- Email: [email protected]
Cholera vaccine containing stable nontoxigenic Vibrio cholerae mutant; recombinant vaccine strain improvement
13, No. 16, p. 1626, 1995 Copyright 0 1995 Elsevier Science Ltd Printed in Great Britain. All rights reserved 0264-410X/95-$10.00+0.00
Vaccme, Vol.
Patent Report This section provides information on worldwide patents relevant to vaccine design and production. The Patent Report gives the following information: title of patent, patentee, patent number, publication date and summary of the patent. A number of patents in this report are reproduced from ‘Derwent Biotechnology Abstracts’ with permission of Derwent Information Ltd, Derwent House, 14 Great Queen Street, London WC2B SDF. New enzymatic RNA molecules; ribozyme specific for hepatitis C virus, for use in intracellular immunization, therapy or defective virus particle attenuated recombinant vaccine production Ribogene-Pharm. World 95 19 429; 20 July 1995 A new ribozyme specifically cleaves RNA of hepatitis C virus (HCV). The following are also new: a mammal cell containing the ribozyme; an expression vector containing DNA encoding the ribozyme, for expression in a mammal cell; a method for providing defective virus particles (DVPs) by contacting a cell infected with HCV with the ribozyme, which cleaves a gene required for virus replication; DVPs produced by contacting an HCV-infected cell with the ribozyme; and a method for inducing an immune response or production of anti-HCV lg in a human, by administering the DVP. The ribozyme is specific for the 5’-untranslated region of HCV genomic RNA, or the C-protein or NS3 open reading frame. The ribozyme may be produced by transcription or oligonucleotide synthesis. The ribozyme may be used in intracellular immunization and therapy of human and non-human HCV infections, and on other pestivirus and flavivirus groups. It may also be used for producing defective genomes in recombinant vaccine production, or as a diagnostic agent. The ribozyme is highly specific for viral RNA of HCV-infected cells. 068-95 Human parvovirus gene coding for a polypeptide; VP-l and VP-Z and nonstructural protein expression in e.g. Escherichia coli for use in disease diagnosis or recombinant vaccine construction De&i Chem; Denka-Seiken Jpn 07147 986; 13 June 1995 A human parvovirus gene (I) encoding a protein (II) is claimed. The gene comprises 4680 bases. Also claimed are human parvovirus structural proteins VP-l and VP-2 of 781 and 554 amino acids, respectively, and a nonstructural protein of 660 amino acids. The recombinant antigens are useful for diagnosis and development of a recombinant vaccine for parvovirus diseases. e.g. erythroblastemia, abortion, universal fetal hydrops, liver disease, hemorrhagic fever, arthritis, and rheumatism. The parvovirus antigens can be prepared in high yield. The structural and nonstructural genes of human parvovirus are isolated and used for the production of a vector for expression in host cells of (II). In an example, VP-l and VP-2 mixed antigen was expressed in Escherichin co/i and was used to detect parvovirus IgG antibodies. 069-95 Cholera vaccine containing stable nontoxigenic Vibvio cholevae mutant; recombinant vaccine strain improvement Univ. Harvard: Krus Res. Inst. Cambridge World 9518 633; 13 July 1995 A new vaccine comprising a nontoxinogenic genetically stable mutant strain (MS) of I’ibrio cholerae. where the MS lacks DNA encoding a functional CtxA subunit and has a soft agar penetration-defective phenotype (SAPDP). The MS also lacks any attRS1 sequences and is derived from a parental strain of the El Tor biotype, lnaba or Ogawa serotype and of the
1626
Vaccine 1995 Volume 13, Number 16
Bengal-2, Bengal-3, Peru-‘, Peru-3, Peru-15. Bah-2, Bah-3, Bah-15, Bang-2, Bang-3, Bang-15 serogroup. but not of the non-01 serogroup. The MS lacks CTX core sequences and a recA gene, but encodes a B subunit of cholera toxin (CTB). Also new are: a vaccine containing at least two strains of V. cholevae (Peru-3+Bengal-3, Peru-14+Bengal-15 or Peru1S+Bengal-15); a li cholerae strain where at least 25% of the cells are capable of forming filaments of at least 15 nM under stationary phase growth; a vaccine MS with the motility and flagellar genes inactivated; a method for vaccinating against cholera; a method for making a killed ‘v cholerne vaccine from a SAPDP MS and CTRB; a method for forming a genetically stable MS by inserting a plasmid; Y cholerue motB and fliC 070-95 DNA; a cell containing the DNA; and MS VRl-16. New nucleic acid encoding highly cross-reactive allergen: grass, birch, ragweed or Puvietaviu sp. pollen allergen gene cloning and expression using a plasmid pNH1 vector, for use as an antiallergic recombinant vaccine Univ. Manitoba World 9519 437; 30 July 1995 A new DNA fragment encodes an allergen present in pollens from both monocotyledonous and dicotyledonous plants, e.g. Graminae (bermudagrass (C~rzodonduct~lon), Kentucky bluegrass (Poa pratensis), red top grass, reed canarygrass (Phaluris arwdinncea), ryegrass (Lo/&m sp.), timothygrass. bromegrass (Bromus sp.), orchardgrass (Dactylis glomeram) or maize (Zeu tq.xf, birch (Bet&u sp.), short ragweed (Ambrosia sp.) or Parierariu sp.). The DNA may be inserted into a vector, e.g. plasmid pNH1 (ATCC 75634) with control sequences and expressed as a fusion protein with glutathione-transferase (EC 2.5.1.18). p-galactosidase (EC 32.123) or protein-A. The recombinant protein may be used as an antiallergic recombinant vaccine, with a Snlmonelln sp., M}‘cobncterium bovis BCG, adenovirus. poxvirus. vaccinia virus or poliovirus vector, or as a diagnostic agent. The allergen is highly crossreactive with IgE antibodies induced by many different pollens, and may thus be used where purified allergens or peptide fragments are not available. 071-95 Antiallergic vaccine containing polypeptide fragment of IgE heavy chain; recombinant vaccine production IgE Fc-epsilon monomer fragment expression in Eschevichiu cofi using vector plasmid pE2-4 Pasteur-Merieux vflccines France 2715 304; 28 July 1995 An antiallergic vaccine is composed of a polypeptide (I) at least part of the protein sequence of which is derived from the Fc-epsilon monomer fragment of primate (especially human) 1gE. Compared to natural IgE of human or primates, (I) has one or more neoantigenic sites or epitopes. A clone containing the complete epsilon chain sequence is isolated from a human myeloma cDNA library by screening with a DNA probe corresponding to the N-terminus of IgE. The fragment encoding the 218-547 amino acid region is isolated and cloned into plasmid pWT211, under control of the tryptophan promoter-operator. The resulting plasmid expresses a protein containing some non-Fe amino acid, to avoid this, an NcoI site is engineered into pWT211 at the ATG codon, forming plasmid pWT211NcoI. A 42 bp synthetic linker is introduced at the NcoI site to form the bicistronic vector plasmid pWT311 NcoIBos. DNA sequences encoding fragments of the Fc epsilon chain are inserted into the BamHI and NcoI sites to produce plasmid pE2-4(7) which when expressed in Escherichia coli, produces non-glycosylated Fc epsilon fragment as 072-95 inclusion bodies.
Vaccme, Vol.
Patent Report This section provides information on worldwide patents relevant to vaccine design and production. The Patent Report gives the following information: title of patent, patentee, patent number, publication date and summary of the patent. A number of patents in this report are reproduced from ‘Derwent Biotechnology Abstracts’ with permission of Derwent Information Ltd, Derwent House, 14 Great Queen Street, London WC2B SDF. New enzymatic RNA molecules; ribozyme specific for hepatitis C virus, for use in intracellular immunization, therapy or defective virus particle attenuated recombinant vaccine production Ribogene-Pharm. World 95 19 429; 20 July 1995 A new ribozyme specifically cleaves RNA of hepatitis C virus (HCV). The following are also new: a mammal cell containing the ribozyme; an expression vector containing DNA encoding the ribozyme, for expression in a mammal cell; a method for providing defective virus particles (DVPs) by contacting a cell infected with HCV with the ribozyme, which cleaves a gene required for virus replication; DVPs produced by contacting an HCV-infected cell with the ribozyme; and a method for inducing an immune response or production of anti-HCV lg in a human, by administering the DVP. The ribozyme is specific for the 5’-untranslated region of HCV genomic RNA, or the C-protein or NS3 open reading frame. The ribozyme may be produced by transcription or oligonucleotide synthesis. The ribozyme may be used in intracellular immunization and therapy of human and non-human HCV infections, and on other pestivirus and flavivirus groups. It may also be used for producing defective genomes in recombinant vaccine production, or as a diagnostic agent. The ribozyme is highly specific for viral RNA of HCV-infected cells. 068-95 Human parvovirus gene coding for a polypeptide; VP-l and VP-Z and nonstructural protein expression in e.g. Escherichia coli for use in disease diagnosis or recombinant vaccine construction De&i Chem; Denka-Seiken Jpn 07147 986; 13 June 1995 A human parvovirus gene (I) encoding a protein (II) is claimed. The gene comprises 4680 bases. Also claimed are human parvovirus structural proteins VP-l and VP-2 of 781 and 554 amino acids, respectively, and a nonstructural protein of 660 amino acids. The recombinant antigens are useful for diagnosis and development of a recombinant vaccine for parvovirus diseases. e.g. erythroblastemia, abortion, universal fetal hydrops, liver disease, hemorrhagic fever, arthritis, and rheumatism. The parvovirus antigens can be prepared in high yield. The structural and nonstructural genes of human parvovirus are isolated and used for the production of a vector for expression in host cells of (II). In an example, VP-l and VP-2 mixed antigen was expressed in Escherichin co/i and was used to detect parvovirus IgG antibodies. 069-95 Cholera vaccine containing stable nontoxigenic Vibvio cholevae mutant; recombinant vaccine strain improvement Univ. Harvard: Krus Res. Inst. Cambridge World 9518 633; 13 July 1995 A new vaccine comprising a nontoxinogenic genetically stable mutant strain (MS) of I’ibrio cholerae. where the MS lacks DNA encoding a functional CtxA subunit and has a soft agar penetration-defective phenotype (SAPDP). The MS also lacks any attRS1 sequences and is derived from a parental strain of the El Tor biotype, lnaba or Ogawa serotype and of the
1626
Vaccine 1995 Volume 13, Number 16
Bengal-2, Bengal-3, Peru-‘, Peru-3, Peru-15. Bah-2, Bah-3, Bah-15, Bang-2, Bang-3, Bang-15 serogroup. but not of the non-01 serogroup. The MS lacks CTX core sequences and a recA gene, but encodes a B subunit of cholera toxin (CTB). Also new are: a vaccine containing at least two strains of V. cholevae (Peru-3+Bengal-3, Peru-14+Bengal-15 or Peru1S+Bengal-15); a li cholerae strain where at least 25% of the cells are capable of forming filaments of at least 15 nM under stationary phase growth; a vaccine MS with the motility and flagellar genes inactivated; a method for vaccinating against cholera; a method for making a killed ‘v cholerne vaccine from a SAPDP MS and CTRB; a method for forming a genetically stable MS by inserting a plasmid; Y cholerue motB and fliC 070-95 DNA; a cell containing the DNA; and MS VRl-16. New nucleic acid encoding highly cross-reactive allergen: grass, birch, ragweed or Puvietaviu sp. pollen allergen gene cloning and expression using a plasmid pNH1 vector, for use as an antiallergic recombinant vaccine Univ. Manitoba World 9519 437; 30 July 1995 A new DNA fragment encodes an allergen present in pollens from both monocotyledonous and dicotyledonous plants, e.g. Graminae (bermudagrass (C~rzodonduct~lon), Kentucky bluegrass (Poa pratensis), red top grass, reed canarygrass (Phaluris arwdinncea), ryegrass (Lo/&m sp.), timothygrass. bromegrass (Bromus sp.), orchardgrass (Dactylis glomeram) or maize (Zeu tq.xf, birch (Bet&u sp.), short ragweed (Ambrosia sp.) or Parierariu sp.). The DNA may be inserted into a vector, e.g. plasmid pNH1 (ATCC 75634) with control sequences and expressed as a fusion protein with glutathione-transferase (EC 2.5.1.18). p-galactosidase (EC 32.123) or protein-A. The recombinant protein may be used as an antiallergic recombinant vaccine, with a Snlmonelln sp., M}‘cobncterium bovis BCG, adenovirus. poxvirus. vaccinia virus or poliovirus vector, or as a diagnostic agent. The allergen is highly crossreactive with IgE antibodies induced by many different pollens, and may thus be used where purified allergens or peptide fragments are not available. 071-95 Antiallergic vaccine containing polypeptide fragment of IgE heavy chain; recombinant vaccine production IgE Fc-epsilon monomer fragment expression in Eschevichiu cofi using vector plasmid pE2-4 Pasteur-Merieux vflccines France 2715 304; 28 July 1995 An antiallergic vaccine is composed of a polypeptide (I) at least part of the protein sequence of which is derived from the Fc-epsilon monomer fragment of primate (especially human) 1gE. Compared to natural IgE of human or primates, (I) has one or more neoantigenic sites or epitopes. A clone containing the complete epsilon chain sequence is isolated from a human myeloma cDNA library by screening with a DNA probe corresponding to the N-terminus of IgE. The fragment encoding the 218-547 amino acid region is isolated and cloned into plasmid pWT211, under control of the tryptophan promoter-operator. The resulting plasmid expresses a protein containing some non-Fe amino acid, to avoid this, an NcoI site is engineered into pWT211 at the ATG codon, forming plasmid pWT211NcoI. A 42 bp synthetic linker is introduced at the NcoI site to form the bicistronic vector plasmid pWT311 NcoIBos. DNA sequences encoding fragments of the Fc epsilon chain are inserted into the BamHI and NcoI sites to produce plasmid pE2-4(7) which when expressed in Escherichia coli, produces non-glycosylated Fc epsilon fragment as 072-95 inclusion bodies.