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Imd Pathway
The Imd pathway is a broadly-conserved NF-κB immune signalling pathway of insects and some arthropods that regulates a potent antibacterial defence response. The pathway is named after the discovery of a mutation causing severe immune deficiency (the gene was named ''"Imd"'' for "immune deficiency"). The Imd pathway was first discovered in 1995 using ''Drosophila'' fruit flies by Bruno Lemaitre and colleagues, who also later discovered that the ''Drosophila'' Toll gene regulated defence against Gram-positive bacteria and fungi. Together the Toll and Imd pathways have formed a paradigm of insect immune signalling; as of September 2, 2019, these two landmark discovery papers have been cited collectively over 5000 times since publication on Google Scholar. The Imd pathway responds to signals produced by Gram-negative bacteria. Peptidoglycan recognition proteins (PGRPs) sense DAP-type peptidoglycan, which activates the Imd signalling cascade. This culminates in the translocation of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Drosocin
Drosocin is a 19-residue long antimicrobial peptide (AMP) of flies first isolated in the fruit fly ''Drosophila melanogaster'', and later shown to be conserved throughout the genus ''Drosophila''. Drosocin is regulated by the NF-κB Imd signalling pathway in the fly. The ''Drosocin'' gene encodes two peptides: its namesake Drosocin peptide and a second peptide called Buletin. Structure and function Drosocin is primarily active against Gram-negative bacteria. The peptide is proline-rich with proline-arginine repeats, as well a critical threonine residue. This threonine is ''O''-glycosylated, which is required for antimicrobial activity. This ''O''-glycosylation can be performed either by mono- or disaccharides, which have different activity spectra. Like the antimicrobial peptides pyrrhocoricin and abaecin, drosocin binds to bacterial DnaK, inhibiting cell machinery and replication. The action of these drosocin-like peptides is potentiated by the presence of pore-forming pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AMP Ecc15-19-02-2019
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Acyrthosiphon Pisum
''Acyrthosiphon pisum'', commonly known as the pea aphid (and colloquially known as the green dolphin, pea louse, and clover louse), is a sap-sucking insect in the family Aphididae. It feeds on several species of legumes (plant family Fabaceae) worldwide, including forage crops, such as pea, clover, alfalfa, and broad bean, and ranks among the aphid species of major agronomical importance. The pea aphid is a model organism for biological study whose genome has been sequenced and annotated. Generalities and life cycle In the autumn, female pea aphids lay fertilized eggs overwinter that hatch the following spring. The nymphs that hatch from these eggs are all females, which undergo four moults before reaching sexual maturity. They will then begin to reproduce by viviparous parthenogenesis, like most aphids. Each adult female gives birth to four to 12 female nymphs per day, around a hundred in her lifetime. These develop into mature females in about seven to ten days. The life span ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acyrthosiphon Pisum (pea Aphid)-PLoS
''Acyrthosiphon pisum'', commonly known as the pea aphid (and colloquially known as the green dolphin, pea louse, and clover louse), is a sap-sucking insect in the family Aphididae. It feeds on several species of legumes (plant family Fabaceae) worldwide, including forage crops, such as pea, clover, alfalfa, and broad bean, and ranks among the aphid species of major agronomical importance. The pea aphid is a model organism for biological study whose genome has been sequenced and annotated. Generalities and life cycle In the autumn, female pea aphids lay fertilized eggs overwinter that hatch the following spring. The nymphs that hatch from these eggs are all females, which undergo four moults before reaching sexual maturity. They will then begin to reproduce by viviparous parthenogenesis, like most aphids. Each adult female gives birth to four to 12 female nymphs per day, around a hundred in her lifetime. These develop into mature females in about seven to ten days. The life span ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Providencia Burhodogranariea
Providencia may refer to: * Providencia, Chile, a commune in the Santiago Province * Providencia District in Amazonas, Peru * Providencia Island, part of the San Andrés y Providencia Department district of Colombia in the Caribbean sea * Providencia, Nariño Providencia () is a town and municipality in the Nariño Department, Colombia. References Municipalities of Nariño Department {{Nariño-geo-stub ... a town in municipality in southern Colombia * ''Providencia'' (bacterium) a Gram-negative bacterial genus {{Disambig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enterobacter Cloacae
''Enterobacter cloacae'' is a clinically significant Gram-negative, facultatively-anaerobic, rod-shaped bacterium. Microbiology In microbiology labs, ''E. cloacae'' is frequently grown at 30 °C on nutrient agar or at 35 °C in tryptic soy broth. It is a rod-shaped, Gram-negative bacterium, is facultatively anaerobic, and bears peritrichous flagella. It is oxidase-negative and catalase-positive. Industrial use ''Enterobacter cloacae'' has been used in a bioreactor-based method for the biodegradation of explosives and in the biological control of plant diseases. ''Enterobacter cloacae'' strain MBB8 isolated from the Gulf of Mannar, India was reported to degrade poly vinyl alcohol (PVA). This was the first report of a PVA degrader from the Enterobacter genus. ''E. cloacae'' was also reported to produce exopolysaccharide (EPS) as high as 18.3g/L. GC-MS analysis of ''E. cloacae'' EPS showed the presence of glucose and mannose in the molar ratio of 1: 1.5e−2. Safe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Providencia Rettgeri
''Providencia rettgeri'' (commonly ''P. rettgeri''), is a Gram negative bacterium that is commonly found in both water and land environments. ''P. rettgeri'' is in the genus Providencia, along with '' Providencia stuartii'', '' Providencia alcalifaciens'', and '' Providencia rustigianii''. ''P. rettgeri'' can be incubated at 37 °C in nutrient agar or nutrient broth. It was first discovered in 1904 after a waterfowl epidemic. Strains of the species have also been isolated from nematodes of the genus ''Heterorhabditis''. ''Providencia rettgeri'' also found in marine environment. Biochemical characteristics of ''Providencia rettgeri'' S.I. Paul et al. (2021) isolated, characterized and identified salt tolerant ''Providencia rettgeri'' from marine sponge (''Niphates erecta'') of the Saint Martin's Island Area of the Bay of Bengal, Bangladesh. Colony, morphological, physiological, and biochemical characteristics of ''Providencia rettgeri'' are shown in the Table below. N ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arthropod Defensin
Arthropod defensins are a family defensin proteins found in mollusks, insects, and arachnids. These cysteine-rich antibacterial peptides are primarily active against Gram-positive bacteria and fungi in vitro. However ''Drosophila'' fruit flies mutant for the fly defensin were more susceptible to infection by the Gram-negative bacteria '' Providencia burhodogranariea'', and resisted infection against Gram-positive bacteria like wild-type flies. It remains to be seen how in vitro activity relates to in vivo function. Mutants for the defensin-like antimicrobial peptide Drosomycin were more susceptible to fungi, validating a role for defensin-like peptides in anti-fungal defence. Structure Arthropod defensin peptides range in length from 38 to 51 amino acids. There are six conserved cysteines all involved in intrachain disulfide bonds. Studies have shown that the cysteine-bridge disulfide bonds are not required for antimicrobial activity, similar to findings in mammalian defensins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cecropin
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. Cecropins constitute a main part of the innate immune system of insects. Cecropins are small proteins anywhere from 31 - 37 amino acids long and are active against both gram-positive and gram-negative bacteria. Cecropins isolated from insects other than ''Hyalophora cecropia'' (Cecropia moth) have been given various names, such as bactericidin, lepidopterin, and sarcotoxin. All of these peptides are structurally related. Members Members include: ;Cecropin A: Peptide Sequence (KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK). Secondary structure includes two α helices. At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed. ;Cecropin B: Peptide Sequence (KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL). Sec ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Attacin
Attacin is a glycine-rich protein of about 20 kDa belonging to the group of antimicrobial peptides (AMP). It is active against Gram-negative bacteria. Attacin was first discovered in ''Hyalophora cecropia'', but is widely conserved in different insects from butterflies to fruit flies. See also *Diptericin Diptericin is a 9 kDa antimicrobial peptide (AMP) of flies first isolated from the blowfly '' Phormia terranova''. It is primarily active against Gram-negative bacteria, disrupting bacterial membrane integrity. The structure of this protein incl ..., a structurally related antimicrobial peptide References {{Reflist Insect immunity Antimicrobial peptides ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diptericin
Diptericin is a 9 kDa antimicrobial peptide (AMP) of flies first isolated from the blowfly ''Phormia terranova''. It is primarily active against Gram-negative bacteria, disrupting bacterial membrane integrity. The structure of this protein includes a proline-rich domain with similarities to the AMPs drosocin, pyrrhocoricin, and abaecin, and a glycine-rich domain with similarity to attacin. Diptericin is an iconic readout of immune system activity in flies, used ubiquitously in studies of ''Drosophila'' immunity. Diptericin is named after the insect order Diptera. Structure and function Diptericins are found throughout Diptera, but are most extensively characterized in ''Drosophila'' fruit flies. The mature structures of diptericins are unknown, though previous efforts to synthesize Diptericin have suggested Diptericin in ''Protophormia terraenovae'' is one linear peptide. Yet ''Drosophila melanogaster's'' Diptericin B peptide is likely cleaved into two separate peptides. Synt ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
