Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Virus or component thereof
Reexamination Certificate
2007-09-11
2007-09-11
Chen, Stacy B. (Department: 1648)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Virus or component thereof
C424S185100, C424S186100, C530S300000, C530S325000, C530S326000
Reexamination Certificate
active
10384976
ABSTRACT:
Using CTL epitopes to theEbolaGP, NP, VP24, VP30, VP35 and VP40 virion proteins, a method and composition for use in inducing an immune response which is protective against infection withEbolavirus is described.
REFERENCES:
patent: 5792462 (1998-08-01), Johnston et al.
patent: 5977316 (1999-11-01), Chatterjee et al.
patent: 6340463 (2002-01-01), Mitchell et al.
patent: 6630144 (2003-10-01), Hart et al.
patent: 6713069 (2004-03-01), Gallaher
patent: 2002/0164582 (2002-11-01), Hart et al.
patent: 2004/0053865 (2004-03-01), Hart et al.
patent: 2004/0146859 (2004-07-01), Hart et al.
patent: WO96/37616 (1996-11-01), None
patent: WO99/32147 (1999-07-01), None
patent: WO 00/00616 (2000-01-01), None
patent: WO 00/00617 (2000-01-01), None
patent: WO 01/016183 (2001-03-01), None
Hart, Mary Kate, Vaccine reserach efforts for filoviruses, International Journal for Parasitology, 2003, 33:583-595.
Voichkov et al., “The envelope glycoprotein of Ebola virus contains an immunosuppressive-like domain similar to oncogenic retroviruses”, FEBS Letters, vol. 305, No. 3, pp. 181-184 (Jul. 1992).
Sanchez et al., “Biochemical Analysis of the Secreted and Virion Glycoproteins of Ebola Virus”, J. Virology, Aug. 1998, vol. 72, pp. 6442-6447.
Wilson et al., “Epitopes Involved in Antibody-Mediated Protection from Ebola Virus”, Science, vol. 387, Mar. 3, 2000, pp. 1664-1666.
Ichihashi and Oie, “Neutralizing Epitope on Penetration Protein of Vaccinia Virus”, Virology 220, pp. 491-494 (1996).
Wolffe et al., “A myristylated membrane protein encoded by the vaccinia virus L1R open reading frame is the target of potent neutralizing monoclonal antibodies”, Virology 211, pp. 53-63 (1995).
Roper et al., “Extracellular vaccinia virus envelope glycoprotein encoded by the A33R gene”, J. Virology, Jun. 1996, vol. 70, No. 6, pp. 3753-3762.
Isaacs et al., “Characterization of a vaccinia virus-encoded 42-kilodalton class 1 membrane glycoprotein component of the extracellular virus envelope”, J. Virology, Dec. 1992, vol. 66, No. 12, pp. 7217-7224.
Abstract W33-5, “DNA vaccination against poxviruses using combinations of IMV and EEV immungens”, presented Jul. 2000, American Society for Virology Meeting, p. 113.
Abstract P23-6, “DNA immunization with the vaccinia L1R and/or A33R genes”, Jul. 1998, poster at American Society for Virology meeting.
Meyer et al., “Identification of binding sites for neutralizing monoclonal antibodies on the 14-kDa fusion protein of orthodox viruses”, Virology 200, Short Communications, pp. 778-783 (1994).
Czerny and Mahnel, “Structural and functional analysis of orthopoxvirus epitope with neuralizing monoclonal antibodies”, J. General Virology (1990) vol. 71, pp. 2341-2352.
Hooper et al., “DNA vaccination with vaccinia virus L1R and A33R genes protects mice against a lethal poxvirus challenge”, Virology 266, pp. 329-339 (2000).
Vazquez and Esteban, “Identification of functional domains in the 14-kilodalton envelope protein (A27L) of vaccinia virus”, J. Virology, Nov. 1999, vol. 73, No. 11, pp. 9098-9109.
Vazquez et al., “The vaccinia virus 14-kilodalton (A27L) fusion protein forms a triple coiled-coil structure and interacts with the 21-kilodalton (A17L) virus membrane protein through a C-terminal of alpha-helix”, J. Virology, Dec. 1998, vol. 72, No. 12, pp. 10126-10137.
Rodriguez et al., “The vaccinia virus 14-kilodalton fusion proteins forms a stable complex with the processed protein encoded by the vaccinia virus A17L gene”, J. Virology, Jun. 1993, vol. 67, No. 6, pp. 3435-3440.
Lai et al., “The purified 14-kilodalton envelope protein of vaccinia virus produced onEscherichia coliinduces virus immunity in animals”, J. Virology, Oct. 1991, vol. 65, No. 10, pp. 5631-5635.
Rodriguez and Esteban, “Mapping and nucleotide sequence of the vaccinia virus gene that encodes a 14-kilodalton fusion protein”, J. Virology, Nov. 1987, vol. 61, No. 11, pp. 3550-3554.
Rodriguez et al., “Isolation and characterization of neutralizing monoclonal antibodies to vaccinia virus”, J. Virology, Nov. 1985, vol. 56, No. 2, pp. 482-488.
NCBI PubMed medline, Abstract for Rodriguez et al., “Isolation and characterization of neutralizing monoclonal antibodies to vaccinia virus”, J. Virology, Nov. 1985, vol. 56, No. 2, pp. 482-488.
Lin et al., “Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphorogenesis and a virus infection in vtiro and in vivo”, J. Virology, Apr. 2000, vol. 74, No. 7, pp. 3353-3365.
Gordon et al., “A prominent antigenic surface polypeptide involved in the biogenesis and function of the vaccinia virus envelope”, Virology 181, pp. 671-686 (1991).
Ichihashi et al., “Identification of a vaccinia virus penetration protein”, Virology 202, pp. 834-843 (1994).
Demkowicz et al., “Identification and characterization of vaccinia virus genes encoding proteins that are highly antigenic in animals and are immunodominant in vaccinated humans”, J. Virology, jan. 1992, vol. 66, No. 1, pp. 386-398.
Wilson et al., “Ebola virus: the search for vaccines and treatments”, CMLS Cell., Mol Life Sci., 58 (2001) pp. 1-16.
Pushko et al, “Venezuelan Equine Encephalitis virus replicon vector: immunogenicity studies with ebola NP and GP genes in guinea pigs”, Vaccines 97, Molecular Approaches to the Control of Infectious Diseases, Cold Spring Harbor Laboratory Press, 1997, pp. 253-258.
Geisbert et al., “Evaluation in nonhuman primates of vaccines against Ebola virus”, Perspectives, Emerging Infectious Diseases, vol. 8, No. 5, May 2002, pp. 503-507.
Pushko et al., “Recombinant RNA replicons derived from attenuated Venezuelan equine encephalitis virus protect guinea pigs and mice from Ebola hemorrhagic fever virus”, Vaccine 11 (2000) pp. 1-12.
Wilson et al., “Vaccine potential of Ebola virus VP24, VP30, VP35, and VP40 proteins”, Virology 286, pp. 384-390 (2001).
Wilson and Hart, “Protection from Ebola virus mediated by cytotoxic T lymphocytes specific for the viral nucleoprotein”, J. Virology, Mar. 2001, vol. 75, No. 6, pp. 2660-2664.
Maruyama et al., “Recombinant human monoclonal antibodies to Ebola virus”, J. Infectious Diseases, 1999, 179 (Suppl 1), pp. S235-S239.
Jahrling et al., “Evaluation of immune globulin and recombinant interferon-alpha2b for treatment of experimental Ebola virus infections”, J. Infectious Diseases, 1999, 170 (Suppl 1), pp. S224-S234.
Volchkov et al., “Release of viral glycoproteins during Ebola virus infection”, Virology 245, pp. 110-119 (1998).
GenBank, Database printout, for Sanchez et al., Ebola virus nuceoprotein, polymerase copmlex protein (VP35), matrix protein (VP40), glycoprotein (GP), minor nucleoprotein (VP30), and membrance-associates structural protein (VP24), Oct. 14, 1997 (7 pages).
Hevey et al., “Antigenicity and vaccine potential of Marburg virus glycoprotein expressed by baculovirus recombinants”, Virology 239, pp. 206-216 (1997).
Maruyama et al., “Ebola virus can be effectively neutralized by antibody produced in natural human infection”, J. Virology, Jul. 1999, vol. 73, No. 7, pp. 6024-6030.
Wilson et al., “Ebola virus: the search for vaccines and treatments”, CMLS Cell. Mol. Life Sci. 58 (2001), pp. 1826-1841.
Maruyama et al., “Recombinant human monoclonal antibodies to Ebola virus”, J. Infectious Diseases, 1999, 179 (Suppl 1), pp. S235-S239.
Sanchez et al., “The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing”, PNAS, USA, vol. 93, pp. 3602-3607, Apr. 1996.
Jahrling et al., “Passive immunization of Ebola virus-infected cynomol
Bailey Michael Adam
Hart Mary Katherine
Olinger, Jr. Gene Garrard
Wilson Julie Ann
Arwine Elizabeth
Chen Stacy B.
United States of America as Represented by the Secretary of the
LandOfFree
Ebola peptides and immunogenic compositions containing same does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Ebola peptides and immunogenic compositions containing same, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Ebola peptides and immunogenic compositions containing same will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3730739