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Drosophila melanogaster is a species of fly in the family Drosophilidae. The species is often referred to as the fruit fly or lesser fruit fly, however its common name is more accurately the vinegar fly. Starting with Charles W. Woodworth's proposal of the use of this species as a model organism, D. melanogaster continues to be widely used for biological research in genetics, physiology, microbial pathogenesis, and life history evolution. As of 2017, five Nobel Prizes have been awarded to drosophilists for their work using the animal.
Ceratitis capitata, commonly known as the Mediterranean fruit fly or medfly is a yellow and brown fly native to sub-Saharan Africa. C. capitata has no near relatives in the Western Hemisphere and is considered to be one of the most destructive fruit pests in the world. There have been occasional medfly infestations in the states of California, Florida, and Texas requiring extensive eradication efforts to prevent the fly from establishing itself in the US.
Leucyl/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human placental leucine aminopeptidase (PLAP), oxytocinase, and vasopressinase, is an enzyme of the aminopeptidase group that in humans is encoded by the LNPEP gene.
Dermcidin is a protein with 110 amino acids that in humans is encoded by the DCD gene. The full-length protein produces derived peptides as proteolysis-inducing factor (PIF) and other anti-microbial peptides, secreted by human eccrine sweat glands onto the skin as a part of the innate host defense of the immune system. PIF is involved in muscular proteolysis.
CD59 glycoprotein, also known as MAC-inhibitory protein (MAC-IP), membrane inhibitor of reactive lysis (MIRL), or protectin, is a protein that in humans is encoded by the CD59 gene. It is an LU domain and belongs to the LY6/uPAR/alpha-neurotoxin protein family.
Calcitonin receptor-like (CALCRL), also known as the calcitonin receptor-like receptor (CRLR), is a human protein; it is a receptor for calcitonin gene-related peptide.
Semenogelin-1 is a protein that in humans is encoded by the SEMG1 gene. The protein encoded by this gene is the predominant protein in semen. The encoded secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes this protein into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to move more freely. Two transcript variants encoding different isoforms have been found for this gene.
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CAMP responsive element binding protein-like 1, also known as CREBL1, is a protein which in humans is encoded by the CREBL1 gene.
Sarcophaga is a genus of true flies and the type genus of the flesh-fly family (Sarcophagidae). The members of this cosmopolitan genus are frequently known as common flesh flies.
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.
Sarcophaga pernix, also known as the red-tailed flesh fly, is a fly in the Sarcophagidae family. This fly often breeds in carrion and feces, making it a possible vector for disease. The larvae of this species can cause myiasis, as well as accidental myiasis. It is potentially useful in forensic entomology.
Kunitz domains are the active domains of proteins that inhibit the function of protein degrading enzymes or, more specifically, domains of Kunitz-type are protease inhibitors. They are relatively small with a length of about 50 to 60 amino acids and a molecular weight of 6 kDa. Examples of Kunitz-type protease inhibitors are aprotinin, Alzheimer's amyloid precursor protein (APP), and tissue factor pathway inhibitor (TFPI). Kunitz STI protease inhibitor, the trypsin inhibitor initially studied by Moses Kunitz, was extracted from soybeans.
In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes which are part of primary metabolism, such as sterols and carotene and also part of the secondary metabolism. This entry will focus on the N terminal domain of the TPS protein.
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Sarcophaga peregrina is a species of flesh fly belonging to the family Sarcophagidae. They easily breed, multiply and spread in human habitation, from garbage, faeces and livestock manures. In many regions, they are health concerns as they are active vectors of infectious diseases such as myiasis in humans. Due to their close contact with human activities, they are considered as forensically important insects. They can be used for molecular analysis of the time of postmortem intervals. They are also occasionally parasitic in other invertebrates. They produce a group of antibacterial peptide called sarcotoxins. The first of such protein, sarcotoxin 1A, was determined in 1983 by Masayuki Okada and Shunji Natori at the University of Tokyo, Japan.
Ribosomally synthesized and post-translationally modified peptides (RiPPs), also known as ribosomal natural products, are a diverse class of natural products of ribosomal origin. Consisting of more than 20 sub-classes, RiPPs are produced by a variety of organisms, including prokaryotes, eukaryotes, and archaea, and they possess a wide range of biological functions.
Pacifastin is a family of serine proteinase inhibitors found in arthropods. Pacifastin inhibits the serine peptidases trypsin and chymotrypsin.
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.
Sarcophaga barbata is a species from the genus Sarcophaga and the family of flesh fly, Sarcophagidae. It is most closely related to S. plinthopyga, S. securifera, and S. bullata of the same genus. The species was first discovered by Eugene Thomson in 1868. S. barbata has also been found in the Middle East near carcasses, where the larvae can thrive. S. barbata is also a prominent organism in scientific research and has been used to study L-3-glycerophosphate Oxidation and location within the mitochondria.
References
- ↑ Iwai, H.; Nakajima, Y.; Natori, S.; Arata, Y.; Shimada, I. (Oct 1993). "Solution conformation of an antibacterial peptide, sarcotoxin IA, as determined by 1H-NMR". Eur J Biochem. 217 (2): 639–44. doi: 10.1111/j.1432-1033.1993.tb18287.x . PMID 8223606.
- ↑ Okada M, Natori S (1984). "Mode of action of a bactericidal protein induced in the haemolymph of Sarcophaga peregrina (flesh-fly) larvae". Biochem J. 222 (1): 119–124. doi:10.1042/bj2220119. PMC 1144151 . PMID 6383355.
- ↑ "Sarcotoxin II-3 precursor - Sarcophaga peregrina (Flesh fly)". www.uniprot.org. Retrieved 2021-02-02.
- ↑ "Sarcotoxin-1A precursor - Sarcophaga peregrina (Flesh fly)". www.uniprot.org. Retrieved 2021-02-02.