New Approaches to Animal Vaccines Utilizing Genetic Engineering

References

• Nathanson N., Langmuir A. D. The Cutter incident. Poliomyelitis following formaldehyde-inactivated poliovirus vaccination in the United States during the Spring of 1955. I. Background. Am. J. Hyg. 1963; 78: 16
   PubMed Web of Science ®Google Scholar
• King A. M. Q., Underwood B. O., McCahon D., Newman J. W. I., Brown F. Biochemical identification of viruses causing the 1981 outbreaks of foot-and-mouth disease in the UK. Nature (London) 1981; 293: 479
   PubMed Web of Science ®Google Scholar
• Nkowane B. M., Wassilak S. G. F., Orenstein W. A., Bart K. J., Schonberger L. B., Hinman A. R., Kew O. M. Vaccine-associated paralytic poliomyelitis in the United States: 1973 through 1984. JAMA 1987; 257: 1335
   PubMed Web of Science ®Google Scholar
• Kelling C. L., Schipper I. A., Strum G. E., Carlson R. B., Tilton J. E. Infectious bovine rhinotracheitis (IBR) abortion — observations on incidence in vaccinated and non-vaccinated and exposed cattle. Cornell Vet. 1973; 63: 383
   PubMedGoogle Scholar
• Allen G. P., Yeargan M. R., Turtinin L. W., Bryans J. T. A new field strain of equine abortion virus (equine herpesvirus-1) among Kentucky horses. Am. J. Vet. Res. 1985; 46: 139
   Web of Science ®Google Scholar
• Itakura K., Hirose T., Crea R., Riggs A. D., Heyneker H. L., Bolivar F., Boyer H. W. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 1977; 198: 1056
   PubMed Web of Science ®Google Scholar
• Maniatis T., Fritsch E. F., Sambrook J. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. 1982
   Google Scholar
• Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base specific chemical cleavages. Methods in Enzymology, L. Grossman, K. Moldave. Academic Press, New York 1980; Vol. 65: 499
   Google Scholar
• Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 1977; 74: 5463
   PubMed Web of Science ®Google Scholar
• Merrifield R. B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc 1963; 85: 2149
   Web of Science ®Google Scholar
• Barany G., Merrifield R. B. Solid-phase peptide synthesis. The Peptides, E. Gross, J. Meienhofer. Academic Press, New York 1980; Vol. 2: 1
   Google Scholar
• Kohler G., Milstein C. Coninuous cultures of fused cells secreting antibody of predefined specificity. Nature (London) 1975; 256: 495
   PubMed Web of Science ®Google Scholar
• McCullough K. C. Monoclonal antibodies: implications for virology. Arch. Virol. 1986; 87: 1
   PubMed Web of Science ®Google Scholar
• Bittle J. L., Houghten R. A., Alexander H., Shinnick T. M., Sutcliffe J. G., Lerner R. A., Rowlands D. J., Brown F. Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature (London) 1982; 298: 30
   PubMed Web of Science ®Google Scholar
• Sutcliffe J. G., Shinnick T. M., Green N., Lerner R. A. Antibodies that react with predetermined sites on proteins. Science 1983; 219: 660
   PubMed Web of Science ®Google Scholar
• Steward M. W., Howard C. R. Synthetic peptides: a next generation of vaccines. Immunol. Today 1987; 8: 51
   PubMedGoogle Scholar
• Atassi M. Z. Perspectives of the immunology of proteins. Immunobiology of Proteins and Peptides — III. Viral and Bacterial Antigens, M. Z. Atassi, H. L. Bachrach. Plenum Press, New York 1985; 1
   Google Scholar
• Geysen H. M., Meloen R. H., Barteling S. J. Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 3998
   PubMed Web of Science ®Google Scholar
• Geysen H. M., Barteling S. J., Meloen R. H. Small peptides induce antibodies with a sequence and structural requirement for binding antigen comparable to antibodies raised against the native protein. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 178
   PubMed Web of Science ®Google Scholar
• Geysen H. M., Rodda S. J., Mason T. The delineation of peptides able to mimic assembled epitopes. Synthetic Peptides as Antigens, Ciba Found. Symp. 119. John Wiley & Sons, New York 1986; 130
   Google Scholar
• Perrin P., Thibodeau L., Sureau P. Rabies immunosome (subunit vaccine) structure and immunogenicity. Pre- and post-exposure protection studies. Vaccine 1985; 3: 325
   PubMed Web of Science ®Google Scholar
• Morein B., Simons K. Subunit vaccines against enveloped viruses: virosomes, micelles and other protein complexes. Vaccine 1985; 3: 83
   PubMed Web of Science ®Google Scholar
• Paoletti E., Weinberg R. L., Davis S. W., Davis M. Genetically engineered poxviruses: a novel approach to the construction of live vaccines. Vaccine 1984; 2: 204
   PubMedGoogle Scholar
• Kit S., Kit M., Pirtle E. C. Attenuated properties of thymidine kinase-negative deletion mutant of pseudorabies virus. Am. J. Vet. Res. 1985; 46: 1359
   PubMed Web of Science ®Google Scholar
• Bona C., Moran T. Idiotype vaccines. Ann. Inst. Pasteur Immunol. 1985; 136C: 299
   PubMedGoogle Scholar
• Babbitt B. P., Allen P. M., Matsueda G., Haber E., Unanue E. R. Binding of immunogenic peptides to la histocompatibility molecules. Nature (London) 1985; 317: 359
   PubMed Web of Science ®Google Scholar
• Zanetti M., Sercarz E., Salk J. The immunology of new generation vaccines. Immunol. Today 1987; 8: 18
   PubMedGoogle Scholar
• Buus S., Sette A., Colon S. M., Jenis D. M., Grey H. M. Isolation and characterization of antigen-la complexes involved in T-cell recognition. Cell 1986; 47: 1071
   PubMed Web of Science ®Google Scholar
• Kleid D. G., Yansura D., Small B., Dowbenko D., Moore D. M., Grubman M. J., McKercher P. D., Morgan D. O., Robertson B. H., Bachrach H. L. Cloned viral protein vaccine for foot-and-mouth disease responses in cattle and swine. Science 1981; 214: 1125
   PubMed Web of Science ®Google Scholar
• Hunsmann G., Moennig V., Schafer W. Properties of mouse leukemia viruses. IX. Active and passive immunization of mice against Friend leukemia with isolated viral GP 71 glycoprotein and its corresponding antiserum. Virology 1975; 66: 327
   PubMed Web of Science ®Google Scholar
• Ihle J. N., Collins J. J., Lee J. C., Fischinger P. J., Moenning V., Schafer W., Hanna M. G., Jr., Bolognese D. P. Characterization of the immune response to the major glycoprotein (gp71) of Friend leukemia virus I response in BALB/c mice. Virology 1976; 75: 74
   PubMed Web of Science ®Google Scholar
• Osterhaus A., Weijer K., Uytdehaag F., Jarrett O., Sundquist B., Morein B. Induction of protective immune response in cats by vaccination with feline leukemia virus iscom. J. Immunol. 1985; 135: 591
   PubMed Web of Science ®Google Scholar
• Blancou J., Kieny M. P., Lathe R., Lecocq J. P., Pastoret P. P., Souiebot J. P., Desmettre P. Oral vaccination of the fox against rabies using a live recombinant vaccinia virus. Nature (London) 1986; 322: 373
   PubMed Web of Science ®Google Scholar
• Rupprecht C. E., Wiktor T. J., Johnston D. H., Hamir A. N., Dietzhold B., Wunner W. H., Glickman L. T., Koprowski H. Oral immunization and protection of raccoons (Procyon lotor) with a vaccinia-rabies glycoprotein recombinant virus vaccine. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 7947
   PubMed Web of Science ®Google Scholar
• Faras A., Sadowski P., Pilacinski W., Hu S. L., Hailing S., Collett M., Salstrom J., Watson R., Robbins A., Muscoplat C., Enquist L., Sherman D., Acres S. The efficacy of bioengineered anti-toxins and vaccines for animals health care. Advances in Gene Technology: Molecular Genetics of Plants and Animals, K. Downey, R. W. Voellmy, F. Ahmad, J. Schultz. Academic Press, New York 1983; 495
   Google Scholar
• Brown E. Prospects for synthetic peptide vaccines against foot-and-mouth disease. Ann. Inst. Pasteur Virol. 1986; 137E: 479
   Google Scholar
• Bachrach H. L., Moore D. M., McKercher P. D., Polatnick J. An experimental protein vaccine for foot-and-mouth disease. Perspectives in Virology, M. Pollard. Raven Press, New York 1978; Vol. 10: 147
   Google Scholar
• Bachrach H. L., Moore D. M., McKercher P. D., Polatnick J. Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus. J. Immunol. 1975; 115: 1636
   PubMed Web of Science ®Google Scholar
• Bachrach H. L., Morgan D. O., Moore D. M. Foot-and-mouth disease immunogenic capsid protein VPT: N-terminal sequences and immunogenic peptides obtained by CNBr and tryptic cleavages. Intervirology 1979; 12: 65
   PubMed Web of Science ®Google Scholar
• Bachrach H. L., Swaney J. B., VandeWoude G. F. Isolation of the structural polypeptides of foot-and-mouth disease virus and analysis of their C-terminal sequences. Virology 1973; 52: 520
   PubMed Web of Science ®Google Scholar
• Shire S. J., Bock L., Ogez J., Bilder S., Kleid D., Moore D. M. Purification and immunogenicity of fusion VP1 protein of foot-and-mouth disease virus. Biochemistry 1984; 23: 6474
   PubMed Web of Science ®Google Scholar
• McKercher P. D., Moore D. M., Morgan D. O., Robertson B. H., Callis J. J., Kleid D. G., Shire S. J., Yansura D. G., Dowbenko D., Small B. Dose-response evaluation of a genetically engineered foot-and-mouth disease virus polypeptide immunogen in cattle. Am. J. Vet. Res. 1985; 46: 587
   PubMed Web of Science ®Google Scholar
• Bachrach H. L. Recombinant DNA technology for the preparation of subunit vaccines. J. Am. Vet. Med. Assoc. 1982; 181: 992
   PubMed Web of Science ®Google Scholar
• Robertson B. H., Moore D. M., Grubman M. J., Kleid D. G. Identification of an exposed region of the immunogenic capsid polypeptide VP1 on foot-and-mouth disease virus. J. Virol. 1983; 46: 311
   PubMed Web of Science ®Google Scholar
• Yansura D. G., Dowbenko D., Weddeil G. N., Hoatlin M. E., Shire S. J., Bock L. A., Patzer E. J., Kleid D. G., Moore D. M., Robertson B. H., Grubman M. J., Morgan D. O., McKercher P. D. Biosynthetic vaccine for foot-and-mouth disease. Advances in Gene Technology: Molecular Genetics of Plants and Animals, K. Downey, R. W. Voellmy, F. Ahmad, J. Schultz. Academic Press, New York 1983; 479
   Google Scholar
• Moore D., Morgan D., Robertson B., McKercher P., Patzer E., Shire S., Kleid D. G. A highly antigenic portion of FMDV 01 VP1 elicits bovine antibodies which protect mice but not cattle from FMDV infection. Abstracts: Modern Approaches to Vaccines. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. 1983
   Google Scholar
• Ouldridge E. J., Rowlands D. New approaches to the epidemiology of foot-and-mouth disease. Outlook Agric 1986; 15: 40
   Web of Science ®Google Scholar
• Morgan D. O., McKercher P. D., Bachrach H. L. Quantitation of the antigenicity and immunogenicity of purified foot-and-mouth disease virus vaccines for swine and steers. Appl. Microbiol. 1970; 20: 770
   PubMedGoogle Scholar
• Bachrach H. L. Foot-and-mouth disease and its antigens. Immunobiology of Proteins and Peptides — III. Viral and Bacterial Antigens, M. Z. Atassi, H. L. Bachrach. Plenum Press, New York 1985; 27
   Google Scholar
• Rweyemamu M. M., Ouldridge E. J., Head M., Purse F. Evaluation of the antigenic variation within type A foot-and-mouth disease virus isolates from Asia. J. Biol. Stand. 1984; 12: 191
   PubMedGoogle Scholar
• DiMarchi R., Brooke G., Gale C., Cracknell V., Doel T., Mowat N. Protection of cattle against foot-and-mouth disease by a synthetic peptide. Science 1986; 232: 639
   PubMed Web of Science ®Google Scholar
• Strohmaier K., Franze R., Adam K. H. Location and characterization of the antigenic portion of the FMDV immunizing protein. J. Gen. Virol. 1982; 59: 295
   PubMed Web of Science ®Google Scholar
• Murdin A. D., Doel T. R. Synthetic peptide vaccines against foot-and-mouth disease. I. Duration of the immune response and priming in guinea pigs, rabbits and mice. J. Biol. Stand. 1987; 15: 39
   PubMedGoogle Scholar
• Murdin A. D., Doel T. R. Synthetic peptide vaccines against foot-and-mouth disease. II. Comparison of the resonse of guinea pigs, rabbits and mice to various formulations. J. Biol. Stand. 1987; 15: 53
   PubMedGoogle Scholar
• Allison A. C., Byars N. E., Waters R. V. Immunologic adjuvants: efficacy and safety considerations. Advances in Carriers and Adjuvants for Veterinary Biologies, R. M. Nervig, P. M. Gough, M. L. Kaeberle, C. A. Whetstone. Iowa State University Press, Ames 1986; 91
   Google Scholar
• Baxt B., Morgan D. O., Robertson B. H., Timpone C. A. Epitopes on foot-and-mouth disease virus outer capsid protein VP1 involved in neutralization and cell attachment. J. Virol. 1984; 51: 298
   PubMed Web of Science ®Google Scholar
• McCullough K. C., Smale C. J., Carpenter W. C., Crowther J. R., Brocchi E. Conformational alteration in foot-and-mouth disease virion capsid structure after complexing with monospecific antibody. Immunology 1987; 60: 75
   PubMed Web of Science ®Google Scholar
• Pay T. W. F., Hingley P. J. Correlation of 140S antigen dose with the serum neutralizing antibody response and the level of protection induced in cattle by foot-and-mouth disease vaccines. Vaccine 1987; 5: 60
   PubMed Web of Science ®Google Scholar
• Vakharia V. N., Devaney M. A., Moore D. M., Dunn J. J., Grubman M. J. Proteolytic processing of foot-and-mouth disease virus polyprotein expressed in a cell-free system from clone-derived transcripts. J. Virol. 1987; 61: 3199
   PubMed Web of Science ®Google Scholar
• Rweyemamu M. M., Terry G., Pay T. W. F. Stability and immunogenicity of empty particles of foot-and-mouth disease virus. Arch. Virol. 1979; 59: 69
   PubMed Web of Science ®Google Scholar
• Grubman M. J., Morgan D. O., Kendall J., Baxt B. Capsid intermediates assembled in a foot-and-mouth disease virus genome RNA-programmed cell-free translation system and in infected cells. J. Virol. 1985; 56: 120
   PubMed Web of Science ®Google Scholar
• Ludwig H. Bovine herpesviruses. The Herpesviruses, B. Roizman. Plenum Press, New York 1983; Vol. 2: 135
   Google Scholar
• Schipper I. A., Kelling C. L. Evaluation of inactivated infectious bovine rhinotracheitis vaccines. Can. J. Comp. Med. 1975; 39: 402
   PubMedGoogle Scholar
• Frerichs G. N., Woods S. B., Lucas M. H., Sands J. J. Safety and efficacy of live and inactivated infectious bovine rhinotracheitis vaccines. Vet. Rec. 1982; 111: 116
   PubMed Web of Science ®Google Scholar
• Whetstone C. A., Wheeler J. G., Reed D. E. Investigation of possible vaccine-induced epizootics of infectious bovine rhinotracheitis, using restriction endonuclease analysis of viral DNA. Am. J. Vet. Res. 1986; 47: 1789
   PubMed Web of Science ®Google Scholar
• Straub O. C. Allergische Sofort- und Spatreaktionen bei IBR-IPV-immunen Rinder. Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. Orig. 1970; 214: 483
   Google Scholar
• Crandell R. Feline viral rhinotracheitis (FVR). Advances in Veterinary Science and Comparative Medicine, C. A. Brandly, E. L. Jungherr. Academic Press, New York 1973; Vol. 17: 201
   Google Scholar
• Gustafson D. P. Pseudorabies. Diseases of Swine5th Ed., A. D. Leman, R. D. Glock, W. L. Mengeling, R. H. C. Penny, E. Scholl, B. Straw. Iowa State University Press, Ames 1981; 209
   Google Scholar
• Rouse B. T., Lopez C. Strategies for immune intervention against herpes simplex virus. Immunobiology of Herpes Simplex Virus Infection, B. T. Rouse, C. Lopez. CRC Press, Boca Raton, Ha. 1984; 145
   Google Scholar
• Buchman T. G., Roizman B., Nahmias A. J. Demonstration of exogenous genital reinfection with herpes simplex virus type 2 by restriction endonuclease Finger printing of viral DNA. J. Infect. Dis. 1979; 140: 295
   PubMed Web of Science ®Google Scholar
• Kit S., Trkula D., Qavi H., Dreesman G., Kennedy R. C., Adler-Storthz K., Kaufman R., Adam E. Sequential genital infections by herpes simplex viruses type 1 and type 2: restriction nuclease analyses of viruses from recurrent infections. Sex. Transm. Dis. 1983; 10: 67
   PubMed Web of Science ®Google Scholar
• Johnson D. C., Wittels M., Spear P. G. Binding to cells of virosomes containing herpes simplex virus type 1 glycoproteins and evidence for fusion. J. Virol. 1984; 52: 238
   PubMed Web of Science ®Google Scholar
• Sarmiento M., Haffey M., Spear P. G. Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7 (B2) in virion infectivity. J. Virol 1979; 29: 1149
   PubMed Web of Science ®Google Scholar
• Fuller A. O., Spear P. G. Specificities of monoclonal and polyclonal antibodies that inhibit adsorption of herpes-simplex virus to cells and lack of inhibition by potent neutralizing antibodies. J. Virol. 1985; 55: 475
   PubMed Web of Science ®Google Scholar
• Nobel A. G., Lee G. T.-Y., Spear P. G. Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type I. Virology. 1983; 129: 218
   PubMed Web of Science ®Google Scholar
• Kumel G., Kaerner H. C., Levine M., Schroder C. H., Glorioso J. C. Passive immune protection by herpes simplex virus-specific monoclonal antibodies and monoclonal antibody-resistant mutants altered in pathogenicity. J. Virol. 1985; 56: 930
   PubMed Web of Science ®Google Scholar
• Balachandran N., Bacchetti S., Rawls W. E. Protection against lethal challenge of BALB/c mice by passive transfer of monoclonal antibodies to five glycoproteins of herpes simplex virus type 2. Infect. Immun. 1982; 37: 1132
   PubMed Web of Science ®Google Scholar
• Paoletti E., Lipinskas R. B., Samsonoff C., Mercer S., Panicali D. Construction of live vaccines using genetically engineered poxviruses: biological activity of vaccinia virus recombinants expressing the hepatis B virus surface antigen and the herpes simplex virus glycoprotein D. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 193
   PubMed Web of Science ®Google Scholar
• Collins J. K., Butcher A. C., Riegel C. A., McGrane V., Blair C. D., Teramoto Y. A., Winston S. Neutralizing determinants defined by monoclonal antibodies on polypeptides specified by bovine herpes virus 1. J. Virol. 1984; 52: 403
   PubMed Web of Science ®Google Scholar
• Van Drunen Littel-Van Den Hurk S. J., Van Hurk Den J. V., Gilchrist J. E., Misra V., Babiuk L. A. Interactions of monoclonal antibodies and bovine herpes virus type 1 (BHV-1) glycoproteins: characterization of their biochemical and immunological properties. Virology 1984; 135: 466
   PubMed Web of Science ®Google Scholar
• Marshall R. L., Rodriguez L. L., Letchworth G. J. Characterization of envelope proteins of infectious bovine rhinotracheitis virus (bovine herpesvirus 1) by biochemical and immunological methods. J. Virol. 1986; 57: 745
   PubMed Web of Science ®Google Scholar
• Van Drunen Littel-Van Den Hurk S., Babiuk L. A. Synthesis and processing of bovine herpesvirus 1 glycoproteins. J. Virol. 1986; 59: 401
   PubMed Web of Science ®Google Scholar
• Lawrence W. C., D'Urso R. C., Kundel C. A., Whitbeck J. C., Bello L. J. Map location of the gene for a 130,000-dalton glycoprotein of bovine herpesvirus 1. J. Virol. 1986; 60: 405
   PubMed Web of Science ®Google Scholar
• Trudel M., Seguin C., Nadon F., Boulay G., Trepanier P., Lussier G. Hemagglutination inhibition and virus neutralizing response of rabbits inoculated with bovine herpesvirus 1 subunit vaccine. Vet. Microbiol. 1987; 13: 107
   PubMed Web of Science ®Google Scholar
• Lupton H. W., Reed D. E. Evaluation of experimental subunit vaccines for infectious bovine rhinotracheitis. Am. J. Vet. Res. 1980; 41: 383
   PubMed Web of Science ®Google Scholar
• Kit S., Kit M., McConnell S. Intramuscular and intravaginal vaccination of pregnant cows with thymidine kinase-negative, temperature-resistant infectious bovine rhinotracheitis virus (bovine herpes virus 1). Vaccine 1986; 4: 55
   PubMed Web of Science ®Google Scholar
• Kit S. Genetic engineering of novel animal virus vaccines. Proc. 90th Annu. Meet. U.S., Animal Health Association. Carter Printing, Richmond, Va. 1986; 105
   Google Scholar
• Hampl H., Ben-Porat T., Ehrlicher L., Habermehl K. O., Kaplan A. S. Characterization of the envelope protein of pseudorabies virus. J. Virol. 1984; 52: 583
   PubMed Web of Science ®Google Scholar
• Wathen M. W., Wathen L. M. K. Isolation, characterization, and physical mapping of a pseudorabies virus mutant containing antigenically altered gp 50. J. Virol. 1984; 51: 57
   PubMed Web of Science ®Google Scholar
• Rea T. J., Timmins J. G., Long G. W., Post L. E. Mapping and sequence of the gene for the pseudorabies virus glycoprotein which accumulates in the medium of infected cells. J. Virol. 1985; 54: 21
   PubMed Web of Science ®Google Scholar
• Mettenleiter T. C., Lukacs N., Rziha H.-J. Mapping of the structural gene of pseudorabies virus glycoprotein A and identification of two non-glycosylated precursor polypeptides. J. Virol. 1985; 53: 52
   PubMed Web of Science ®Google Scholar
• Petrovskis E. A., Timmins J. G., Gierman T. M., Post L. E. Deletions in vaccine strains of pseudorabies virus and their effect on synthesis of glycoprotein gp 63. J. Virol. 1986; 60: 1166
   PubMed Web of Science ®Google Scholar
• Tenser R. B., Ressel S., Fralish F., Jones J. The role of pseudorabies virus thymidine kinase expression in trigeminal ganglion infection. J. Gen. Virol. 1983; 64: 1369
   PubMed Web of Science ®Google Scholar
• Kit S., Kit M., Pirtle E. C. Attenuated properties of thymidine kinease negative deletion mutant of pseudorabies virus. Am. J. Vet. Res. 1985; 46: 1359
   PubMed Web of Science ®Google Scholar
• Wathen M. W., Wathen L. M. K. Characterization and mapping of a nonessential pseudorabies virus glycoprotein. J. Virol. 1986; 58: 173
   PubMed Web of Science ®Google Scholar
• Thomsen D. R., Marchioli C. C., Yancey R. J., Jr., Post L. E. Replication and virulence of pseudorabies virus mutants lacking glycoprotein X. J. Virol. 1987; 61: 229
   PubMed Web of Science ®Google Scholar
• Robbins A. K., Watson R. J., Whealy M. E., Hays W. W., Enquist L. W. Characterization of a pseudorabies virus glycoprotein gene with homology to herpes simplex virus type 1 and 2 glycoprotein C. J. Virol. 1986; 58: 339
   PubMed Web of Science ®Google Scholar
• Sun M. News and comment: USDA suspends license for engineered vaccine. Science 1986; 232: 446
   PubMed Web of Science ®Google Scholar
• Kit S., Kit M., Lawhorn B., McConnell S. Immunization of pregnant pigs in a quarantined swine herd with a thymidine kinase deletion mutant of pseudorabies virus. High Tech Route to Virus Vaccines, G. R. Dreesman, J. G. Bronson, R. C. Kennedy. American Society for Microbiology, Washington, D.C. 1985; 82
   Google Scholar
• Palca J. News: violation of rules alleged. Nature (London) 1986; 321: 190
   PubMed Web of Science ®Google Scholar
• Kit S., Sheppard M., Ichimura H., Kit M. Second-generation pseudorabies virus vaccine with deletions in thymidine kinase and glycoprotein genes. Am. J. Vet. Res. 1987; 48: 780
   PubMed Web of Science ®Google Scholar
• Committee on Pseudorabies. Proc. 90th Annu. Meet. U.S. Animal Health Association. Carter Printing, Richmond, Va. 1986; 334, Report.
   Google Scholar
• Quint W., Gieikens A., Vanoirschot J., Berns A., Cuypers H. T. Construction and characterization of deletion mutants of pseudorabies virus: a new generation of “live” vaccines. J. Gen. Virol. 1987; 68: 523
   PubMed Web of Science ®Google Scholar
• Rota P. A., Maes R. K., Ruyechan W. T. Physical characterization of the genome of feline herpes virus-1. Virology 1986; 154: 168
   PubMed Web of Science ®Google Scholar
• Siegl G. Biology and pathogenicity of autonomous parvoviruses. The Parvoviruses, K. I. Bems. Plenum Press, New York 1984; 297
   Google Scholar
• Hauswirth W. W. Autonomous parvovirus DNA structure and replication. The Parvoviruses, K. I. Bems. Plenum Press, New York 1984; 129
   Google Scholar
• Parrish C. R., Carmichael L. E. Antigenic structure and variation of canine parvovirus type-2, feline panleukopenia virus, and mink enteritis virus. Virology 1983; 129: 401
   PubMed Web of Science ®Google Scholar
• Molitor T. W., Joo H. S., Collett M. S. Porcine parvoviruses: virus purification and structural and antigenic properties of virion polypeptides. J. Virol. 1983; 45: 842
   PubMed Web of Science ®Google Scholar
• Lederman M., Bates R. C., Stout E. R. In vitro and in vivo studies of bovine parvovirus proteins. J. Virol. 1983; 48: 10
   PubMed Web of Science ®Google Scholar
• Lederman M., Patton J. T., Stout E. R., Bates R. C. Virally coded non-capsid protein associated with bovine parvovirus infection. J. Virol. 1984; 49: 315
   PubMed Web of Science ®Google Scholar
• Chen K. C., Shull B. C., Moses E. A., Lederman M., Stout E. R., Bates R. C. Complete nucleotide sequence and genome organization of bovine parvovirus. J. Virol. 1986; 60: 1085
   PubMed Web of Science ®Google Scholar
• Lederman M., Chen K. C., Stout E. R., Bates R. C. Possible sequences for nuclear accumulation of parvoviral proteins. Cell Biol. Int. Rep. 1986; 10: 383
   PubMedGoogle Scholar
• Simpson R. W., McGinty L., Simon L., Smith C. A., Godzesky C. W., Body R. J. Association of parvoviruses with rheumatoid arthritis of humans. Science 1984; 223: 1425
   PubMed Web of Science ®Google Scholar
• Carlson J., Rushlow K., Maxwell I., Maxwell F., Winston S., Hahn W. Cloning and sequence of DNA encoding structural proteins of the autonomous parvovirus feline panleukopenia virus. J. Virol. 1985; 55: 574
   PubMed Web of Science ®Google Scholar
• Carlson J. O., Lynde-Mass M. K., Zheng-Da S. A nonstructural protein of feline panleukope-niavirus: expression in Escherichia coli and detection of multiple forms in infected cells. J. Virol. 1987; 61: 621
   PubMed Web of Science ®Google Scholar
• Molitor T., Joo H. S., Collett M. C. Indentification and characterization of a porcine parvovirus non-structural polypeptide. J. Virol. 1985; 55: 554
   PubMed Web of Science ®Google Scholar
• Cotmore S. F., Sturzenbecker L. J., Tattersall P. The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid proteins. Virology 1983; 129: 333
   PubMed Web of Science ®Google Scholar
• Malmquist W. A., Hay D. Hemadsorption and cytopathic effect produced by African swine fever virus in swine bone marrow and buffy coat cultures. Am. J. Vet. Res. 1960; 21: 104
   PubMed Web of Science ®Google Scholar
• Hess W. R. African swine fever virus. Virol. Monogr. 1971; 9: 1
   PubMedGoogle Scholar
• Coggins L. African swine fever virus, pathogenesis. Prog. Med. Virol. 1974; 18: 48
   PubMedGoogle Scholar
• DeTray D. E. Persistence of viremia and immunity in African swine fever. Am. J. Vet. Res. 1957; 18: 811
   PubMed Web of Science ®Google Scholar
• Forman A. J., Wardley R. C., Wilkinson P. J. The immunological response of pigs and guinea pigs to antigens of African swine fever virus. Arch. Virol. 1982; 74: 91
   PubMed Web of Science ®Google Scholar
• Norley S. G., Wardley R. C. Complement-mediated lysis of African swine fever virus-infected cells. Immunology 1982; 46: 75
   PubMed Web of Science ®Google Scholar
• Hess W. R. African swine fever: a reassessment. Adv. Vet. Sci. Comp. Med. 1981; 25: 39
   PubMedGoogle Scholar
• Wiktor T. J., Gyorgie E., Schlemberger H. D., Sokol F., Koprowski H. Antigenic properties of rabies virus components. J. Immunol. 1973; 110: 269
   PubMed Web of Science ®Google Scholar
• Yelverton E., Norton S., Obijeski J. F., Goeddel D. V. Rabies virus glycoprotein analogs: biosynthesis in Escherichia coli. Science 1983; 219: 614
   PubMed Web of Science ®Google Scholar
• Kieny M. P., Lathe R., Drillein R., Spehner D., Skory S., Schmitt D., Wiktor T., Koprowski H., Lecocq J. P. Expression of rabies virus glycoprotein from a recombinant vaccinia virus. Nature (London) 1984; 312: 163
   PubMed Web of Science ®Google Scholar
• Wiktor T. J., MacFarlan R. I., Reagan K. J., Dietzschold B., Curtis P. J., Wunner W. H., Kiedhy M.-P., Lathe R., Lecocq J.-P., Mackett M., Moss B., Koprowski H. Protection from rabies by a vaccinia recombinant containing the rabies virus glycoprotein gene. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 7194
   PubMed Web of Science ®Google Scholar
• Celis E., Wiktor T. J., Dietzschold B., Koprowski H. Amplification of rabies virus-induced stimulation of human T-cell lines and clones by antigen-specific antibodies. J. Virol. 1985; 56: 426
   PubMed Web of Science ®Google Scholar
• Kelly J. M., Emerson S. U., Wagner R. R. The glycoprotein of vesicular stomatitis virus is the antigen that gives rise to and reacts with neutralizing antibody. J. Virol. 1972; 10: 1231
   PubMedGoogle Scholar
• Rose J. K., Gallione C. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. J. Virol. 1981; 39: 519
   PubMed Web of Science ®Google Scholar
• Gallione C. J., Greene J. R., Iverson L. E., Rose J. K. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus N and NS proteins. J. Virol. 1981; 39: 529
   PubMed Web of Science ®Google Scholar
• Rose J. K., Schafferman A. Conditional expression of the vesicular stomatitis virus glycoprotein gene in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 6670
   PubMed Web of Science ®Google Scholar
• Rose J. K., Bergmann J. E. Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eukaryotic cells. Cell 1982; 30: 753
   PubMed Web of Science ®Google Scholar
• Sprague J., Condra J. H., Arntheiter H., Lazzarini R. A. Expression of a recombinant DNA gene coding for the vesicular stomatitis virus nucleocapsid protein. J. Virol. 1983; 45: 773
   PubMed Web of Science ®Google Scholar
• Mackett M., Yilma T., Rose J. K., Moss B. Vaccinia virus recombinants: expression of VSV genes and protective immunization of mice and cattle. Science 1985; 227: 433
   PubMed Web of Science ®Google Scholar
• Garwes D. J., Pocock D. H. The polypeptide structure of transmissible gastroenteritis virus. J. Gen. Virol. 1975; 29: 25
   PubMed Web of Science ®Google Scholar
• Crouch C. F. Vaccination against enteric rota and coronaviruses in cattle and pigs: enhancement of lactogenic immunity. Vaccine 1985; 3: 284
   PubMed Web of Science ®Google Scholar
• Jacobs L., VanderZeijst B. A. M., Horzinek M. C. Characterization and translation of transmissible gastroenteritis virus mRNAs. J. Virol. 1986; 57: 1010
   PubMed Web of Science ®Google Scholar
• Kapke P. A., Brian D. Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene. Virology 1986; 151: 41
   PubMed Web of Science ®Google Scholar
• Jimenez G., Correa I., Melgosa M. P., Bullido M. J., Enjuanes L. Critical epitopes in transmissible gastroenteritis virus neutralization. J. Virol. 1986; 60: 131
   PubMed Web of Science ®Google Scholar
• Lapps W., Hogue B. G., Brian D. A. Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes. Virology 1987; 157: 47
   PubMed Web of Science ®Google Scholar
• King B., Brian D. A. Bovine coronavirus structural proteins. J. Virol. 1982; 42: 700
   PubMed Web of Science ®Google Scholar
• Bohl E. H., Theil K. W., Saif L. J. Isolation and serotyping of porcine rotaviruses and antigenic comparison with other rotaviruses. J. Clin. Microbiol. 1984; 19: 105
   PubMed Web of Science ®Google Scholar
• Woode G. N., Kelso N. E., Simpson T. F., Gaul S. K., Evans L. E., Babiuk L. Antigenic relationships among some bovine rotaviruses: serum neutralization and cross protection in gnotobiotic calves. J. Clin. Microbiol. 1983; 18: 358
   PubMed Web of Science ®Google Scholar
• Matsuno L., Inouye L. Purification of an outer capsid glycoprotein of neonatal calf diarrhea virus and preparation of its antisera. Infect. Immun. 1983; 39: 155
   PubMed Web of Science ®Google Scholar
• Sahara M., Gilchrist J. E., Hudson G. R., Babiuk L. A. Preliminary characterization of an epitope involved in neutralization and cell attachment that is located on the major bovine rotavirus glycoprotein. J. Virol. 1985; 53: 58
   PubMed Web of Science ®Google Scholar
• Gillespie J. H., Timoney J. F. Bluetongue. Hagan and Bruner's Infectious Diseases of Domestic Animals7th Ed. Comstock Publishing Associates, Cornell University, Ithaca, N.Y. 1981; 653
   Google Scholar
• Gorman B. M., Taylor J., Walker P. J. Orbiviruses. The Reoviridae, W. K. Joklik. Plenum Press, New York 1983; 287
   Google Scholar
• Huismans H., Van Der Walt N. T., Cleote M., Erasmus B. J. Isolation of a capsid protein of bluetongue virus that induces a protective immune response in sheep. Virology 1987; 157: 172
   PubMed Web of Science ®Google Scholar
• Inumaru S., Roy P. Production and characterization of the neutralization antigen VP2 of bluetongue virus serotype 10 using a baculovirus expression vector. Virology 1987; 157: 472
   PubMed Web of Science ®Google Scholar
• Taylor W. P. The distribution and epidemiology of peste des petits ruminants. Prev. Vet. Med. 1984; 2: 157
   Web of Science ®Google Scholar
• Schultz R. D., Scott F. W. Canine and feline immunization. Vet. Clin. North Am. 1978; 8: 755
   PubMedGoogle Scholar
• Ishii H., Yoshikawa Y., Yamanouchi K. Adaption of the lapinized rinderpest virus to in vitro growth and attenuation of its virulence in rabbits. J. Gen. Virol. 1986; 67: 275
   PubMed Web of Science ®Google Scholar
• Rozenblatt S., Gesang C., Lavie V., Neumann F. S. Cloning and characterization of DNA complementary to the measles virus mRNA encoding hemagglutinin and matrix protein. J. Virol. 1982; 42: 790
   PubMed Web of Science ®Google Scholar
• Rozenblatt S., Eizenberg O., Englund G., Bellini W. J. Cloning and characterization of DNA complementary to the canine distemper virus mRNA encoding matrix, phosphoprotein, and nucleocapsid protein. J. Virol. 1985; 53: 691
   PubMed Web of Science ®Google Scholar
• Russell S. E. H., Clarke D. K., Hoey E. M., Rima B. K., Martin S. J. cDNA cloning of the messenger RNAs of five genes of canine distemper virus. J. Gen. Virol. 1985; 66: 433
   PubMed Web of Science ®Google Scholar
• Rozenblatt S., Eizenberg O., Ben-Levy R., Lavie V., Bellini W. J. Sequence homology within the morbilliviruses. J. Virol. 1985; 53: 684
   PubMed Web of Science ®Google Scholar
• Bellini W. J., Englund G., Richardson C. D., Rozenblatt S., Lazzarini R. A. Matrix genes of measles virus and canine distemper virus: cloning, nucleotide sequences, and deduced amino acid sequences. J. Virol. 1986; 58: 408
   PubMed Web of Science ®Google Scholar
• Norrby E., Sheshberadaran H., McCullough K. C., Carpenter W. C., Orvell C. Is rinderpest virus the archevirus of the Morbillivirus genus?. Intervirology 1985; 23: 228
   PubMed Web of Science ®Google Scholar
• Merz D. C., Scheid A., Choppin P. W. The importance of antibodies to the fusion glycoprotein (F) of paramyxoviruses in the prevention of spread of infection. J. Exp. Med. 1980; 151: 275
   PubMed Web of Science ®Google Scholar
• Norrby E., Utter G., Orvell C., Appel M. J. G. Protection against canine distemper virus in dogs after immunization with isolated fusion protein. J. Virol. 1986; 58: 536
   PubMed Web of Science ®Google Scholar
• Barrett T., Underwood B. Comparison of messenger RNAs induced in cells infected with each member of the morbillivirus group. Virology 1985; 145: 195
   PubMed Web of Science ®Google Scholar
• Meegan J. M., Hoogstraal H., Moussa M. I. An epizootic of Rift Valley fever in Egypt in 1977. Vet. Rec. 1979; 105: 124
   PubMed Web of Science ®Google Scholar
• Parker M. D., Smith J. F., Dalrymple J. M. Rift Valley fever virus intracellular RNA: a functional analysis. Segmented Negative Strand Viruses, R. W. Compans, D. H. L. Bishop. Academic Press, New York 1984; 21
   Google Scholar
• Collett M. S., Purchio A. F., Keegan K., Frazier S., Hays W., Anderson D. K., Parker M. D., Schmaljohn C., Schmidt A., Dalrymple J. M. Complete nucleotide sequence of the M RNA segment of Rift Valley fever virus. Virology 1985; 144: 228
   PubMed Web of Science ®Google Scholar
• Keegan K., Collett M. S. Use of bacterial expression cloning to define the amino acid sequences of antigenic determinants on the G2 glycoprotein of Rift Valley fever virus. J. Virol. 1986; 58: 263
   PubMed Web of Science ®Google Scholar
• Oroszlan S., Gilden R. V. Antigenic structure of retroviruses. Immunochemistry of Viruses, M. H. V. VanRegenmortel, A. R. Neurath. Elsevier, New York 1985; 447
   Google Scholar
• Hunsmann G., Moennig V., Pister L., Seifert E., Schafer W. Properties of mouse leukemia viruses. VIII. The major viral glycoprotein of Friend leukemia virus. Seroimmunological, interfering and hemagglutinating capacities. Virology 1974; 62: 307
   PubMed Web of Science ®Google Scholar
• De Noronha F., Schafer W., Essex M., Bolognese D. P. Influence of antisera to oncornavirus glycoprotein (gp 71) on infections of cats with feline leukemia virus. Virology 1978; 85: 617
   PubMed Web of Science ®Google Scholar
• Cianciolo G. J., Matthews T. J., Bolognese D. P., Synderman R. Macrophage accumulation in mice is inhibited by low molecular weight products from murine leukemia viruses. J. Immunol. 1980; 124: 2900
   PubMed Web of Science ®Google Scholar
• Rein A. Interference grouping of murine leukemia viruses: a distinct receptor for the MCF-recombinant viruses on mouse cells. Virology 1982; 120: 251
   PubMed Web of Science ®Google Scholar
• Bassin R. H., Ruscetti S., AH I., Haapala D. K., Rein A. Normal DBA/2 mouse cells synthesize a glycoprotein which interferes with MCF virus infection. Virology 1982; 123: 139
   PubMed Web of Science ®Google Scholar
• Legrain P., Goud B., Buttin G. Increase of retroviral infection in vitro by the binding of anti-retroviral antibodies. J. Virol. 1986; 60: 1141
   PubMed Web of Science ®Google Scholar
• Stewart M. A., Warnock M., Wheeler A., Wilkie N., Mullins J. I., Onions D. E., Neil J. C. Nucleotide sequences of a feline leukemia virus subgroup A envelope gene and long terminal repeat and evidence for the recombinational origin of subgroup B viruses. J. Virol. 1986; 58: 825
   PubMed Web of Science ®Google Scholar
• Elder J. H., Mullins J. I. Nucleotide sequence of the envelope gene of Gardner-Amstein feline leukemia virus B reveals unique sequence homologies with a murine mink cell focus-forming virus. J. Virol. 1983; 46: 871
   PubMed Web of Science ®Google Scholar
• Nunberg J. H., Williams M. E., Innis M. A. Nucleotide sequences of the envelope genes of two isolates of feline leukemia virus subgroup B. J. Virol. 1984; 49: 629
   PubMed Web of Science ®Google Scholar
• Wunsch M., Schulz A. S., Koch W., Friederich R., Hunsmann G. Sequence analysis of Gardner-Amstein feline leukemia virus envelope gene reveals common structural properties of mammalian retroviral gene envelopes. EMBO J. 1984; 2: 2239
   Web of Science ®Google Scholar
• Okabe H., Twiddy E., Gilden R. V., Masakazu H., Hoover E. A., Olsen R. G. FeLV-related sequences in DNA from a FeLV-free cat colony. Virology 1976; 69: 798
   PubMed Web of Science ®Google Scholar
• Soe L. H., Devi B. G., Mullins J. I., Roy-Burman P. Molecular cloning and characterization of endogenous feline leukemia virus sequences from a cat genomic library. J. Virol. 1983; 46: 829
   PubMed Web of Science ®Google Scholar
• Elder J. H., McGee J. S., Munson M., Houghten R. A., Kloetzer W., Bittle J. L., Grant C. K. Localization of neutralizing regions of the envelope gene of feline leukemia virus by using anti-synthetic peptide antibodies. J. Virol. 1987; 61: 8
   PubMed Web of Science ®Google Scholar
• Nunberg J. H., Rodgers G., Gilbert J. H., Snead R. M. Method to map antigenic determinants recognized by monoclonal antibodies: localization of a determinant of virus neutralization on the feline leukemia virus envelope protein gp 70. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 3675
   PubMed Web of Science ®Google Scholar
• Martin S., Moss B., Berman P. W., Laskey L. A., Rouse B. T. Mechanisms of antiviral immunity induced by a vaccinia virus recombinant expressing herpes simplex virus type 1 glycoprotein D: cytotoxic T cells. J. Virol. 1987; 61: 726
   PubMed Web of Science ®Google Scholar
• Yewdell J. W., Bennick J. R., Mackett M., Lefrancois L., Lyles D. S., Moss B. Recognition of cloned vesicular stomatitis virus internal and external gene products by cytotoxic T lymphocytes. J. Exp. Med. 1986; 163: 1529
   PubMed Web of Science ®Google Scholar
• Puddington L., Bevan M. J., Rose J. K., Lefrancois L. N protein is the predominant antigen recognized by vesicular stomatitis virus-specific cytotoxic T cells. J. Virol. 1986; 60: 708
   PubMed Web of Science ®Google Scholar
• Gooding L. R. Specificities of killing by cytotoxic lymphocytes generated in vivo and in vitro to syngeneic SV40 transformed cells. J. Immunol. 1977; 118: 920
   PubMed Web of Science ®Google Scholar
• Bennick J. R., Yewdell J. W., Gerhard W. A viral polymerase involved in recognition of influenza-infected cell by a cytotoxic T cell clone. Nature (London) 1982; 296: 75
   PubMed Web of Science ®Google Scholar
• Townsend A. R. M., Skehel J. J. Influenza A specific cytotoxic T-cell clones that do not recognize viral glycoproteins. Nature (London) 1982; 300: 655
   PubMed Web of Science ®Google Scholar
• Braciale T. J., Braciale V. L., Henkle T. J., Sam brook J., Gething M. J. Cytotoxic T lymphocytes recognition of the influenza hemagglutinin gene product expressed by DNA-mediated gene transfer. J. Exp. Med. 1984; 159: 341
   PubMedGoogle Scholar
• Bennick J. R., Yewdell J. W., Smith G. L., Moller C., Moss B. Recombinant vaccinia virus primes and stimulates influenza haemagglutinin-specific cytotoxic T cells. Nature (London) 1984; 311: 578
   PubMed Web of Science ®Google Scholar
• Yewdell J. W., Bennick J. R., Smith G. L., Moss B. Influenza A virus nucleoprotein is a major target antigen for cross-reactive anti-influenza A virus cytoxic T lymphocytes. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 1785
   PubMed Web of Science ®Google Scholar
• Bennick J. R., Yewdell J. W., Smith G. L., Moss B. Anti-influenza virus cytotoxic T lymphocytes recognize the three viral polymerases and a nonstructural protein: responsiveness to individual viral antigens is major histocompatibility complex controlled. J. Virol. 1987; 61: 1098
   PubMed Web of Science ®Google Scholar
• Pala P., Askonas B. A. Low responder MHC alleles for Tc recognition of influenza nucleoprotein. Immunogenetics 1986; 23: 379
   PubMed Web of Science ®Google Scholar
• Lukacher A. E., Morrison L. A., Braciale V. L., Malissen B., Braciale T. J. Expression of specific cytolytic activity by H-21 region-restricted, influenza virus-specific T lyphocyte clones. J. Exp. Med. 1985; 162: 171
   PubMed Web of Science ®Google Scholar
• Townsend A. R. M., Gotch F. M., Davey J. Cytotoxic T cells recognize fragments of the influenza nucleoprotein. Cell 1985; 42: 457
   PubMed Web of Science ®Google Scholar
• Townsend A. R. M., Rothbard J., Gotch F. M., Bahadur G., Wraith D., McMichael A. J. The epitope of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides. Cell 1986; 44: 959
   PubMed Web of Science ®Google Scholar
• Moore D., Vakharia V., personal communication
   Google Scholar
• Baxt B., personal communication
   Google Scholar