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Antimicrobial peptides from animals, plants and fungi organised by their secondary structure content. Circle size indicates overall molecular weight of each peptide. Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. [3]
Other invertebrates known to produce defensins from this protein superfamily include molluscs, annelids and cnidaria. [24] Plant defensins were discovered in 1990 and have subsequently been found in most plant tissues with antimicrobial activities, with both antifungal and antibacterial examples. [25]
Plant defensins (formerly gamma-thionins) are a family of primitive, highly stable, cysteine-rich defensins found in plants that function to defend them against pathogens and parasites. [1] Defensins are integral components of the innate immune system and belong to the ancient superfamily of antimicrobial peptides (AMPs).
In addition, some of the products of the coagulation system are directly antimicrobial. For example, beta-lysine, a protein produced by platelets during coagulation, can cause lysis of many Gram-positive bacteria by acting as a cationic detergent. [3] Many acute-phase proteins of inflammation are involved in the coagulation system.
Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. [1] While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.
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Pathogenesis-related (PR) proteins are proteins produced in plants in the event of a pathogen attack. [1] 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.
The most recently proposed subclass is the Class IIe, which encompasses those bacteriocins composed of three or four non-pediocin like peptides. The best example is aureocin A70, a four-peptide bacteriocin, highly active against Listeria monocytogenes, with potential biotechnological applications. [16]