characterizing them as autothrophic organisms. Thus, plants are de facto the source of all food on earth, either directly or indirectly via feed to livestock. Glucose is stored as polymeric glucan, in animals as glycogen and in plants as starch. Despite serving a general source for metabolic energy and energy storage, glucose is the main building block for cellulose synthesis and represents the metabolic starting point of carboxylate- and amino acid synthesis. Finally yet importantly, glucose functions as signalling molecule conveying the plant metabolic status for adjustment of growth, development, and survival. Therefore, cell-to-cell and long-distance transport of photoassimilates/sugars throughout the plant body require the fine-tuned activity of sugar transporters facilitating the transport across membranes. The functional plant counterparts of the animal sodium/glucose transporters (SGLTs) are represented by the proton-coupled sugar transport proteins (STPs) of the plant monosaccharide transporter(-like) family (MST). In the framework of this special issue on "Glucose Transporters in Health and Disease," this review gives an overview of the function and structure of plant STPs in comparison to the respective knowledge obtained with the animal Na-coupled glucose transporters (SGLTs).
Topics: Glucose; Monosaccharide Transport Proteins; Phylogeny; Plant Proteins; Plants
PubMed: 32845347
DOI: 10.1007/s00424-020-02449-3 -
International Journal of Molecular... Jan 2021Advancements in high-throughput "Omics" techniques have revolutionized plant molecular biology research [...].
Advancements in high-throughput "Omics" techniques have revolutionized plant molecular biology research [...].
Topics: Metabolic Networks and Pathways; Plant Proteins; Plants; Proteomics
PubMed: 33466599
DOI: 10.3390/ijms22020766 -
World Journal of Microbiology &... May 2019Antimicrobial proteins, and especially antimicrobial peptides (AMPs) hold great promise in the control of animal and plant diseases with low risk of pathogen resistance.... (Review)
Review
Antimicrobial proteins, and especially antimicrobial peptides (AMPs) hold great promise in the control of animal and plant diseases with low risk of pathogen resistance. The two puroindolines, a and b, from wheat control endosperm softness of the wheat caryopsis (grain), but have also been shown to inhibit the growth and kill various bacteria and fungi, while showing little toxicity to erythrocytes. Puroindolines are small (~ 13 kDa) amphipathic proteins with a characteristic tryptophan-rich domain (TRD) that is part of an 18 or 19 amino acid residue loop subtended by a disulfide bond. This review presents a brief history of the puroindolines, their physical-chemical characteristics, their interaction with lipids and membranes, and their activity as antimicrobial proteins and AMPs. In this latter context, the use of the TRDs of puroindoline a and b in puroindoline AMP function is reviewed. The activity of puroindoline a and b and their AMPs appear to act through similar but somewhat different modes, which may involve membrane binding, membrane disruption and ion channel formation, and intra-cellular nucleic acid binding and metabolic disruption. Natural and synthetic mutants have identified key elements of the puroindolines for antimicrobial activity.
Topics: Amino Acid Sequence; Animals; Anti-Infective Agents; Edible Grain; Plant Proteins; Plants, Genetically Modified; Recombinant Proteins; Sequence Analysis, Protein; Triticum
PubMed: 31134452
DOI: 10.1007/s11274-019-2655-4 -
Molecular Biology Reports Apr 2021Protein changes under drought or water stress conditions have been widely investigated. These investigations have given us enormous understanding of how drought is... (Review)
Review
Protein changes under drought or water stress conditions have been widely investigated. These investigations have given us enormous understanding of how drought is manifested in plants and how plants respond and adopt to such conditions. Chlorophyll fluoroescence, gas exchange, OMICS, biochemical and molecular analyses have shed light on regulation of physiology and photosynthesis of plants under drought. Use of proteomics has greatly increased the repertoire of drought-associated proteins which nevertheless, need to be investigated for their mechanistic and functional roles. Roles of such proteins have been succinctly discussed in various review articles, however more information on their functional role in countering drought is needed. In this review, recent developments in the field, alterations in the abundance of plant proteins in response to drought, monitored through numerous proteomic and immuno-blot analyses, and how these could affect plants growth and development, are discussed.
Topics: Droughts; Photosynthesis; Plant Proteins; Plants; Stress, Physiological
PubMed: 33856605
DOI: 10.1007/s11033-021-06329-6 -
Chemical Reviews Dec 2019This Review explores the class of plant-derived macrocyclic peptides called cyclotides. We include an account of their discovery, characterization, and distribution in... (Review)
Review
This Review explores the class of plant-derived macrocyclic peptides called cyclotides. We include an account of their discovery, characterization, and distribution in the plant kingdom as well as a detailed analysis of their sequences and structures, biosynthesis and chemical synthesis, biological functions, and applications. These macrocyclic peptides are around 30 amino acids in size and are characterized by their head-to-tail cyclic backbone and cystine knot motif, which render them to be exceptionally stable, with resistance to thermal or enzymatic degradation. Routes to their chemical synthesis have been developed over the past two decades, and this capability has facilitated a wide range of mutagenesis and structure-activity relationship studies. In turn, these studies have both led to an increased understanding of their mechanisms of action as well as facilitated a range of applications in agriculture and medicine, as ecofriendly crop protection agents, and as drug leads or scaffolds for pharmaceutical design. Our overall objective in this Review is to provide readers with a comprehensive overview of cyclotides that we hope will stimulate further work on this fascinating family of peptides.
Topics: Amino Acid Sequence; Animals; Cyclotides; Humans; Models, Molecular; Plant Proteins; Plants; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Tandem Mass Spectrometry
PubMed: 31829013
DOI: 10.1021/acs.chemrev.9b00402 -
Trends in Plant Science May 2018Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) fixes atmospheric CO into organic compounds and is composed of eight copies each of a large subunit (RbcL) and... (Review)
Review
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) fixes atmospheric CO into organic compounds and is composed of eight copies each of a large subunit (RbcL) and a small subunit (RbcS). Recent reports have revealed unusual RbcS, which are expressed in particular tissues and confer higher catalytic rate, lesser affinity for CO, and a more acidic profile of the activity versus pH. The resulting Rubisco was proposed to be adapted to a high CO environment and recycle CO generated by the metabolism. These RbcS belong to a cluster named T (for trichome), phylogenetically distant from cluster M, which gathers well-characterized RbcS expressed in mesophyll or bundle-sheath tissues. Cluster T is largely represented in different plant phyla, including pteridophytes and bryophytes, indicating an ancient origin.
Topics: Carbon Dioxide; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Models, Molecular; Phylogeny; Plant Proteins; Plants; Protein Conformation; Ribulose-Bisphosphate Carboxylase
PubMed: 29525130
DOI: 10.1016/j.tplants.2018.02.006