Temporins are a family of peptides isolated originally from the skin secretion of the European red frog, Rana temporaria . [1] Peptides belonging to the temporin family have been isolated also from closely related North American frogs, such as Rana sphenocephala. [2]
In 1996, the skin of the Rana temporaria was screened into a cDNA library, discovering three peptide precursors, known as Temporin B, Temporin G, and Temporin H. Once discovered, the three peptide, along with other temporins found in the sample, were separated from secretions of the frog's skin. Biological assays were performed, revealing that all temporins, in exception of temporin D and H, exhibited antibacterial activity. It was soon discovered that other species of frog also possess temporal, resulting in the discovery of more than 150 peptides from the temporin family. Some of the genera of frogs include the Amolops, Hylarana, Lithobathes, Odorrana, Pelophylax, Rana, and Hylarana. [3]
Temporins are a family of antimicrobial peptides (AMPs), which are highly targetable toward Gram-positive bacteria, allowing it to penetrate the cell wall and damage the inner membrane of the bacteria. These proteins are also capable of killing specific cancer cells when they are locally administered to a tumor, making it a good anticancer drug. [4]
The common frog or grass frog, also known as the European common frog, European common brown frog, European grass frog, European Holarctic true frog, European pond frog or European brown frog, is a semi-aquatic amphibian of the family Ranidae, found throughout much of Europe as far north as Scandinavia and as far east as the Urals, except for most of the Iberian Peninsula, southern Italy, and the southern Balkans. The farthest west it can be found is Ireland. It is also found in Asia, and eastward to Japan. The nominative, and most common, subspecies Rana temporaria temporaria is a largely terrestrial frog native to Europe. It is distributed throughout northern Europe and can be found in Ireland, the Isle of Lewis and as far east as Japan.
Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa. The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu opioid receptors. Dermorphin is about 30–40 times more potent than morphine, but theoretically may be less likely to produce drug tolerance and addiction due to its high potency. The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.
Defensins are small cysteine-rich cationic proteins across cellular life, including vertebrate and invertebrate animals, plants, and fungi. They are host defense peptides, with members displaying either direct antimicrobial activity, immune signaling activities, or both. They are variously active against bacteria, fungi and many enveloped and nonenveloped viruses. They are typically 18-45 amino acids in length, with three or four highly conserved disulphide bonds.
The European fire-bellied toad is a species of fire-bellied toad native to eastern parts of mainland Europe, where it can be found near waterbodies such as ponds and marshes. It is known for its red colored belly used to ward off predators, an example of aposematism, and its distinctive "whoop" call.
The foothill yellow-legged frog is a small-sized frog from the genus Rana in the family Ranidae. This species was historically found in the Coast Ranges from northern Oregon, through California, and into Baja California, Mexico as well as in the foothills of the Sierra Nevada and southern Cascade Range in California. The foothill yellow-legged frog is a Federal Species of Concern and California State Endangered. A federal rule to list four out of six extant distinct population segments (DPS) under the Endangered Species Act was proposed in December 2021.
Paneth cells are cells in the small intestine epithelium, alongside goblet cells, enterocytes, and enteroendocrine cells. Some can also be found in the cecum and appendix. They are located below the intestinal stem cells in the intestinal glands and the large eosinophilic refractile granules that occupy most of their cytoplasm.
Lithobates sphenocephalus or Rana sphenocephala, commonly known as the southern leopard frog, is a medium-sized anuran in the family Ranidae. The southern leopard frog is one of the 36 species currently or formerly classified in the Rana genus found in North America. It is native to eastern North America from Kansas to New York to Florida. It is also an introduced species in some areas. This species lives in cool, clear water in the north, whereas in the south it occurs in warmer turbid and murky waters of coastal and floodplain swamps, twilight zones of caves, and abandoned mines.
Indosylvirana aurantiaca, commonly known as the golden frog, is a species of frog endemic to the Western Ghats of India. The species is also known as the Trivandrum frog, the common wood frog, or the small wood frog.
Cathelicidin antimicrobial peptide (CAMP) is an antimicrobial peptide encoded in the human by the CAMP gene. The active form is LL-37. In humans, CAMP encodes the peptide precursor CAP-18, which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37.
Phyllomedusa trinitatis is a species of frog in the subfamily Phyllomedusinae. It is found in Venezuela and the island of Trinidad.
The Cascades frog is a species of frog in the family Ranidae found in the Pacific Northwest, mainly in the Cascade Range and Olympic Mountains.
Rana sauteri is a species of true frog endemic to Taiwan. It inhabits low-altitude hill forests and the associated streams. It is an endangered species threatened by habitat loss due to agriculture and infrastructure development. Common names recorded for Rana sauteri include Kanshirei Village frog, Taiwan groove-toed frog, Sauter's brown frog, and Taiwan pseudotorrent frog.
Hylarana latouchii, also known as Kuatun frog, La Touche's frog, or broad-folded frog, is a species of frog in the family Ranidae. It was formerly placed in genus Rana. The specific name honours the collector of the type series: "Hylarana" latouchii was described by George Albert Boulenger based on three specimens collected by Irish ornithologist John D. La Touche in Guadun village in Wuyishan, Fujian, China.
Pseudin is a peptide derived from Pseudis paradoxa. Pseudins have some antimicrobial function.
Polypeptide antibiotics are a chemically diverse class of anti-infective and antitumor antibiotics containing non-protein polypeptide chains. Examples of this class include actinomycin, bacitracin, colistin, and polymyxin B. Actinomycin-D has found use in cancer chemotherapy. Most other polypeptide antibiotics are too toxic for systemic administration, but can safely be administered topically to the skin as an antiseptic for shallow cuts and abrasions.
The magainins are a class of antimicrobial peptides found in the African clawed frog. The peptides are cationic, generally lack a stable conformation in water but form amphipathic α-helix in membranes; their mechanism against micro-organisms is unclear but they disrupt the cell membranes of a broad spectrum of bacteria, protozoa, and fungi.
Cecropins are antimicrobial peptides. They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.
The bombinin family of antimicrobial peptides includes the bombinin and maximin proteins from Bombina maxima. Two groups of antimicrobial peptides have been isolated from skin secretions of B. maxima. Peptides in the first group, named maximins 1, 2, 3, 4 and 5, are structurally related to bombinin-like peptides (BLPs). Unlike BLPs, sequence variations in maximins occurred all through the molecules. In addition to the potent antimicrobial activity, cytotoxicity against tumour cells and spermicidal action of maximins, maximin 3 possessed a significant anti-Simian-Human immunodeficiency virus (HIV) activity. Maximins 1 and 3 have been found to be toxic to mice. Peptides in the second group, termed maximins H1, H2, H3 and H4, are homologous with bombinin H peptides.
Esculentin-2CHa is an antimicrobial peptide located outside the epithelial cell's membrane of the skin of many species of amphibians, such as Rana chiricahuensis. This peptide has recently become more important due to its defense response function and its possible application in the treatment of various human pathologies, that range from type 2 diabetes to bacterial and fungi infections. Esculentin-2CHa is a peptide that belongs to the Esculentin-2 family, which is known for its broad-spectrum of antimicrobial activity and its low cytotoxicity to human erythrocytes. However, not much is known about its structures and their relation to the functions these peptides carry out.
Bacterial secretion systems are protein complexes present on the cell membranes of bacteria for secretion of substances. Specifically, they are the cellular devices used by pathogenic bacteria to secrete their virulence factors to invade the host cells. They can be classified into different types based on their specific structure, composition and activity. Generally, proteins can be secreted through two different processes. One process is a one-step mechanism in which proteins from the cytoplasm of bacteria are transported and delivered directly through the cell membrane into the host cell. Another involves a two-step activity in which the proteins are first transported out of the inner cell membrane, then deposited in the periplasm, and finally through the outer cell membrane into the host cell.