Immunolocalization of the Oostatic and Prothoracicostatic Peptide, Neb-TMOF, in Adults of the Fleshfly,Neobellieria bullata

Bylemans, D.; Verhaert, Peter; Janssen, Ine; Broeck, Jozef Vanden; Borovsky, Dov; McDonough, Michael A.; Loof, Arnold De

doi:10.1006/gcen.1996.0122

Cited by 16 publications

(12 citation statements)

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“…Neb-TMOF is produced by vitellogenic follicles but, in this case, the oocyte rather than the cells of the follicular epithelium is the major source of the peptide (Bylemans et al, 1996). The effects of Neb-TMOF include inhibition of trypsin biosynthesis in the gut and concomitant lowering of yolk protein concentration in the hemolymph (Bylemans et al, 1994).…”

Section: Aedes Aegypti and Anautogenous Fliesmentioning

confidence: 99%

Vitellogenesis and Post-Vitellogenic Maturation of the Insect Ovarian Follicle

Swevers

2005

Comprehensive Molecular Insect Science

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Section: Aedes Aegypti and Anautogenous Fliesmentioning

confidence: 99%

Vitellogenesis and Post-Vitellogenic Maturation of the Insect Ovarian Follicle

Swevers

2005

Comprehensive Molecular Insect Science

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“…Cytoimmunochemical studies indicate that the site of synthesis of TMOF in the mosquito and the flesh fly is the follicular epithelium of the ovary. TMOF was not initially detected in the mosquito brain, indicating that the hormone is not a neuropeptide (Borovsky et al, 1994b;Bylemans et al, 1996). Recent studies of Aea-TMOF, however, have identified an immunoreactive material (IR) in all the ganglia of the central nervous system in larvae as well as in male and female A. aegypti adults.…”

Section: Synthesis and Secretion Of Tmofmentioning

confidence: 99%

Trypsin-modulating oostatic factor: a potential new larvicide for mosquito control

Borovsky

2003

Journal of Experimental Biology

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Trypsin-modulating oostatic factor (TMOF), a mosquito decapeptide, terminates trypsin biosynthesis in the mosquito gut. The hormone is secreted from the ovary, starting 18·h after the blood meal, circulates in the hemolymph, binds to a gut receptor and stops trypsin biosynthesis by exerting a translational control on trypsin mRNA. Because of the unique primary amino acid sequence of the hormone (YDPAPPPPPP) and its stable three-dimensional conformation, TMOF is not degraded by gut proteolytic enzymes and can traverse the gut epithelial cells into the hemolymph of adults and larvae. Using this unique property, hormone fed to different species of mosquito larvae stops food digestion and causes larval mortality. To determine the shortest amino acid sequence that can bind to the gut receptor and still cause high larval mortality, 25 analogues of TMOF were synthesized and tested. The tetrapeptide (YDPA) was as effective as the decapeptide, indicating that the binding to the gut receptor is at the N-terminus of the molecule. Cloning and expressing the hormone on the coat protein of tobacco mosaic virus (TMV) in Chlorella sp. and Saccharomyces cerevisiae cells and feeding the recombinant cells to mosquito larvae caused larval mortality. These results indicate that TMOF can be used as a new biorational insecticide against mosquito larvae.

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“…The synthesis reached a maximum at 33 h, and rapidly declined thereafter to a minimum at 48 h. The peak of TMOF synthesis coincides with a rapid decline in trypsin biosynthesis (30). Cytoimmunochemical studies indicate that the site of synthesis of TMOF in the mosquito and the fleshfly is the follicular epithelium of the ovary (30,31). Recently we have shown by cytoimmunochemical studies that TMOF-like peptide is found in the brain and neuroendocrine organs of adults and larvae Ae.…”

Section: Tmofmentioning

confidence: 99%

Biosynthesis and Control of Mosquito Gut Proteases

Borovsky

2003

IUBMB Life

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SummaryEarlier investigations of the proteases that digest the blood meal in mosquitoes identified the midgut epithelial cells as the source of the main blood digesting protease, trypsin. Surgical manipulations and cytoimmunochemical studies indicated that trypsin in the mosquito is not stored in the epithelial cells as an inactive enzyme, but is synthesized, activated and released into the gut lumen after the blood meal. Using molecular biology techniques the major trypsin genes have been sequenced and some information on the transcription factors that regulate the induction of the genes have been reported. Although all the hormone(s) and the factors that are responsible for the induction of trypsin biosynthesis are not known, the termination of trypsin biosynthesis is controlled by a decapeptide hormone; trypsin modulating oostatic factor (TMOF) that is secreted by the mosquito ovary. Genetic engineering and expression of TMOF in bacteria, yeast and algae is emerging as a potential future larval control of mosquitoes in the field. IUBMB Life, 55: 435-441, 2003

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Immunolocalization of the Oostatic and Prothoracicostatic Peptide, Neb-TMOF, in Adults of the Fleshfly,Neobellieria bullata

Cited by 16 publications

References 0 publications

Vitellogenesis and Post-Vitellogenic Maturation of the Insect Ovarian Follicle

Vitellogenesis and Post-Vitellogenic Maturation of the Insect Ovarian Follicle

Trypsin-modulating oostatic factor: a potential new larvicide for mosquito control

Biosynthesis and Control of Mosquito Gut Proteases

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