Synthetic mammalian sulphamidase and genetic sequences...

Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Bacteria or actinomycetales; media therefor

Reexamination Certificate

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C435S255100, C435S195000, C536S023200

Reexamination Certificate

active

06458579

ABSTRACT:

FIELD OF INVENTION
The present invention relates generally to mammalian sulphamidase and to genetic sequences encoding same and to the use of these in the investigation, diagnosis and treatment of subjects suspected of or suffering from sulphamidase deficiency.
Bibliographic details of the publications referred to by author in this specification are collected at the end of the description. Sequence Identity Numbers (SEQ ID NOs.) for the nucleotide and amino acid sequences referred to in the specification are defined following the bibliography.
Throughout this specification, unless the context requires otherwise, the word “comprise”, or variations such as “comprises” or “comprising”, will be understood to imply the inclusion of a stated element or Beer or group of elements or integers but not the exclusion of any other element or integer or group of elements or integers.
BACKGROUND TO THE INVENTION
The increasing sophistication of recombinant DNA technology is greatly facilitating the efficacy of many commercially important industries including areas of medical and pharmaceutical research and development The ability to purify native proteins and subsequently clone genetic sequences encoding these proteins is an important first step in the development of a range of therapeutic and diagnostic procedures. However, practitioners have faced many difficulties in purifying target molecules to an extent sufficient to determine amino acid sequences to permit the development of oligonucleotide probes to assist in the cloning of genetic sequences encoding the target molecules.
Such difficulties have been particularly faced in the research and development of lysosomal enzymes. An important lysosomal enzyme Is sulphamidase (sulphamate sulphohydrolase EC 3.10.11). This enzyme acts as a exosulphatase in lysosomes to hydrolyse the sulphate ester bond in 2-sulphaminoglucosamine residues present in heparan sulphate and heparin (Hopwood, 1989). A deficiency in this lysosomal hydrolase is responsible for the pathogenesis of Sanfilippo A Mucopolysaccharidosis type IIIA [MPS-IIIA3]) syndrome (Kresse, 1973; Matalon and Dorfman, 1974). This is an autosomal recessive disorder of glycosaminoglycan catabolism leading to storage and excretion of excessive amounts of heparan sulphate and a variety of clinical phenotypes, but classically presenting with progressive mental retardation in conjunction with skeletal deformities (McKusick and Neufeld, 1983).
There is a need, therefore, to purify sulphamidase and to clone genetic sequences encoding same to permit development of a range of therapeutic and diagnostic procedures to assist in the diagnosis and treatment of disease conditions arising from sulphamidase deficiency.
SUMMARY OF THE INVENTION
One act of the invention provides an isolated nucleic acid molecule comprising a sequence of nucleotides which encodes or is complementary to a sequence which encodes a mammalian sulphamidase or fragment or derivative thereof.
Another aspect of the invention is directed to an isolated nucleic acid molecule having a nucleotide sequence substantially as set forth in SEQ ID NO:1 or having at least 40% similarity to all or part thereof.
Yet another aspect of the present invention contemplates a recombinant mammalian sulphamidase or fragment or derivative thereof.
Still yet another aspect of the present invention provides a nucleic acid molecule comprising a sequence of nucleotides encoding or complementary to a sequence encoding a polypeptide capable of hydrolysing the sulphate ester bond in 2-sulphaminoglucosamine residues and wherein said nucleotide sequence is capable of hybridising under low stringency conditions to the nucleotide sequence set forth in
FIG. 2
(SEQ ID NO:1).
Still another aspect of the present invention is directed to a polypeptide comprising a sequence of amino acids corresponding to the amino sequence set forth in
FIG. 2
(SEQ ID NO:2) or having at least 40% similarity thereto, more preferably at least 60% similarity thereto and still more preferably at least 80% or 85-90% similarity thereto or encoded by the nucleotide sequence set forth in
FIG. 2
(SEQ ID NO:1) or a nucleotide sequence capable of hybridising to SEQ ID NO:1 under low, preferably under medium and more preferably under high stringent conditions.
In still yet another aspect of the present invention there is contemplated a method for treating a patient suffering from sulphamidase deficiency said method comprising administering to said patient an effective amount of recombinant mammalian sulphamidase or an active fragment or derivative thereof.
Another aspect of the present invention is directed to a pharmaceutical composition comprising a recombinant mammalian sulphamidase or an active fragment or derivative thereof and one or more pharmaceutically acceptable carriers and/or diluents.


REFERENCES:
patent: 5298395 (1994-03-01), Park
Alberts, et al. (1989) “DNA Cloning and Genetic Engineering”,The Molecular Biology of The Cell, Second Edition, Chapter 5, Garland Publishing, Inc., New York, pp. 258-266.
Bielicki, J., et al. (1998) “Recombinant huan sulphamidase: expression, amplification, purification and characterization”,Biochem. J. 329:145-150.
Coulter II, et al. (1993) “Identification of Cortexin: A Novel, Neuron-Specific, 82-Residue Membrane Protein Enriched in Rodent Cerebral Cortex”,Journal of Neurochemistry 62(2): 756-759.
Dean, et al. (1973) “Mobilization of glycosaminoglycans by plasma infusion in mucopolysaccharidosis type III-two types of response”,Nature New Biology 243:143-146.
Ford, et al. (1991) “Fusion Tails for the recovery and purification of recombinant proteins”,Protein Expression and Purification 2(2/3):95-107.
Freeman, et al. (1986) “Human Liver Sulphamate Sulphohydrolase”,Biochem. J. 234:83-92.
Mahuran, et al. (1983) “A Rapid Four Column Purification of 2-Deoxy-D-Glucoside-2-Sulphamate Sulphohydrolase from Human Liver”,Biochimica et Biophysica Acta 757:359-365.
O'Brien, et al. (1973) “Sanfilippo disease type B: enzyme replacement and metabolic correction in cultured fibroblasts”,Science 181(101): 753-755.

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