Federal Tech Transfer Opportunities

During the past two weeks, the following agencies have listed inventions available for licensing.


Government-Owned Inventions, Available for Licensing

SUMMARY: The inventions listed below is assigned to the National Aeronautics and Space Administration, has been in the United States Patent and Trademark Office, and is available for licensing.

  1. NASA Case Code No. ARC 14366_1: Masked Proportional Routing.
  2. NASA Case No. MSC 22724_2/3/4/5: Endothelium Preserving Microwave Treatment for Atherosclerosis;
  3. NASA Case No. MSC 22743_2/3: Moving Object Control System;
  4. NASA Case No. MSC 22931_1: Androgynous, Reconfigurable Closed Loop Feedback Controlled Low Impact Docking System with Load Sensing Electromagnetic Capture Ring;
  5. NASA Case No. MSC 22953_1: Method and Apparatus for Reducing the Vulnerability of Latches to Single Event Upsets;
  6. NASA Case No. MSC 22980_1: Bubble Measuring Instrument and Method;
  7. NASA Case No. MSC 23026_1: Manually Operated Welding Wire Feeder;
  8. NASA Case No. MSC 23049_1: Microwave Treatment System for Prostate Cancer and Hyperplasia;
  9. NASA Case No. MSC 23076_1: Portable Hyperbaric Chamber;
  10. NASA Case No. MSC 23089_1: Improved Circularly Polarized Microstrip Antenna;
  11. NASA Case No. KSC 11886: Extreme Wind Velocity Measurement System;
  12. NASA Case No. KSC 12052: Communications Interface for Wireless Communications Headset.
  13. NASA Case No. LAR 15361_2: Gas Sensor Detector Balancing;
  14. NASA Case No. LAR 15463_2_SB: Fabrication of Molded Magnetic Article (Div of _1);
  15. NASA Case No. LAR 15493_2/3/4: Pistons and Cylinders Made of Carbon_Carbon Composites (Div of _1);
  16. NASA Case No. LAR 15499_1: Method and Apparatus for Assessment of Changes in Intracranial Pressure;
  17. NASA Case No. LAR 15508_1: Distributed Rayleigh Scatter Fiber Optic Strain Sensor;
  18. NASA Case No. LAR 15555_2: Molecular Level Coating of Metal Oxide Particles;
  19. NASA Case No. LAR 15761_1_SB: Melt_Extrusion of Polyimide Fibers, Ribbons, Rods, and Shaped Parts;
  20. NASA Case No. LAR 15816_1: Piezoelectric Macro_Fiber Composite Actuator and Method for Making Same;
  21. NASA Case No. LAR 15818_2: Optical Path Switching Based Differential Absorption Radiometry for Substance Detection;
  22. NASA Case No. LAR 15831_3: Hollow Polyimide Microspheres;
  23. NASA Case No. LAR 15856_1: Device and Method for Reducing Aircraft Noise;
  24. NASA Case No. LAR 15934_1: Edge Triggered Apparatus and Method for Measuring Strain in Bragg Gratings;
  25. NASA Case No. LAR 16093_1: Thickness Measurement Device for Ice or Ice Mixed with Water or Other Liquids (CIP of 15825 which was a CIP of 15061_1).
  26. NASA Case No. LEW 16056_2: Design and Manufacture of Long Life Hollow Cathode Assemblies;
  27. NASA Case No. LEW 16803_1: Segmented Thermal Barrier Coating;
  28. NASA Case No. LEW 16833_1: Self Tuning Impact Damper;
  29. NASA Case No. LEW 16968_1: Development of Processable Polyimides for High Temperature Applications with the Use of Triamine Additives;
  30. NASA Case No. LEW 16987_1: New Latent Reactive Endcaps for Polymers with Improved Thermal Oxidative Stability;
  31. NASA Case No. LEW 17012_1: Cyclohexene Endcaps for Polymers with Improved Thermal Oxidative Stability;
  32. NASA Case No. LEW 26691_1: PMR Extended Shelf Life Tech__A Chemical Process to Significantly Retard the Premature Aging of PMR Resin Solutions and PMR Prepregs.
  33. NASA Case No. MFS 26503_1: Microgravity Fiber Pulling Apparatus;
  34. NASA Case No. MFS 31066_1: Attachment Fitting for Pressure Vessel;
  35. NASA Case No. MFS 31230_1: Method and Apparatus for Reading Two Dimensional Identification Symbols Using Radar Techniques;
  36. NASA Case No. MFS 31289_1: Method and System for Reducing Plasma Loss in a Magnetic Mirror Fusion Reactor;
  37. NASA Case No. MFS 31331_1: Infrared Communication System;
  38. NASA Case No. MFS 31340_1: Lightweight Fluid Container;
  39. NASA Case No. MFS 31341_1: Atomic_Based Combined Cycle Propulsion System and Method;
  40. NASA Case No. MFS 31343_1: Low_Cost Gas Generator and Ignitor;
  41. NASA Case No. MFS 31364_1: Small Mobility Base Docking Simulator;
  42. NASA Case No. MFS 31368_1: Electro_Mechanical Multi_Message Display;
  43. NASA Case No. MFS 31387_1: Gravity Responsive NADH Oxidase of the Plasma Membrane;
  44. NASA Case No. MFS 31388_1: Identification of the Biological Clock;
  45. NASA Case No. MFS 31396_1: Method of Making Molecular Connections on a Nanometric Scale Using Nucleic Acids;
  46. NASA Case No. MFS 31403_1: Structural Assembly Device;
  47. NASA Case No. MFS 31419_1: Apparatus & Method for Generating Thrust Using a Two Dimensional, Asymmetrical Capacitor;
  48. NASA Case No. MFS 31438_1: Rocket Combustion Chamber Coating;
  49. NASA Case No. MFS 31454_1: Thermally Activated Joining Apparatus.


National Institutes of Health

SUMMARY: The inventions listed below are owned by agencies of the U.S. Government and are available for licensing in the U.S. in accordance with 35 U.S.C. 207 to achieve expeditious commercialization of results of federally-funded research and development. Foreign patent applications are filed on selected inventions to extend market coverage for companies and may also be available for licensing.

ADDRESSES: Licensing information and copies of the U.S. patent applications listed below may be obtained by contacting Dennis Penn, at the Office of Technology Transfer, National Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville, Maryland 20852_3804; telephone: 301/496_7056 ext. 211; fax: 301/402_0220; e_mail: pennd@od.nih.gov. A signed Confidential Disclosure Agreement will be required to receive copies of the patent applications.

1. Preparation and Use of Androgenic Compounds
Richard P. Blye and Hyun K. Kim (NICHD) DHHS Reference Nos. E_069_00/0 filed 31 Mar 2000 and E_069_00/1 filed 04 Apr 2000.
The technology describes the finding of the orally active androgenic compound, 7<greek_a>, 11<greek_b>_dimethyl_19_ nortestosterone 17_bucyclate (Also known as CDB_4386A). This 17_ bucyclate androgen compound is orally bioavailable and possesses greater potency than Methyltestosterone, the only oral androgen commercially available in this country. Too, this compound may be injected as an aqueous suspension, whereas other injectable androgens require an oil diluent. Androgens find use in the treatment of male hypogonadism regardless of the cause. Consequently they are used for the treatment of hypogonadotropic hypogonandism, as the androgenic component of male hormonal contraceptives and for androgen supplementation in hormone replacement therapy (HRT) in both men and women.

2. Process for Preparing 17-Alpha-Acetoxy-11-Beta-[4_(N,N-Dimethylamino)phenyl]-21-Methoxy-19-Norpregna-4, 9-Diene-3, 20-Dione Intermediates Useful in the Process, and Processes for Preparing Such Intermediates
Hyun K. Kim (NICHD), and Pemmaraju Rao, James Cessac, and Anne Marie Simmons of the Southwest Foundation for Biomedical Research DHHS Reference No. E_013_00/0 filed 29 Dec 1999.
This invention relates to a process for preparing 17_alpha_acetoxy_11_beta_[4_(N,N_dimethylamino)phenyl]_21_methoxy_19_norpregna_4,9_diene_3,20_dione. This method substantially increases the yield over existing methods and will substantially reduce the cost of production of this compound. Other advantages include: (1) Use of smaller quantities of solvent and reagent; (2) use of intermediates, reagents, or byproducts which are relatively safe to handle and dispose of, no use of chromatography; (3) a purification procedure easier to practice on large scale from kilograms to multi-kilograms, including no use of chromatography if possible; and (4) in some cases, recycling the by-products was successfully achieved. 

3. Novel Anti_thrombin Peptide From Mosquito Salivary Gland
Jesus G. Valenzuela, Jose M.C. Ribeiro, and Ivo Francischetti (NIAID) DHHS Reference No. E_143_99/0 filed 29 Jun 1999.
Currently, treatment and prophylaxis of thrombotic diseases involve therapeutic agents which act in one of two different ways. The first type inhibits a_thrombin activity or a_thrombin formation, thus preventing clot formation. The second category accelerates thrombolysis and dissolves the blood clot, thereby removing it from the blood vessel and unblocking the flow of blood. Heparin is an example of the first class and is widely used; however, heparin is less effective in treating patients with an anti_thrombin III deficiency. Hirudin is an example of the second class of anti_thrombotic drugs. This invention relates to an anti_thrombin (Anophelin) isolated from the salivary glands of the mosquito Anopheles albimanus. The purified peptide inhibits thrombin induced platelet aggregation, thrombin esterolytic activity, and thrombin cleavage of fibrinogen. This peptide has no homologies to proteins of known function in GenBank, and is a novel, specific, and tight binding inhibitor of <greek_a>_thrombin.

4. Ichthyosiform Skin Diseases
Peter M. Steinert, Nemes Zoltan and Lyuben Marckov (NIAMS) DHHS
Reference No. E_149_99/0 filed 23 Jun 1999.
Many inherited autosomal recessive ichthyoses (ARI) are caused by improper or incomplete lipid barrier function in the skin due to genetic errors of either protein or lipid synthesis. It is previously known that the mutations in the transglutaminase 1 gene resulting in inactive enzyme is the cause of one ARI disease termed lamellar ichthyosis. This relates to the discovery that a principal function of the enzyme is to attach ceramide lipids for complete protein/lipid barrier function in the skin. This invention also describes how to: (1) Make large quantities of this enzyme that can be stored in a stable form which can be readied for use at short notice; (2) a simple way to make synthetic ceramide lipid analogs that function the same way as normal skin ceramides; and (3) make synthetic lipid vesicles that can carry, in a stable fashion, both the enzyme and synthetic ceramide so that it might be applied to affected ARI skin in order to provide ameliorative therapy.

5. High Sensitivity Phage Display Protein Detection Method
Carl R. Merril (NIMH) DHHS Reference No. E_185_98/0 filed 14 Apr 1999.
This new technology extends the range of protein detection appreciably under the absolute limit of 0.01ng for the Silver stain method. In an average protein molecule this amounts to 20 million molecules. The average cellular concentration of protein is 5000 molecules, so that an amplification system is needed to detect protein on that level. In this method, phage that display specific ligands or antibodies provide such an amplification system and therefore allow for detection. In addition, a particular phage expressing a known binding protein may be used to identify a specific protein and aid in the purification of that specific protein. The identification ability has both diagnostic and therapeutic potential. The key novel feature of this technology in the market place would be its high sensitivity and the numerous benefits associated with it. It opens up whole new areas of analysis, such as on the cellular level, allowing for looking at protein variations within a single cell. Theoretically, as little as one protein molecule could be detectable. The potential market for this invention would be in several distinct areas: Research__incorporation into kits to perform complete assays; Purification__aiding in the manufacturing process; Diagnostic__detection of variations of a specific protein within a cell; Therapeutic__identification of specific drug targets through the ability to bind to receptor sites.


ADDRESSES: Licensing information and copies of the U.S. patent applications listed below may be obtained by writing to the indicated licensing contact at the Office of Technology Transfer, National Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville, Maryland 20852_3804; telephone: 301/496_7057; fax: 301/402_0220. A signed Confidential Disclosure Agreement will be required to receive copies of the patent applications.

6. Identification of a Novel Renal NADPH Oxidase
Thomas L. Leto, Miklos Geiszt (NIAID)
DHHS Reference No. E_116_00/0 Filed 12 Apr 2000
Licensing Contact: Marlene Shinn; 301/496_7056 ext. 285; e_mail: shinnm@od.nih.gov

The NIH announces the identification of a renal NAD(P)H oxidase termed RenOX, produced by the proximal convoluted tubule cells of the kidney, which is proposed to be an oxygen sensor in the kidney involved in regulation of production of erythropoietin. As a source of superoxide and other reactive oxygen species in the kidney, RenOX is thought to have a direct role in the oxidative down_regulation of erythropoietin and other hypoxia_responsive genes in response to oxygen levels detected in the kidney. Because the inhibition of RenOX may lead to an increase in the production of erythropoietin, it has been suggested that it can be used as a screening tool for the development of therapies against diseases which currently use recombinant erythropoietin as a treatment. These include anemia associated with chronic renal failure, HIV infection and antiretroviral therapy, cancer, cancer chemotherapy, and chronic inflammatory conditions (rheumatoid arthritis, inflammatory bowel disease). Because recombinant erythropoietin is considered a costly therapy, it may be that an inhibitor of RenOX may prove to be a less expensive alternative. It is also possible that drugs determined to affect RenOX activity may be used to treat hypertension in patients, since RenOX may also affect proton transport and sodium reabsorption by kidney tubule cells. Because expression of recombinant RenOX was shown to induce cellular senescence, other uses of RenOX, by way of gene therapy, may include limiting the growth of tumors either by inducing tumor cell senescence or inhibiting angiogenesis. Because RenOX is proposed to be a key component of oxygen sensing in the kidney, the NIH believes it to be a valuable means by which new drugs and therapies can be developed and benefit the public health. This research has been published in Geiszt et al., ``Identification of RenOX, an NAD(P)H Oxidase in Kidney,'' Proc. Nat. Acad.Sci., U.S.A., vol 97, pp 8010_8014 (July 5, 2000). 

7. Amyloid <greek_b> Is a Ligand for FPR Class Receptors 
Ji Ming Wang et al. (NCI) Serial No. 60/186,144 
Licensing Contact: Marlene Shinn; 301/496_7056 ext. 285; e_mail: shinnm@od.nih.gov

Alzheimer's disease is the most important dementing illness in the United States because of its high prevalence. 5 to 10% of the United States population 65 years and older are afflicted with the disease. In 1990 there were approximately 4 million individuals with Alzheimer's, and this number is expected to reach 14 million by the year 2050. It is the fourth leading cause of death for adults, resulting in more than 100,000 deaths annually. Amyloid beta (A<greek_b>) has been identified as playing an important role in the neurodegeneration of Alzheimer's disease. However the mechanism used is unknown and has been postulated to be either direct or indirect through an induction of inflammatory responses. The NIH announces a new early stage technology, that identifies the 7_transmembrane, G_protein_coupled receptor, FPRL_1, as a functional receptor for A<greek_b> peptides. The A<greek_b> peptides use the FPRL_ 1 receptor to attract and activate human monocytes, and have been identified as a principal component of the amyloid plaques associated with Alzheimer's disease. In addition, astrocytes stimulated with ligands of FPRL1 produce a proinflammatory cytokine interleukin 6. Because amyloid <greek_b> peptides interact with the FPRL1 receptor, a direct link is created between A<greek_b> and the inflammation observed during the course of Alzheimer's disease. This technology provides a target in which to direct the development of preventative or therapeutic agents for Alzheimer's disease. Newly discovered A<greek_b>_FPR class receptor complexes can be used to modulate the A<greek_b>_induced inflammation response by administering polynucleotides, chemical compounds, or polypeptides that interact with either A<greek_b> or the FPR class receptor(s), or inhibit complex formation altogether. Although this technology is in the early stages of drug development, the potential to find new drugs to Alzheimer's and other neurodegenerative diseases is a real possibility, through its use, to those working in this field. 

8. Constitutively Open Voltage_Gated K+ Channels and Methods for Discovering Modulators Thereof 
Drs. Kenton J. Swartz, David H. Hackos (NINDS)
DHHS Reference Number E_286_99/0 Filed 10 Feb 2000
Licensing Contact: John Rambosek, Ph.D.; 301/496_7056 ext. 270; e_mail: rambosej@od.nih.gov

This technology relates to materials and methods for developing high throughput strategies for discovery of both inhibitors and activators of voltage_gated potassium channels. Voltage gated potassium channels are important regulators of electrical excitability throughout the nervous system, vascular and cardiac smooth muscle, and various secretory tissues such as the pancreas. Drugs that modulate the activity of these receptors could have applications in a variety of therapeutic areas involving abnormal electrical activity, including epilepsy, stroke, cardiac arrhythmia, hypertension, and diabetes. The technology described here involves the identification of mutations in voltage_gated potassium channels that effectively lock the pore open at all membrane potentials. Previously, it has not been possible to develop yeast_based high throughput screens using voltage-gated potassium channels because these channels are normally closed at the negative membrane potentials associated with yeast. In addition, other types of high_throughput screens for K channel inhibitors and activators use voltage_sensitive dyes or indicators as reporters of K channel activity. Mutations that lock voltage_gated K channels open at negative voltages could significantly improved the sensitivity of these voltage_sensitive screens. The strategy employed to lock open voltage_gated potassium channels involves alterations in an area of the protein that is conserved in all voltage-gated potassium channels, and should therefore be applicable to all such potassium channels. This will allow generally for the development of high_throughput screens for activators and inhibitors of all voltage_gated potassium channels.

A Provisional Patent Application Serial Number 60/081,692 has been filed for this technology. It is available for licensing through a DHHS Patent license.

9. Equilibrium Thermodynamics_Based Ligand Binding Assays for Macromolecules
Dong Xie, John W. Erickson (NCI) DHHS Reference No. E_076_00/0 Filed 01 Feb 2000
Licensing Contact: J.P. Kim; 301/496_7056 ext. 264; e_mail: kimj@od.nih.gov

High affinity binding is observed in many biological processes and is assayed in the design and development of compounds as therapeutic agents for specific biological targets. The accurate determination of binding affinities for HIV protease inhibitors is important for the determination of the biochemical fitness of drug_resistant HIV variants that contain mutations in the protease gene. There remains a need for a highly sensitive, accurate, and widely applicable method for determining the binding affinity of a ligand for a folded macromolecule. Accordingly, the present invention provides methods for determining the binding affinity of a ligand for a macromolecule and methods for determining whether or not a compound is a reversible ligand for a macromolecule, e.g., in the development of HIV therapeutics.

10. Delivery of Proteins Across Polar Epithelial Cell Layers
David Fitzgerald et al. (NCI) DHHS Reference No. E_277_98/0 Filed 22 Oct 1999
Licensing Contact: Carol Salata; 301/496_7735 ext. 232; e_mail: salatac@od.nih.gov

Many pharmaceutical proteins which need to gain systemic access cannot be administered enterally because the enzymes of the digestive system degrade the proteins before they gain access. Therefore, pharmaceutical proteins generally are administered by injection. Diseases that require repeated administration of a protein over long period of time, such as diabetes, can require daily injection. Of course, frequent injections are not pleasant for the patient and means to deliver proteins without injection would be advantageous. This invention provides methods for parenteral administration of a protein by transmucosal delivery and without injection. Molecules that bind <greek_a>2 macroglobulin receptor, when applied to the apical surface of a polarized epithelial cell layer, are able to traverse through the basal side of the cell and released into the sub_epithelial space. This invention takes advantage of that fact by using Pseudomonas exotoxin and derivatives as carriers to deliver proteins and molecules bound to them across the epithelial surface without resorting to injection of the protein.

11. Nucleic Acid Molecules Encoding Hepatitis C Virus, Chimeric Hepatitis C Virus or Hepatitis C Virus Envelope Two Protein Which Lacks All or Part of Hypervariable Region One of the Envelope Two Protein and Uses Thereof
Xavier Forns, Jens Bukh, Suzanne U. Emerson, Robert H. Purcell (NIAID)
DHHS Reference No. E_287_99/0 Filed 23 Sep 1999
Licensing Contact: Carol Salata; 301/496_7735 ext. 232; e_mail: salatac@od.nih.gov

HCV is an enveloped, single stranded RNA virus, approximately 50 nm in diameter, that has been classified as a separate genus in the Flaviviridae family. The ability of HCV to undergo rapid mutation in a hypervariable region(s) of the genome coding for envelope protein mayallow it to escape immune surveillance by the host; thus, most persons infected with HCV develop chronic infection. These chronically infected individuals have a relatively high risk of developing chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. This invention relates to nucleic acid molecules which encode a hepatitis C virus envelope two protein which lacks all or part of the hypervariable region one (HVR1) of the envelope two (E2) protein. RNA transcripts from a full_length HCV cDNA clone from which the HVR1 was removed were able to replicate when transfected into the liver of a chimpanzee. The fact that the HVR1 is not essential for virus replication is relevant because the partial or complete deletion of this region might change the immune response to a more effective one. Attenuated viruses could be generated and used as vaccine candidates. In addition, DNA constructs or proteins lacking this region could be used as vaccine candidates.

12. Agonist and Antagonist Peptides of CEA
Jeffrey Schlom, Elena Barzaga, Sam Zaremba (NCI)
Serial No. 60/061,589 filed 10 Oct 1997; PCT/US98/19794 filed 22 Sep 1998; DHHS Reference No. E_099_96/3 filed 06 Apr 2000
Licensing Contact: Elaine White; 301/496_7056 ext. 282; e_mail: gesee@od.nih.gov

The current invention embodies the identification of an enhancer agonist peptide variant of a nine amino acid sequence (designated CAP_1) contained in the human carcinoembryonic antigen (CEA) gene. CEA is an antigen which is overexpressed on a variety of human tumor types including the following carcinomas: colorectal, breast, non_small cell lung, pancreatic and head and neck. Studies have shown that the CAP_1 peptide is an immunodominant epitope of CEA. Moreover, recent studies have shown that the modification of a single amino acid in the CAP_1 sequence results in the generation of a enhancer agonist peptide, designated CAP1_6D. The CAP1_6D peptide is capable of stimulating human T_cells to far greater levels than that of CAP1. These T_cells, moreover, have been shown to lyse human tumor cells expressing native CEA. Thus the CAP1_6D enhancer agonist peptide represents a potential immunogen for use as therapeutic vaccine against a wide range of human cancers which express CEA and may also have potential use as a vaccine to prevent preneoplastic lesions or cancers expressing CEA. 


ADDRESSES: Licensing information and copies of the U.S. patent applications listed below may be obtained by contacting Peter A. Soukas, J.D., at the Office of Technology Transfer, National Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville, Maryland 20852_3804; telephone: 301/496_7056 ext. 268; fax: 301/402_0220; e-mail: soukasp@od.nih.gov . A signed Confidential Disclosure Agreement will be required to receive copies of the patent applications. 

13. Cloned Genome of Infectious Hepatitis C Virus of Genotype 2a and Uses Thereof
Jens Bukh, Masayuki Yanagi, Robert H. Purcell, Suzanne U. Emerson (NIAID)
DHHS Reference No. E_100_99/0 Filed 04 Jun 1999

The current invention provides a nucleic acid sequence comprising the genome of infectious hepatitis C viruses (HCV) of genotype 2a. The encoded polyprotein differs from those of the infectious clones of genotypes 1a and 1b (PHS Invention Number E_050_98/0) by approximately thirty (30) percent. It covers the use of this sequence and polypeptides encoded by all or part of the sequence, in the development of vaccines and diagnostic assays for HCV and the development of screening assays for the identification of antiviral agents for HCV. Additional information can be found in Yanagi et al. (1999), Virology 262, 250_263.

14. HCV/BVDV Chimeric Genomes and Uses Thereof 
Jae_Hwan Nam, Jens Bukh, Robert H. Purcell, Suzanne U. Emerson (NIAID)
DHHS Reference No. E_102_99/0 Filed 04 June 1999

The current invention provides nucleic acid sequences comprising chimeric viral genome of hepatitis C Virus (HCV) and bovine viral diarrhea viruses (BVDV). The chimeric viruses are produced by replacing the structural region or a structural gene of an infectious BVDV clone with the corresponding region or gene of an infectious HCV. It covers the use of these sequences and polypeptides encoded by all or part of the sequences in the development of vaccines and diagnostic assays for HCV and the development of screening assays for the identification of antiviral agents for HCV.

15. Infectious cDNA Clone of GB Virus B and Uses Thereof
Jens Bukh, Masayuki Yanagi, Robert H. Purcell, Suzanne U. Emerson (NIAID)
DHHS Reference No. E_173_99/0 Filed 04 Jun 1999

The current invention provides nucleic acid sequences comprising the genomes of infectious GB virus B, the most closely related member of the Flaviviridae to hepatitis C virus (HCV). It also covers chimeric GBVB_HCV sequences and polypeptides for use in the development of vaccines and diagnostic assays for HCV and the development of screening assays for the identification of antiviral agents for HCV. Additional information can be found in Bukh et al. (1999), Virology 262, 470_478.

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