Pathogenesis-related
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Pathogenesis-related
Pathogenesis-related (PR) proteins are proteins produced in plants in the event of a pathogen attack. They are induced as part of systemic acquired resistance. Infections activate genes that produce PR proteins. Some of these proteins are antimicrobial, attacking molecules in the cell wall of a bacterium or fungus. Others may function as signals that spread “news” of the infection to nearby cells. Infections also stimulate the cross-linking of molecules in the cell wall and the deposition of lignin, responses that set up a local barricade that slows spread of the pathogen to other parts of the plant. Salicylic acid plays a role in the resistance to pathogens by inducing the production of pathogenesis-related proteins. Many proteins found in wine are grape pathogen-related proteins. Those include thaumatin-like proteins and chitinases. Many pathogenesis-related protein families also coincide with groups of human allergens, even though the allergy may have nothing to do with ...
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Barwin Domain
In molecular biology, the barwin domain is a protein domain found in barwin ("barley wound-induced"), a basic protein isolated from aqueous extracts of barley seeds. Barwin is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges. In the pathogenesis-related protein nomenclature, it is PR-4. This domain is found in a 122 amino acid stretch in the C-terminal of the products of two wound-induced genes (win1 and win2; , ) from potato, the product of the Pro-hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco (, ). The high levels of similarity among these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plant Plants are predominantly photosynthetic eukaryotes of the kingdom Plantae. Historically, the plant kingdom encompassed all living things that were not animals, and included algae and fungi; however, all current de ...
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Glossary Of Phytopathology
This is a glossary of some of the terms used in phytopathology. Phytopathology is the study of plant diseases. It is a multi-disciplinary science since prerequisites for disease development are the presence of a susceptible host species, a pathogen and the appropriate environmental conditions. This is known as the disease triangle. Because of this interaction, the terminology used in phytopathology often comes from other disciplines including those dealing with the host species ( botany / plant science, plant physiology), the pathogen (bacteriology, mycology, nematology, virology), the environment and disease management practices (agronomy, soil science, meteorology, environmental science, ecology, plant breeding, pesticides, entomology), and areas of study that apply to both the host and pathogen (molecular biology, genetics, molecular genetics). The result is that most phytopathological glossary include terms from these other disciplines in addition to terms (disease incide ...
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Cysteine-rich Secretory Protein Superfamily
The CAP superfamily (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP)) is a large superfamily of secreted proteins that are produced by a wide range of organisms, including prokaryotes and non-vertebrate eukaryotes. The nine subfamilies of the mammalian CAP superfamily include: the human glioma pathogenesis-related 1 ( GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour sup ...
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Proteins In Wine
Proteins are present in wine. The most common proteins include thaumatin-like proteins and chitinases and have a role in the formation of turbidity (haze) especially visible in white wine. The quantity of haze forming is dependent on the quantity of phenolics in the wine. Some of those proteins are considered nuisance. Some of them are grape pathogenesis-related proteins. Those proteins have been identified by mass spectrometry and originate from grape, yeast, bacteria and fungi. These proteins are unstable when submitted to heat, and can be removed by treatment using bentonite, a process that contributes to the clarification and stabilization of wine. Proteins residues from proteinaceous fining agents such as gelatin or egg white can possibly be found in wine. Wheat gluten has also been tested, but there are health issues regarding its use because of gluten intolerance in some people. See also * Wine chemistry * Protein adsorption in the food industry Protein adsorption refe ...
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Systemic Acquired Resistance
Systemic acquired resistance (SAR) is a "whole-plant" resistance response that occurs following an earlier localized exposure to a pathogen. SAR is analogous to the innate immune system found in animals, and although there are many shared aspects between the two systems, it is thought to be a result of convergent evolution. The systemic acquired resistance response is dependent on the plant hormone, salicylic acid. Discovery While, it has been recognized since at least the 1930s that plants have some kind of induced immunity to pathogens, the modern study of systemic acquired resistance began in the 1980s when the invention of new tools allowed scientists to probe the molecular mechanisms of SAR.Ryals, J., U. Neuenschwander, M. Willits, A. Molina, H. Steiner, and M. Hunt. 1996. Systemic Acquired Resistance. Plant Cell 8:1809–1819. A number of 'marker genes' were characterized in the 80s and 90s which are strongly induced as part of the SAR response. These pathogenesis-related ...
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Salicylic Acid
Salicylic acid is an organic compound with the formula HOC6H4CO2H. A colorless, bitter-tasting solid, it is a precursor to and a metabolite of aspirin (acetylsalicylic acid). It is a plant hormone, and has been listed by the EPA Toxic Substances Control Act (TSCA) Chemical Substance Inventory as an experimental teratogen. The name is from Latin ''salix'' for willow tree. It is an ingredient in some anti-acne products. Salts and esters of salicylic acid are known as salicylates. Uses Medicine Salicylic acid as a medication is commonly used to remove the outer layer of the skin. As such, it is used to treat warts, psoriasis, acne vulgaris, ringworm, dandruff, and ichthyosis. Similar to other hydroxy acids, salicylic acid is an ingredient in many skincare products for the treatment of seborrhoeic dermatitis, acne, psoriasis, calluses, corns, keratosis pilaris, acanthosis nigricans, ichthyosis, and warts. Uses in manufacturing Salicylic acid is used as a food preservative ...
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Acibenzolar-S-methyl
Acibenzolar-''S''-methyl is the ISO common name for an organic compound that is used as a fungicide. Unusually, it is not directly toxic to fungi but works by inducing systemic acquired resistance, the natural defence system of plants. History In the 1980s, researchers at Ciba-Geigy in Switzerland were seeking novel fungicides. They discovered that the methyl ester of 1,2,3-benzothiadiazole-7-carboxylic acid, and many other derivatives, had useful activity on fungal diseases, for example ''Pyricularia oryzae'' on rice. In subsequent studies it was shown that the compound responsible for the biological activity was the carboxylic acid itself but that for optimum activity when used commercially it was important to choose a derivative which met requirements of product safety, ease of application and appropriate physical properties for translocation in the crop. After many derivatives of the acid had been tested, the ''S''-methyl thioester was chosen for development under the code na ...
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Thaumatin
Thaumatin (also known as talin) is a low-calorie sweetener and flavor modifier. The protein is often used primarily for its flavor-modifying properties and not exclusively as a sweetener. The thaumatins were first found as a mixture of proteins isolated from the katemfe fruit (''Thaumatococcus daniellii'') (Marantaceae) of West Africa. Although very sweet, thaumatin's taste is markedly different from sugar's. The sweetness of thaumatin builds very slowly. Perception lasts a long time, leaving a liquorice-like aftertaste at high concentrations. Thaumatin is highly water soluble, stable to heating, and stable under acidic conditions. Biological role Thaumatin production is induced in katemfe in response to an attack upon the plant by viroid pathogens. Several members of the thaumatin protein family display significant ''in vitro'' inhibition of hyphal growth and sporulation by various fungi. The thaumatin protein is considered a prototype for a pathogen-response protein do ...
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Thaumatin
Thaumatin (also known as talin) is a low-calorie sweetener and flavor modifier. The protein is often used primarily for its flavor-modifying properties and not exclusively as a sweetener. The thaumatins were first found as a mixture of proteins isolated from the katemfe fruit (''Thaumatococcus daniellii'') (Marantaceae) of West Africa. Although very sweet, thaumatin's taste is markedly different from sugar's. The sweetness of thaumatin builds very slowly. Perception lasts a long time, leaving a liquorice-like aftertaste at high concentrations. Thaumatin is highly water soluble, stable to heating, and stable under acidic conditions. Biological role Thaumatin production is induced in katemfe in response to an attack upon the plant by viroid pathogens. Several members of the thaumatin protein family display significant ''in vitro'' inhibition of hyphal growth and sporulation by various fungi. The thaumatin protein is considered a prototype for a pathogen-response protein do ...
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Cupin Superfamily
The cupin superfamily is a diverse superfamily of proteins named after its conserved barrel domain (''cupa'' being the Latin term for a small barrel). The superfamily includes a wide variety of enzymes as well as non-enzymatic seed storage proteins. Members of the superfamily play a role in allergy, especially seed storage proteins like 7S and 11S globulins, also known as vicilins and legumins, respectively. These proteins can be found at high concentrations in seeds of both mono- and dicotyledonous plants and are an important component of the normal human diet. History Thomas Burr Osborne at the end of the 19th century was the first person to systematically study seed storage proteins by their solubility characteristics. He established 4 classes of proteins: water-soluble albumins; salt soluble globulins: vicilin—typically having sedimentation coefficients, S values (a measure of the protein mass determined by sedimentation equilibrium ultracentrifugation) of about 7 S ...
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Haem Peroxidase
Heme, or haem (pronounced / hi:m/ ), is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver. In biochemical terms, heme is a coordination complex "consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands." The definition is loose, and many depictions omit the axial ligands. Among the metalloporphyrins deployed by metalloproteins as prosthetic groups, heme is one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word ''haem'' is derived from Greek ''haima'' meaning "blood". Function Hemoproteins have diverse biological functions i ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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