Protective Immune Responses Induced by Secretion of a Chimeric Soluble Protein from a Recombinant Mycobacterium bovis Bacillus Calmette-Guerin Vector Candidate Vaccine for Human Immunodeficiency Virus Type 1 in Small Animals
A recombinant Mycobacterium bovis bacillus Calmette-Guérin (BCG) vector-based vaccine that secretes the V3 principal neutralizing epitope of human immunodeficiency virus (HIV) could induce immune response to the epitope and prevent the viral infection. By using the Japanese consensus sequence of HI...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-11, Vol.92 (23), p.10693-10697 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Honda, Mitsuo Matsuo, Kazuhiro Nakasone, Tadashi Okamoto, Yukari Yoshizaki, Hitomi Kitamura, Katsuhiko sugiura, wataru Watanabe, Kuhomi fukushima, Yoshiko Haga, shinji Katsura, Yoshimoto Tasaka, Hiromichi Komuro, Katsutoshi Yamada, Takeshi Asano, Toshihiko Yamazak, akihiro Yamazaki, shudo |
| description | A recombinant Mycobacterium bovis bacillus Calmette-Guérin (BCG) vector-based vaccine that secretes the V3 principal neutralizing epitope of human immunodeficiency virus (HIV) could induce immune response to the epitope and prevent the viral infection. By using the Japanese consensus sequence of HIV-1, we successfully constructed chimeric protein secretion vectors by selecting an appropriate insertion site of a carrier protein and established the principal neutralizing determinant (PND)-peptide secretion system in BCG. The recombinant BCG (rBCG)-inoculated guinea pigs were initially screened by delayed-type hypersensitivity (DTH) skin reactions to the PND peptide, followed by passive transfer of the DTH by the systemic route. Further, immunization of mice with the rBCG resulted in induction of cytotoxic T lymphocytes. The guinea pig immune antisera showed elevated titers to the PND peptide and neutralized HIVMN, and administration of serum IgG from the vaccinated guinea pigs was effective in completely blocking the HIV infection in thymus/liver transplanted severe combined immunodeficiency (SCID)/hu or SCID/PBL mice. In addition, the immune serum IgG was shown to neutralize primary field isolates of HIV that match the neutralizing sequence motif by a peripheral blood mononuclear cell-based virus neutralization assay. The data support the idea that the antigen-secreting rBCG system can be used as a tool for development of HIV vaccines. |
| doi_str_mv | 10.1073/pnas.92.23.10693 |
| format | Article |
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By using the Japanese consensus sequence of HIV-1, we successfully constructed chimeric protein secretion vectors by selecting an appropriate insertion site of a carrier protein and established the principal neutralizing determinant (PND)-peptide secretion system in BCG. The recombinant BCG (rBCG)-inoculated guinea pigs were initially screened by delayed-type hypersensitivity (DTH) skin reactions to the PND peptide, followed by passive transfer of the DTH by the systemic route. Further, immunization of mice with the rBCG resulted in induction of cytotoxic T lymphocytes. The guinea pig immune antisera showed elevated titers to the PND peptide and neutralized HIVMN, and administration of serum IgG from the vaccinated guinea pigs was effective in completely blocking the HIV infection in thymus/liver transplanted severe combined immunodeficiency (SCID)/hu or SCID/PBL mice. In addition, the immune serum IgG was shown to neutralize primary field isolates of HIV that match the neutralizing sequence motif by a peripheral blood mononuclear cell-based virus neutralization assay. The data support the idea that the antigen-secreting rBCG system can be used as a tool for development of HIV vaccines.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.23.10693</identifier><identifier>PMID: 7479867</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>AIDS Vaccines - immunology ; AIDS/HIV ; Amino Acid Sequence ; Animals ; Antibodies ; Antibodies, Viral - blood ; Antigens ; Base Sequence ; DNA ; Enzyme-Linked Immunosorbent Assay ; Genetic Vectors ; Guinea Pigs ; HIV ; HIV 1 ; HIV Envelope Protein gp120 - immunology ; HIV infections ; HIV Infections - prevention & control ; HIV-1 - immunology ; Human immunodeficiency virus ; human immunodeficiency virus 1 ; Humans ; Immunity (Disease) ; Immunization, Passive ; Medical research ; Mice ; Mice, SCID ; Middle Aged ; Molecular Sequence Data ; Mycobacterium bovis ; Mycobacterium bovis - genetics ; Neutralization Tests ; Peptide Fragments - immunology ; Proteins ; Skin Tests ; Spleen cells ; T-Lymphocytes, Cytotoxic ; Tuberculin ; Vaccination ; Vaccines, Synthetic - immunology ; Viral Proteins - metabolism ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-11, Vol.92 (23), p.10693-10697</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 7, 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c591t-230f07db10abcb50a000e1a0a65b55203cabc678c8efbbb091eb0649db726c293</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/23.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2368854$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2368854$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53770,53772,57996,58229</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7479867$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Honda, Mitsuo</creatorcontrib><creatorcontrib>Matsuo, Kazuhiro</creatorcontrib><creatorcontrib>Nakasone, Tadashi</creatorcontrib><creatorcontrib>Okamoto, Yukari</creatorcontrib><creatorcontrib>Yoshizaki, Hitomi</creatorcontrib><creatorcontrib>Kitamura, Katsuhiko</creatorcontrib><creatorcontrib>sugiura, wataru</creatorcontrib><creatorcontrib>Watanabe, Kuhomi</creatorcontrib><creatorcontrib>fukushima, Yoshiko</creatorcontrib><creatorcontrib>Haga, shinji</creatorcontrib><creatorcontrib>Katsura, Yoshimoto</creatorcontrib><creatorcontrib>Tasaka, Hiromichi</creatorcontrib><creatorcontrib>Komuro, Katsutoshi</creatorcontrib><creatorcontrib>Yamada, Takeshi</creatorcontrib><creatorcontrib>Asano, Toshihiko</creatorcontrib><creatorcontrib>Yamazak, akihiro</creatorcontrib><creatorcontrib>Yamazaki, shudo</creatorcontrib><title>Protective Immune Responses Induced by Secretion of a Chimeric Soluble Protein from a Recombinant Mycobacterium bovis Bacillus Calmette-Guerin Vector Candidate Vaccine for Human Immunodeficiency Virus Type 1 in Small Animals</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>A recombinant Mycobacterium bovis bacillus Calmette-Guérin (BCG) vector-based vaccine that secretes the V3 principal neutralizing epitope of human immunodeficiency virus (HIV) could induce immune response to the epitope and prevent the viral infection. By using the Japanese consensus sequence of HIV-1, we successfully constructed chimeric protein secretion vectors by selecting an appropriate insertion site of a carrier protein and established the principal neutralizing determinant (PND)-peptide secretion system in BCG. The recombinant BCG (rBCG)-inoculated guinea pigs were initially screened by delayed-type hypersensitivity (DTH) skin reactions to the PND peptide, followed by passive transfer of the DTH by the systemic route. Further, immunization of mice with the rBCG resulted in induction of cytotoxic T lymphocytes. The guinea pig immune antisera showed elevated titers to the PND peptide and neutralized HIVMN, and administration of serum IgG from the vaccinated guinea pigs was effective in completely blocking the HIV infection in thymus/liver transplanted severe combined immunodeficiency (SCID)/hu or SCID/PBL mice. In addition, the immune serum IgG was shown to neutralize primary field isolates of HIV that match the neutralizing sequence motif by a peripheral blood mononuclear cell-based virus neutralization assay. The data support the idea that the antigen-secreting rBCG system can be used as a tool for development of HIV vaccines.</description><subject>AIDS Vaccines - immunology</subject><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Viral - blood</subject><subject>Antigens</subject><subject>Base Sequence</subject><subject>DNA</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Genetic Vectors</subject><subject>Guinea Pigs</subject><subject>HIV</subject><subject>HIV 1</subject><subject>HIV Envelope Protein gp120 - immunology</subject><subject>HIV infections</subject><subject>HIV Infections - prevention & control</subject><subject>HIV-1 - immunology</subject><subject>Human immunodeficiency virus</subject><subject>human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Immunity (Disease)</subject><subject>Immunization, Passive</subject><subject>Medical research</subject><subject>Mice</subject><subject>Mice, SCID</subject><subject>Middle Aged</subject><subject>Molecular Sequence Data</subject><subject>Mycobacterium bovis</subject><subject>Mycobacterium bovis - genetics</subject><subject>Neutralization Tests</subject><subject>Peptide Fragments - immunology</subject><subject>Proteins</subject><subject>Skin Tests</subject><subject>Spleen cells</subject><subject>T-Lymphocytes, Cytotoxic</subject><subject>Tuberculin</subject><subject>Vaccination</subject><subject>Vaccines, Synthetic - immunology</subject><subject>Viral Proteins - metabolism</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkk9vEzEQxVcIVELhzgGExQFx2eD1_rXEpUTQRioCNSVXy_bOUke7dmp7I_Jt-ShMmhAVDnAaed5vnp5HkyTPMzrNaJ2_W1sZppxNWY7viucPkklGeZZWBacPkwmlrE6bghWPkychrCilvGzoSXJSFzVvqnqS_PzqXQQdzQbIfBhGC-QKwtrZAIHMbTtqaInakgVoD9E4S1xHJJndmAG80WTh-lH1QO5sjCWddwPqV6DdoIyVNpLPW-2U1BH5cSDKbUwgH6Q2fT8GMpP9ADFCej6ibskSsziPbduaVkYgS6m1wVQddi_GQdp9TNdCZ7QBq7dkaTw6XW_XQDKCHotB9j05swZreJo86rDAs0M9Tb59-ng9u0gvv5zPZ2eXqS55FlOW047WrcqoVFqVVOKuIJNUVqUqS0Zzjf2qbnQDnVIKdwyK4pZbVbNKM56fJu_3vutRDdBqsNHLXqw9pvBb4aQRfyrW3IjvbiMKirY4_uYw7t3tCCGKwQQNfS8tuDGIuq4q2hTFf8Gs4g2r6x34-i9w5UZvcQeC0SzPecFzhOge0t6F4KE7Bs6o2F2Y2F2Y4EywXNxdGI68vP_R48DhpFB_e9B3k7_Vew6iG_s-wo-I6Kt_o0i82BOrgGdxRFheNU1Z5L8AQVP0fA</recordid><startdate>19951107</startdate><enddate>19951107</enddate><creator>Honda, Mitsuo</creator><creator>Matsuo, Kazuhiro</creator><creator>Nakasone, Tadashi</creator><creator>Okamoto, Yukari</creator><creator>Yoshizaki, Hitomi</creator><creator>Kitamura, Katsuhiko</creator><creator>sugiura, wataru</creator><creator>Watanabe, Kuhomi</creator><creator>fukushima, Yoshiko</creator><creator>Haga, shinji</creator><creator>Katsura, Yoshimoto</creator><creator>Tasaka, Hiromichi</creator><creator>Komuro, Katsutoshi</creator><creator>Yamada, Takeshi</creator><creator>Asano, Toshihiko</creator><creator>Yamazak, akihiro</creator><creator>Yamazaki, shudo</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7QO</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19951107</creationdate><title>Protective Immune Responses Induced by Secretion of a Chimeric Soluble Protein from a Recombinant Mycobacterium bovis Bacillus Calmette-Guerin Vector Candidate Vaccine for Human Immunodeficiency Virus Type 1 in Small Animals</title><author>Honda, Mitsuo ; Matsuo, Kazuhiro ; Nakasone, Tadashi ; Okamoto, Yukari ; Yoshizaki, Hitomi ; Kitamura, Katsuhiko ; sugiura, wataru ; Watanabe, Kuhomi ; fukushima, Yoshiko ; Haga, shinji ; Katsura, Yoshimoto ; Tasaka, Hiromichi ; Komuro, Katsutoshi ; Yamada, Takeshi ; Asano, Toshihiko ; Yamazak, akihiro ; Yamazaki, shudo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c591t-230f07db10abcb50a000e1a0a65b55203cabc678c8efbbb091eb0649db726c293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>AIDS Vaccines - 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immunology</topic><topic>Viral Proteins - metabolism</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Honda, Mitsuo</creatorcontrib><creatorcontrib>Matsuo, Kazuhiro</creatorcontrib><creatorcontrib>Nakasone, Tadashi</creatorcontrib><creatorcontrib>Okamoto, Yukari</creatorcontrib><creatorcontrib>Yoshizaki, Hitomi</creatorcontrib><creatorcontrib>Kitamura, Katsuhiko</creatorcontrib><creatorcontrib>sugiura, wataru</creatorcontrib><creatorcontrib>Watanabe, Kuhomi</creatorcontrib><creatorcontrib>fukushima, Yoshiko</creatorcontrib><creatorcontrib>Haga, shinji</creatorcontrib><creatorcontrib>Katsura, Yoshimoto</creatorcontrib><creatorcontrib>Tasaka, Hiromichi</creatorcontrib><creatorcontrib>Komuro, Katsutoshi</creatorcontrib><creatorcontrib>Yamada, Takeshi</creatorcontrib><creatorcontrib>Asano, Toshihiko</creatorcontrib><creatorcontrib>Yamazak, akihiro</creatorcontrib><creatorcontrib>Yamazaki, shudo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>MEDLINE - 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PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1995-11-07</date><risdate>1995</risdate><volume>92</volume><issue>23</issue><spage>10693</spage><epage>10697</epage><pages>10693-10697</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A recombinant Mycobacterium bovis bacillus Calmette-Guérin (BCG) vector-based vaccine that secretes the V3 principal neutralizing epitope of human immunodeficiency virus (HIV) could induce immune response to the epitope and prevent the viral infection. By using the Japanese consensus sequence of HIV-1, we successfully constructed chimeric protein secretion vectors by selecting an appropriate insertion site of a carrier protein and established the principal neutralizing determinant (PND)-peptide secretion system in BCG. The recombinant BCG (rBCG)-inoculated guinea pigs were initially screened by delayed-type hypersensitivity (DTH) skin reactions to the PND peptide, followed by passive transfer of the DTH by the systemic route. Further, immunization of mice with the rBCG resulted in induction of cytotoxic T lymphocytes. The guinea pig immune antisera showed elevated titers to the PND peptide and neutralized HIVMN, and administration of serum IgG from the vaccinated guinea pigs was effective in completely blocking the HIV infection in thymus/liver transplanted severe combined immunodeficiency (SCID)/hu or SCID/PBL mice. In addition, the immune serum IgG was shown to neutralize primary field isolates of HIV that match the neutralizing sequence motif by a peripheral blood mononuclear cell-based virus neutralization assay. The data support the idea that the antigen-secreting rBCG system can be used as a tool for development of HIV vaccines.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>7479867</pmid><doi>10.1073/pnas.92.23.10693</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1995-11, Vol.92 (23), p.10693-10697 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_92_23_10693_fulltext |
| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | AIDS Vaccines - immunology AIDS/HIV Amino Acid Sequence Animals Antibodies Antibodies, Viral - blood Antigens Base Sequence DNA Enzyme-Linked Immunosorbent Assay Genetic Vectors Guinea Pigs HIV HIV 1 HIV Envelope Protein gp120 - immunology HIV infections HIV Infections - prevention & control HIV-1 - immunology Human immunodeficiency virus human immunodeficiency virus 1 Humans Immunity (Disease) Immunization, Passive Medical research Mice Mice, SCID Middle Aged Molecular Sequence Data Mycobacterium bovis Mycobacterium bovis - genetics Neutralization Tests Peptide Fragments - immunology Proteins Skin Tests Spleen cells T-Lymphocytes, Cytotoxic Tuberculin Vaccination Vaccines, Synthetic - immunology Viral Proteins - metabolism Viruses |
| title | Protective Immune Responses Induced by Secretion of a Chimeric Soluble Protein from a Recombinant Mycobacterium bovis Bacillus Calmette-Guerin Vector Candidate Vaccine for Human Immunodeficiency Virus Type 1 in Small Animals |
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