Patent Report cattle papilloma virus-2, especially amino acids 90-467, or is a cattle papilloma virus-4 protein or fragment. The L2 protein or fragment is preferably produced by recombinant DNA techniques, and may be in the form of a fusion protein with e.g. fl galactosidase (EC 3.2.t.23) or glutathione-transferase (GT, EC 2.5.1.18). The formulation is suitable for therapy and regression of benign or malignant laryngeal tumours, skin cancer tumours and genital lesions, and for prophylactic vaccination. In an example, the cattle papilloma virus-4 L2 open reading frame was cloned in Escherichia coli, using plasmid pGEX as vector, resulting in production of an L2 fusion protein with GT. The fusion protein was purified and the active component was used for vaccination of young cattle, 061-93
Envelope region nucleic acid fragment of type-C hepatitis virus and its detection; diagnosis using hepatitis C virus D N A probe or RNA probe; D N A sequence; potential recombinant vaccine preparation Teijin Jpn 4349 885; 4 December 1992 A DNA fragment (DNA sequence disclosed) of at least eight bases encoding envelope region nucleic acid fragment of type C hepatitis virus (HCV) is new. A complementary sequence or a complementary RNA sequence is also new. The DNA or RNA fragments may be labelled and used as DNA probes and RNA probes, respectively, for detection of HCV. A kit for detection of HCV containing the DNA or RNA probe, and a peptide encoded by the new DNA are also new. The peptide fragment may be used for preparing a vaccine for protection against HCV. In an example, cDNA is prepared from RNA isolated from the serum of non-A and non-B hepatitis patients by reverse-transcriptase (EC 2.7.7.49) in the presence of a random primer. The envelope region nucleic acid of HCV is amplified against the cDNA solution. Complete doublestranded DNA is prepared by using Escherichia eoli DNA-polymerase (EC 2.7.7.7), and the ends are treated to make them smooth. The DNA is introduced into E. coli JM 101, and single-stranded DNA is prepared, and sequenced. 062-93
Borrelia burgdorferi gene encoding conserved 79 kDa antigen: D N A probe or D N A primer and polymerase chain reaction for Lyme disease diagnosis and recombinant vaccine; monoclonal antibody production Univ. Calif. World 9300 448; 7 January 1993 A new assay for detecting the presence of Borrelia burgdorferi in a sample comprises: (1) detecting the presence of a
chromosomal gene of B. burgdorferi encoding a conserved antigen of 79kDa (79A) using a labelled DNA probe, specific for 79A, and detecting hybridization; (2) using a new DNA primer specific for 79A and performing the polymerase chain reaction; (3) using a monoclonal antibody specific for 79A and detecting binding; or (4) contacting the sample with a whole or partial 79A recombinant protein and detecting binding of this protein with antibodies present in the sample. The following are also claimed: (a) a 79A recombinant protein or a fragment of at least six amino acids; (b) chromosomal DNA from B. burgdorferi encoding 79A; (c) 9A DNA in a self-replicating DNA construct (vector); (d) a DNA probe of at least ten nucleotides of the 79A gene; (e) complementary sequences to (d); (f) a pair of DNA primers of 10-50 nucleotides the same or complementary to a pair of contiguous sequences in the 79A gene; (g) a diagnostic kit; and (h) a recombinant vaccine containing (a); and (i) polyclonal and monoclonal antibodies specific for 79A. 063-93
Peptide blocking the binding of P. aeruginosa to buccal epithelial cells; Pseudomonas aeruginosa recombinant epitope peptide production for use as recombinant vaccine and as adjuvant in lung cancer therapy Synth. Peptide World 9300 358; 7 January 1993 A peptide containing an epitope formed by the sequence, CATTATGPNGSC, is claimed. The peptide exhibits immunospecific binding to monoclonal antibody PK99H or MCA1, comprises less than 20 amino acids, and blocks Pseudomonas aeruoinosa binding to buccal epithelial cells (BECs). The two Cys residues are linked covalently. The peptide contains a sequence which is partly homologous to P. aeruoinosa pilin peptide amino acids 131-43. The epitope was isolated by studying inhibition of binding of P. aeruginosa to BECs. The peptide is obtained by solid-phase synthesis or by recombinant DNA techniques. The peptide is able to bind to a receptor site on human BECs and this binding is effective to inhibit P. aeruginosa binding to these cells. The peptide can be used to produce vaccines inducing immunity against P. aeruginosa infection. The peptide can also be used as a target molecule for drug delivery to pulmonary epithelial cells e.g. in lung cancer therapy. Antibodies immunoreactive with the peptides are useful for producing passive immunity to pathogens which have adhesin molecules characterized by the epitope formed by this peptide. 064-93
Vaccine, Vol. 11, Issue 8, 1993 879