Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1996-09-11
1999-01-26
Hutzell, Paula K.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
530328, 530329, 530333, 514 15, 514 16, C12D 2106, A61K 3804, A61K 3800, C07K 500
Patent
active
058637630
DESCRIPTION:
BRIEF SUMMARY
FIELD OF THE INVENTION
The present invention relates to novel neuropeptides isolated and purified from the blowfly Calliphora vomitoria, which have been designated callatostatins. This new class of neuropeptides may be related to the allatostatin class of neuropeptides isolated from other unrelated insect species.
BACKGROUND OF THE INVENTION
The first group of callatostatins to be isolated from Calliphora vomitoria, callatostatins 1 to 5, were shown to have some sequence homology to cockroach allatostatins (Duve et al in Proc. Nat'l. Acad, Sci. USA 90:2456-2460). The neuropeptides have the following sequences (SEQ ID NO:4) NO:5)
Callatostatins 1 to 4 (SEQ ID NOS:4-7) are know as Leu-callatostatins and callatostatin 5 (SEQ ID NO:8) is known as Met-callatostatin or Met-cast.
The allatostatin class of insect neuropeptides in cockroaches have been shown capable of inhibiting the production of juvenile hormone (JH) by the corpus allatum. The corpus allatum (CA) is a classical endocrine gland of insects situated in close proximity to the brain with which it has nervous connection. To date, members of the allatostatin class of neuropeptides have been isolated and identified in only four species, from three different orders of insects. In the cockroach, Diploptera punctata (Order: Blattodea) five allatostatins ranging in size from 8 to 18 amino acids have been characterized (Pratt et al in Proc. Nat'l. Acad. Sci USA 88, 2412-2416 (1991) and Woodhead et al in Proc. Nat'l. Acad. Sci. USA 86, 5997-6001 (1989)). Two other allatostatins have also been identified in the cockroach Periplaneta americana (Order: Blattodea) (Weaver et al in C Comp. Pharmacol. Toxicol. 107 119-127 (1994)) and in the tobacco hornworm moth. Manduca sexta (Order: Lepidoptera) a further allatostatin has been identified (Kramer et al in Proc. Nat'l. Acad. Sci. USA 88, 9458-9462 (1991)).
The significance of the allatostatins--(and callatostatins) lies in the fact that "in vitro" they have been shown, with the exception of the allatostatin from the tobacco hornworm moth, to inhibit the production of juvenile hormone (JH) by the corpus allatum in cockroaches. The allatostatin molecule isolated from the tobacco hornworm moth inhibits JH production in the species in which it is found i.e. Mandus sexta but not in cockroaches. Callatostatins 1 to 5 (SEQ ID NOS:4-8) are of interest because they are potent inhibitors of JH synthesis and release in cockroaches, but not in the blowfly, the species from which they originate.
Juvenile hormone plays a crucial role in insect development by controlling metamorphosis, adult sexual maturity and reproduction. Interference with juvenile hormone biosynthesis and release through exploitation of the allatostatins and callatostatins may lead to insect control strategies that do not damage the environment.
SUMMARY OF THE INVENTION
The present invention is based on the discovery and potential practical commercial application of one or more of three neuropeptides identified in the blowfly Calliphora vomitoria. The three peptides are all related to callatostatin 5 (SEQ ID NO:8) and might even be derived from the same prohormone by post-translation modification.
DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS
The amino acid sequences of the neuropeptides according to this invention are as follows: Met-callatostatin 3-8 or des-Gly-Pro-Met-callatostatin).
The invention embraces neuropeptides 1-3 defined above when isolated and/or when substantially purified and essentially free of other peptide material.
The presence of the hydroxyproline residues (Hyp) has been confirmed by amino acid analysis and confirmation that the final methionyl residue of peptide No. 1 (SEQ ID NO:1) above is carboxyamidated was obtained by means of standard methylation procedures and comparisons of the masses of methylated and non-methylated peptides. The carboxyamidation of peptides 2 (SEQ ID NO:2) and 3 (SEQ ID NO:3) above is shown by the fact that they are both immunoreactive in the met-callatostatin radioimmunoassay. This recognizes onl
REFERENCES:
Belles, X., et al., "In Vivo and in Vitro Effects of Compactin in Liposome Carriers on Juvenile Hormone Biosynthesis in Adult Females of Blattella germanica," Pesticide Biochem. Physiol. 32:1-10 (1988).
Duve, H., et al., "Callatostatins: Neuropeptides from the blowfly Calliphora vomitoria with sequence homology to cockroach allatostatins," Proc. Natl. Acad. Sci. USA 90(6):2456-2460 (Mar. 15, 1993).
Duve, H., and Thorpe, A., "Distribution and funtional significance of Leu-callatostatins in the blowfly Calliphora vomitoria" Cell Tissue Res. 276(2):367-379 (May 1994). 269(33):21059-21066 (Aug. 19, 1994).
Kramer, S.J., et al., "Identification of an allatostatin from the tobacco hornworm Manduca sexta," Proc. Natl. Acad. Sci. USA 88:9458-9462 (1991).
Piulachs, M.D., et al., "Juvenile Hormone Production and Accessory Reproductive Gland Development During Sexual Maturation of Male Blattella germanica (L.) (Dictyoptera, Blattellidae)," Comp. Biochem. Physiol. 102A(3):477-480 (1992).
Pratt, G.E., et al., "Identity of a second type of allatostatin from cockroach brains: An octadecapeptide amide with a tyrosine-rich address sequence," Proc. Natl. Acad. Sci. USA 88:2412-2416 (1991).
Vuori, K., et al., "Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system," Proc. Natl. Acad. Sci. USA 89:7467-7470 (1992).
Vuori, K., et al., "Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity, and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells," EMBO J. 11:4213-4217 (1992).
Weaver, R.J., "Profile of the Responsiveness of Corpora Allata from Virgin Female Periplaneta americana to an Allatostatin from Diploptera punctata," J. Insect Physiol. 37:111-118 (1991).
Woodhead, A.P., et al., "Primary structure of four allatostatins: Neuropeptide inhibitors of juvenile hormone synthesis," Proc. Natl. Acad. Sci. USA 86:5997-6001 (1989).
Duve Hanne
Johnsen Anders Holten
Thorpe Alan
British Technology Group Ltd.
Hutzell Paula K.
Navarro Mark
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