Flesh fly

Yoder J. A., Denlinger D. L., Dennis M. W. and Kolattukudy P. E. (1992) Enhancement of diapausing flesh fly puparia with additional hydrocarbons and evidence for alkane biosynthesis by a decarbonylation mechanism. Insect Biochem. Molec. Biol. 22, 237-243. 

The g-D-Glucopyranose Site. Since methyl o-D-glucopyranoside was the most stimulatory glucose derivative tested, the presence of an a-D-glucopyranose receptor site was suggested. This type of site has been postulated in the blowfly and flesh fly (24,31). 

The arrival of blowflies, and subsequently their larvae, is followed quickly by the arrival of the flesh flies (Diptera Sarcophagidae), other carrion flies (Diptera Muscidae), and predaceous beetle species such as rove beetles (Coleoptera Staphylinidae), carrion beetles (Silphidae), clown beetles (Histeridae), skin beetles (Dermestidae), and checkered beetles (Cleridae). A variety of other fly families may be found in association with the body, and hide beetles (Trogidae) and larvae of some of the aforementioned beetle groups may feed on carrion itself, often on remains of hair, skin, and clothing in late decomposition (Smith 1986). 

The most important effect of burial on decomposition is the increase in time required for biomass reduction, relative to exposed carrion (Smith 1986). Smith (1986) suggested that blowflies, which are responsible for the majority of biomass reduction on carrion, are excluded from the corpse at a depth of just 2.5 cm. However, Simpson and Strongman (2002) reported the occurrence of the blowfly Cynomyopsis cadaverina on carrion buried at a depth of 30 cm. Rodriguez and Bass (1985) also observed Sarcophagidae (flesh fly) and blowfly larvae on burials at a depth of 1 ft, as did VanLaerhoven and Anderson (1999). In the latter study, adult flies were observed attempting to... 

Calliphoridae (blowflies) and Sarcophagidae (flesh flies) associated with 130- to 160-year-old burials (Gilbert and Bass 1967). The presence of pupae in the burial environments seasonally dated the burials from late March to mid October based on the arrival and disappearance of these flies in South Dakota. Although the approximate dates of the burials were previously known, the entomological evidence was able to further confirm the dates by determining the season of burial. 

Early studies in a termite (Chu and Blomquist, 1980a), a cockroach (Major and Blomquist, 1978) and the housefly (Tillman-Wall et al., 1992) showed that tritium-labeled fatty acids were converted in vivo to hydrocarbons one carbon shorter. The mechanism of how this occurs has been controversial. Kolattukudy and co-workers have proposed a mechanism in which a fatty acyl-CoA is reduced to the aldehyde and, in the absence of cofactors, is decarbonylated to the hydrocarbon one carbon shorter and carbon monoxide. This has been demonstrated in plants, algae, vertebrates (Bognar et al, 1984 Cheesbrough and Kolattukudy, 1984, 1988 Dennis and Kolattukudy, 1991) and the flesh fly Sarcophaga crassipalpis (Yoder et al., 1992). 

Arnold, M.T. and Regnier, F.E. (1975). Stimulation of hydrocarbon biosynthesis by ecdysterone in the flesh fly Sarcophaga bullata. J. Insect Physiol., 21,1581-1586. 

K. H. Clifford, Stereochemistry of the hydrolysis of trehalose by the enzyme trehalase prepared from the flesh fly sarcophaga barbata, Eur. J. Biochem., 106 (1980) 337-340. 

Figure 9.7 Microsomal aldrin epoxidase activity in developmental stages of the flesh fly. (From Terriere, L.C. and Yu, S.J., Pestic. Biochcm. Physiol., 6, 223,1976. With permission.)...

Table 9.8 Microsomal metabolism of JH analogs in flesh flies...

Nevertheless, the authors observed that several molecular masses between 3-5 kDa were detected exclusively in the fat body tissue collected from bacteria-challenged larvae of this flesh-fly while others were only present in control flies [55]. Such approach evidenced the sensitivity and potency of MALDI-MS to perform peptide mass fingerprints directly on tissues or organs. Analyzing complex biological samples by MALDI-MS without any pretreatment of the sample e.g. solid-phase extraction, LC) has thus become a reality. 

Some of the ABs may have structural homology to antibacterial proteins isolated from the flesh fly (20,21) since an oligonucleotide probe that can encode a portion of the sarcotoxin protein recognizes an immune-specific RNA in Drosophila fat body cells, the cellular origin of Drosophila s ABs (unpubl.). The induction mechanism must work relatively rapidly since we found immune-specific RNA in fat body cells within 6 hours after inoculation. Because of its homology to sarcotoxin, we assume that the immune-specific transcript detected by the oligonucleotide probe encodes an antibacterial protein. 

Cecropins. Cecropins (169) were isolated from the larval hemolymph of the giant silkworm moth, Hyalophora cecropia, on the basis of their antibacterial activity subsequent to bacterial injection. Cecropins are also produced by Drosophila (170) and the larva of the tobacco homworm, Manduca sexta (110). Similar compounds called sarcotoxins (171) are produced by the flesh fly, Sarcophaga. Cecropins (169) are specific for prokaryotic cell lysis in contrast to melittin, which lyses eukaryotic cell membranes as well. Cecropins are characterized structurally by a concentration of basic... 

Upon infection, insects can produce a wide range of antimicrobial peptides, which are synthe zed in the fax. body and/or haemocytes and secreted into the haemolymi. Such peptides include ceert ins (33), and defensin-like peptides such as sapecin and phormicin (34,35). Cecropins are highly amphipathic peptides containing 31-39 residues that form voltage-dependent channels in lipid membranes (36). They were initially isolated from the silk moth Hyolop/tora cecropia (37) and have subsequently been isolated from the flesh fly (sarcoroxin 1) and Drosophila (38,39). Cecropins are distinct from other insect cationic peptides in that they contain no cysteine residues and fail to lyse eukaryotic cells (33),... 

Insect defensins 3 disulfides 2 strands 1 a-helix Dragonfiy, blowfly, flesh fly Hiocmicin, sapecin, safcotoxin, royalisin... 

Sapaecin, an insect defensin isolated from the flesh fly Sacrophaga peregrma, consists of 40 amino acids including the conserved six cysteine residues (46) and is most active against Gram-positive bacteria (35). 

Other properties may exist for cationic peptides within the host. For example, sapaecin, the insect defensin, has been found to stimulate cell proliferation of Sorcophoga embryo cells. This perhaps indicates a dual role of antimicrobial agent and developmen-tal hormone for this peptide in the flesh fly (83). Indeed, Magainin Pharmaceuticals, Inc.. Plymouth Meeting, PA has claimed to have available cationic peptides that promote reepithelialiration of damaged corneas. 

Kuzuhara T, Nakajima Y. Matsuyama K, Natori S, Determination of the disulphide array in sapecin, an antibacterial peptide of Sarcopfinga peregTina (flesh fly). J Biochem 1990 107 514-518. 

Komano H, Homma K, Natori S. Invc vement of sapecin in embryonic ceil proliferation of Sarcopfwge peregnna (flesh fly). FEDS Lett 1991 289 167-170. 

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