Augmentation of human immunodeficiency virus type 1 neutralizing antibody by priming with gp160 recombinant vaccinia and boosting with rgp160 in vaccinia-naive adults. The NIAID AIDS Vaccine Clinical Trials Network. 1993

B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
Dept. of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232.

Twelve vaccinia-naive volunteers were inoculated with recombinant vaccinia virus expressing the human immunodeficiency virus type 1 (HIV-1) strain IIIB (HIV-1IIIB) envelope glycoprotein gp160 and subsequently immunized with 640 micrograms of recombinant (r) gp160 protein produced in baculovirus. After booster immunization with rgp160, the sera of all vaccinees showed strong antibody responses detected by Western blot and ELISA; 8 had neutralizing activity and 5 had fusion inhibition activity against the homologous strain; 5 blocked binding of CD4 cells to gp120. Cross-reactive neutralization of HIV-1MN was detected in 3 of 8 sera that neutralized HIV-1IIIB. The combination of live recombinant vaccinia followed by subunit booster immunization was more immunogenic than either product alone and represents a promising approach for HIV-1 immunoprophylaxis. Further definition of recombinant vaccinia safety and augmentation of immune responses to geographically prevalent HIV-1 strains will be necessary before expanding clinical trials to high-risk groups.

UI MeSH Term Description Entries
D007117 Immunization, Secondary Any immunization following a primary immunization and involving exposure to the same or a closely related antigen. Immunization, Booster,Revaccination,Secondary Immunization,Booster Immunization,Booster Immunizations,Immunizations, Booster,Immunizations, Secondary,Revaccinations,Secondary Immunizations
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009500 Neutralization Tests The measurement of infection-blocking titer of ANTISERA by testing a series of dilutions for a given virus-antiserum interaction end-point, which is generally the dilution at which tissue cultures inoculated with the serum-virus mixtures demonstrate cytopathology (CPE) or the dilution at which 50% of test animals injected with serum-virus mixtures show infectivity (ID50) or die (LD50). Neutralization Test,Test, Neutralization,Tests, Neutralization
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011498 Protein Precursors Precursors, Protein
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001667 Binding, Competitive The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements. Competitive Binding

Related Publications

B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
August 1992, The Journal of infectious diseases,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
January 1992, Vaccine,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
January 1991, Annals of internal medicine,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
November 1992, Journal of clinical immunology,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
November 1990, AIDS research and human retroviruses,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
August 1994, Vaccine,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
February 1995, Vaccine,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
November 1996, Clinical and diagnostic laboratory immunology,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
September 1995, Vaccine,
B S Graham, and T J Matthews, and R B Belshe, and M L Clements, and R Dolin, and P F Wright, and G J Gorse, and D H Schwartz, and M C Keefer, and D P Bolognesi
October 1992, Journal of clinical microbiology,
Copied contents to your clipboard!