Drug – bio-affecting and body treating compositions – Preparations characterized by special physical form – Liposomes
Reexamination Certificate
2001-11-27
2004-09-14
Kishore, Gollamudi S. (Department: 1615)
Drug, bio-affecting and body treating compositions
Preparations characterized by special physical form
Liposomes
C424S278100, C424S581000, C514S841000, C514S842000
Reexamination Certificate
active
06790457
ABSTRACT:
FIELD OF THE INVENTION
The present invention relates to a vaccine composition for the immunocontraception of fish. The present invention also relates to a vaccine composition for the immunocontraception of birds.
BACKGROUND OF THE INVENTION
Among vertebrates, mating strategies involve behaviour, gamete structure and the specificity of recognition of sperm and egg. Mammalian oocytes are surrounded by an envelope called the zona pellucida that is composed of three glycoproteins in a ratio of 1:2:2 denoted by ZPA, ZPB, and ZPC (Harris, J. D., Hibler, D. W., Fontenot, G. K., Hsu, K. T., Yurewicz, E. C. and Sacco, A. G.(1994) “Cloning and characterization of zona pellucida genes and cDNA's from a variety of mammalian species: the ZPA, ZPB and ZPC gene families DNA sequence.” J. Sequencing and Mapping 4:361-393). The zona pellucida contains species-specific sperm receptors composed mainly of O-terminal oligosaccharides. Fish eggs have a teleost equivalent of mammalian zona pellucida wherein the carbohydrate moiety has some structural similarity to the carbohydrate moiety of mammalian zona pellucida (Taguchi, T., Seko, A., Kitajima, K., Muko, Y., Inoue, S., Knoo, K-H., Morris, H. R., Dell, A. and Inoue, Y.(1994) “Structural studies of a novel type of pentaantennary large glycan unit in the fertilization-associated carbohydrate-rich glycopeptide isolated from the fertilized eggs of Oryzias latipes.” J. Biol. Chem 269:8762-8771).
Mouse ZP2 (ZPA) contains a 241-amino acid domain at the C-terminus with 28% identity with a white flounder teleost egg protein (Lyons, C. E., Payette, K. L., Price, J. L. and Huang, R. C. C. (1993) “Expression and structural analysis of a teleost homolog of a mammalian zona pellucida gene.” J. Biol. Chem. 268:21351-21358). A 348-amino acid sequence of mouse ZP1 (ZPB) is 47% similar (32% identical) to that of mouse ZP2 (ZPA) suggesting that this protein domain has been duplicated in mammals (Epifano, O., Liang, L-F. and Dean, J. (1996) “Mouse ZP1 encodes a zona pellucida protein homologous to egg envelope proteins in mammals and fish.” J. Biol. Chem. 270: 27254-27258). A smaller region of this sequence (275 amino acids) is 52% similar (36% identical) with a white flounder egg envelope protein that contains 509 amino acids.
Immunization of grey seals with a single administration vaccine containing soluble zona pellucida antigens encapsulated in liposomes has been shown to reduce female fertility by at least 90% for up to at least six years (Brown, R. G., Kimmins, W. C., Mezei, M., Parsons, J. L., Pohajdak, B. and Bowen, W. D. (1996) “Birth control for grey seals.” Nature 379:30-31; Brown, R. G., Bowen, W. D., Eddington, J. D., Kimmins, W. C., Mezei, M., Parsons, J. L., and Pohajdak, B. (1997) “Evidence for a long-lasting single administration contraceptive vaccine in wild grey seals.” J. Reproduct. Immunol. 35:43-51; and U.S. Pat. No. 5,736,141). The same vaccine prevented pregnancy in four rabbits (proven breeders) following 8 matings (unpublished observations).
An example of the use of liposome encapsulation of denatured recombinantly produced protein to raise antibodies against a native protein was shown with Neisseria meningitidis outer membrane protein P1. (Muttilainen, S., Idanpaan-Heikkila, I., Wahlstrom, E., Nurminen, M., Makela, P. H. and Sarvas, M. (1995) “The
Neisseria meningitidis
outer membrane protein P1 produced in
Bacillus subtilis
and reconstituted into phospholipid vesicles elicits antibodies to native P1 epitopes.” Microb. Pathog. 18:423-436).
Specificity of recognition of sperm and egg is essential in any species. However, the mechanism of fertilization varies widely, both physiologically and biochemically, between species. Fertilization in fish differs from that in mammals in that most teleostean fish spermatozoa lack an acrosomal structure. Penetration by a spermatozoon of the fish egg envelope occurs via a discrete micropyle with closure of the micropyle after penetration of the first spermatozoon.
Sperm-egg interaction in birds is significantly different from that in mammals and different again from fish. In birds, sperm-egg recognition is initiated by the binding of spermatozoa to the inner perivitelline layer (IPVL), a proteinaceous structure surrounding the avian ovum (Bakst, M. R. and Howarth, B. (1977) “Hydrolysis of hens perivitelline layer by cock sperm in vitro.” Biol. Reproduct. 17:370-379). There is no block to polyspermy in avian species but a further proteinaceous layer, the outer perivitelline layer (OPVL), is laid down about 15 minutes after the IPVL in chickens and appears to prevent further penetration of sperm. Therefore, if spermatozoa can be prevented from entering the avian egg between the laying down of the IPVL and OPVL, by antibodies directed against the IPVL, then immunocontraception would be realized.
There is some similarity between reproduction in mammals and fish but also many differences. Unlike the C-terminus, the N-terminus domain of white flounder egg protein is quite dissimilar to mouse ZP2 (ZPA) and a transmembrane domain characteristic of all mammalian zona pellucida proteins is not present in teleost egg protein indicating the divergence of these species 650 million years ago (Epifano, O., Liang, L-F. and Dean, J. (1996) “Mouse ZP1 encodes a zona pellucida protein homologous to egg envelope proteins in mammals and fish.” J. Biol. Chem. 270: 27254-27258).
The carbohydrate moiety of teleost egg glycoproteins is also dissimilar, for example, rainbow trout egg envelope glycoprotein has a unique N-linked glycan containing KDN (2-keto-3-deoxy-D-glycero-D-qalacto-nononic acid) in the second layer of the vitelline envelope (Tezuka, T., Taguchi, T., Kanamori, A., Muto, Y., Kitajima, K., Inoue, Y. and Inoue, S. (1994) “Identification and structural determination of the KDN-containing N-linked glycan chains consisting of bi- and triantennary complex-type units of KDN-glycoprotein previously isolated from rainbow trout vitelline envelopes.” Biochem. 33:6495-6502). This KDN-glycoprotein is exposed to the outer surface around the micropyle through which sperm enter the egg at fertilization. Most fish sperm lack an acrosome and penetrate the fish egg envelope via a discrete micropyle. The micropyle forms a guidance system in teleost fertilization that enhances sperm penetration (Amanze, D. and Iyengar, A. (1990) “The micropyle: a sperm guidance system in teleost fertilization.” Development 109:495-500). A chemical attractant may also emanate from the micropyle to enhance the chance of fertilization.
In spite of the significant structural differences between fish egg envelope protein and mammalian zona pellucida, fish egg envelope proteins have been designated the teleost homolog of zona pellucida (TH-ZP for convenience of reference). In fish, TH-ZP3 is made in the liver and transported via the blood to the ovary, while TH-ZP2 is made in the ovary (Hamazaki, T. S., Nagahama, Y. and Yamagami, K. (1989) “A glycoprotein from liver constitutes the inner layer of the egg envelope (zona pellucida interna) of the fish,
Oryzias latipes
.” Dev.Biol.133:101-110; Murata, K., Sasaki, T., Yasumasu, S., Iuchi, I., Enami, J., Yasumasu, I. and Yamagami, K. (1995) “Cloning of cDNAs for the precursor protein of a low-molecular weight subunit of the inner layer of the egg envelope (chorion) of the fish
Oryzias latipes
.”; Chang, Y. S., Wang, S. C., Tsao, C. C. and Huang, F. L. (1996) “Molecular cloning, structural analysis and expression of carp ZP3 gene.” Mol. Reprod. Dev. 44:295-304; Murata, K., Sugiyama, H., Yasumasu, S., Iuchi, I., Yasumasu, I. and Yamagami, K. (1997) “Cloning of cDNA and estrogen-induced hepatic gene expression for chorigenin H, a precursor protein of the fish egg envelope (chorion).” Proc.Natl.Acad.Sci. USA 94:2050-2055; Chang, Y. S., Hsu, C. C., Wang, S. C., Tsao, C. C. and Huang, F. L. (1997) “Molecular cloning, structural analysis and expression of carp ZP2 gene.” Mol. Reprod. Dev. 46:258-67).
It is undesirable that transgenic fish escape from fish farms and mate with fish in the wild. This problem w
Brown Robert
Horrocks Janet
McLaren Leslie
Pohajdak Bill
Dalhousie University
Kishore Gollamudi S.
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