Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization
Lyophilization was used to prepare dry, glassy solid vaccine formulations of recombinant ricin toxin A-chain containing suspensions of colloidal aluminum hydroxide adjuvant. Four lyophilized formulations were prepared by using combinations of rapid or slow cooling during lyophilization and one of tw...
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| Veröffentlicht in: | European journal of pharmaceutics and biopharmaceutics 2013-10, Vol.85 (2), p.279-286 |
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| creator | Hassett, Kimberly J. Cousins, Megan C. Rabia, Lilia A. Chadwick, Chrystal M. O’Hara, Joanne M. Nandi, Pradyot Brey, Robert N. Mantis, Nicholas J. Carpenter, John F. Randolph, Theodore W. |
| description | Lyophilization was used to prepare dry, glassy solid vaccine formulations of recombinant ricin toxin A-chain containing suspensions of colloidal aluminum hydroxide adjuvant. Four lyophilized formulations were prepared by using combinations of rapid or slow cooling during lyophilization and one of two buffers, histidine or ammonium acetate. Trehalose was used as the stabilizing excipient. Aggregation of the colloidal aluminum hydroxide suspension was reduced in formulations processed with a rapid cooling rate. Aluminum hydroxide particle size distributions, glass transition temperatures, water contents, and immunogenicities of lyophilized vaccines were independent of incubation time at 40°C for up to 15weeks. Mice immunized with reconstituted ricin toxin subunit A (RTA) vaccines produced RTA-specific antibodies and toxin-neutralizing antibodies (TNAs) regardless of the length of high temperature vaccine storage or the degree of aluminum adjuvant aggregation that occurred during lyophilization. In murine studies, lyophilized formulations of vaccines conferred protection against exposure to lethal doses of ricin, even after the lyophilized formulations had been stored at 40°C for 4weeks. A corresponding liquid formulation of vaccine stored at 40°C elicited RTA-specific antibody titers but failed to confer immunity during a ricin challenge. |
| doi_str_mv | 10.1016/j.ejpb.2013.03.029 |
| format | Article |
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Four lyophilized formulations were prepared by using combinations of rapid or slow cooling during lyophilization and one of two buffers, histidine or ammonium acetate. Trehalose was used as the stabilizing excipient. Aggregation of the colloidal aluminum hydroxide suspension was reduced in formulations processed with a rapid cooling rate. Aluminum hydroxide particle size distributions, glass transition temperatures, water contents, and immunogenicities of lyophilized vaccines were independent of incubation time at 40°C for up to 15weeks. Mice immunized with reconstituted ricin toxin subunit A (RTA) vaccines produced RTA-specific antibodies and toxin-neutralizing antibodies (TNAs) regardless of the length of high temperature vaccine storage or the degree of aluminum adjuvant aggregation that occurred during lyophilization. In murine studies, lyophilized formulations of vaccines conferred protection against exposure to lethal doses of ricin, even after the lyophilized formulations had been stored at 40°C for 4weeks. A corresponding liquid formulation of vaccine stored at 40°C elicited RTA-specific antibody titers but failed to confer immunity during a ricin challenge.</description><identifier>ISSN: 0939-6411</identifier><identifier>EISSN: 1873-3441</identifier><identifier>DOI: 10.1016/j.ejpb.2013.03.029</identifier><identifier>PMID: 23583494</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Adjuvant ; Adjuvants, Immunologic - chemistry ; Adjuvants, Immunologic - pharmacology ; Adjuvants, Pharmaceutic - chemistry ; Adjuvants, Pharmaceutic - pharmacology ; Aggregation ; Aluminum ; Aluminum Hydroxide - chemistry ; Animals ; Antibodies, Neutralizing - immunology ; Antibody Formation - immunology ; Biodefense ; Buffers ; Chemistry, Pharmaceutical - methods ; Drug Stability ; Drug Storage ; Excipients - chemistry ; Female ; Freeze drying ; Freeze Drying - methods ; Hot Temperature ; Lyophilization ; Mice ; Particle Size ; Recombinant Proteins - chemistry ; Recombinant Proteins - immunology ; Ricin ; Ricin - chemistry ; Ricin - immunology ; Stability ; Transition Temperature ; Trehalose - chemistry ; Vaccine ; Vaccines, Subunit - chemistry ; Vaccines, Subunit - immunology ; Water - chemistry</subject><ispartof>European journal of pharmaceutics and biopharmaceutics, 2013-10, Vol.85 (2), p.279-286</ispartof><rights>2013 Elsevier B.V.</rights><rights>Copyright © 2013 Elsevier B.V. All rights reserved.</rights><rights>2013 Elsevier B.V. All rights reserved. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-434bb9c7b6e8fbc76e46794d93b89a618df995c2ac15d1f96989654198d3a13f3</citedby><cites>FETCH-LOGICAL-c488t-434bb9c7b6e8fbc76e46794d93b89a618df995c2ac15d1f96989654198d3a13f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0939641113001185$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23583494$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hassett, Kimberly J.</creatorcontrib><creatorcontrib>Cousins, Megan C.</creatorcontrib><creatorcontrib>Rabia, Lilia A.</creatorcontrib><creatorcontrib>Chadwick, Chrystal M.</creatorcontrib><creatorcontrib>O’Hara, Joanne M.</creatorcontrib><creatorcontrib>Nandi, Pradyot</creatorcontrib><creatorcontrib>Brey, Robert N.</creatorcontrib><creatorcontrib>Mantis, Nicholas J.</creatorcontrib><creatorcontrib>Carpenter, John F.</creatorcontrib><creatorcontrib>Randolph, Theodore W.</creatorcontrib><title>Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization</title><title>European journal of pharmaceutics and biopharmaceutics</title><addtitle>Eur J Pharm Biopharm</addtitle><description>Lyophilization was used to prepare dry, glassy solid vaccine formulations of recombinant ricin toxin A-chain containing suspensions of colloidal aluminum hydroxide adjuvant. Four lyophilized formulations were prepared by using combinations of rapid or slow cooling during lyophilization and one of two buffers, histidine or ammonium acetate. Trehalose was used as the stabilizing excipient. Aggregation of the colloidal aluminum hydroxide suspension was reduced in formulations processed with a rapid cooling rate. Aluminum hydroxide particle size distributions, glass transition temperatures, water contents, and immunogenicities of lyophilized vaccines were independent of incubation time at 40°C for up to 15weeks. Mice immunized with reconstituted ricin toxin subunit A (RTA) vaccines produced RTA-specific antibodies and toxin-neutralizing antibodies (TNAs) regardless of the length of high temperature vaccine storage or the degree of aluminum adjuvant aggregation that occurred during lyophilization. In murine studies, lyophilized formulations of vaccines conferred protection against exposure to lethal doses of ricin, even after the lyophilized formulations had been stored at 40°C for 4weeks. A corresponding liquid formulation of vaccine stored at 40°C elicited RTA-specific antibody titers but failed to confer immunity during a ricin challenge.</description><subject>Adjuvant</subject><subject>Adjuvants, Immunologic - chemistry</subject><subject>Adjuvants, Immunologic - pharmacology</subject><subject>Adjuvants, Pharmaceutic - chemistry</subject><subject>Adjuvants, Pharmaceutic - pharmacology</subject><subject>Aggregation</subject><subject>Aluminum</subject><subject>Aluminum Hydroxide - chemistry</subject><subject>Animals</subject><subject>Antibodies, Neutralizing - immunology</subject><subject>Antibody Formation - immunology</subject><subject>Biodefense</subject><subject>Buffers</subject><subject>Chemistry, Pharmaceutical - methods</subject><subject>Drug Stability</subject><subject>Drug Storage</subject><subject>Excipients - chemistry</subject><subject>Female</subject><subject>Freeze drying</subject><subject>Freeze Drying - methods</subject><subject>Hot Temperature</subject><subject>Lyophilization</subject><subject>Mice</subject><subject>Particle Size</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - immunology</subject><subject>Ricin</subject><subject>Ricin - chemistry</subject><subject>Ricin - immunology</subject><subject>Stability</subject><subject>Transition Temperature</subject><subject>Trehalose - chemistry</subject><subject>Vaccine</subject><subject>Vaccines, Subunit - chemistry</subject><subject>Vaccines, Subunit - immunology</subject><subject>Water - chemistry</subject><issn>0939-6411</issn><issn>1873-3441</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kV9LHDEUxYNUdKt-gT6UPPZl1vybTAKlIGJbQfBBfQ5JJuNmmU22SWZRP71ZVpf6IlzuheTcX8I5AHzDaI4R5ufLuVuuzZwgTOeoFpEHYIZFRxvKGP4CZkhS2XCG8TH4mvMSIcS6VhyBY0JbQZlkM3B3V7Txo3_RxccA4wA1TM7GlfFBhwKTtz7AEp9qv4B5MlPwBW60rccOlkWK0-MCjs9xvdhTTsHhoMfszt7mCXj4fXV_-be5uf1zfXlx01gmRGkYZcZI2xnuxGBsxx3jnWS9pEZIzbHoBylbS7TFbY8HyaWQvGVYip5qTAd6An7tuOvJrFxvXShJj2qd_EqnZxW1Vx9vgl-ox7hRtJMdIawCfrwBUvw3uVzUymfrxlEHF6escEsQ5ZQLUqVkJ7Up5pzcsH8GI7VNQy3VNg21TUOhWkTWpe__f3C_8m5_FfzcCVy1aeNdUtl6F6zrfQ2hqD76z_ivd1Wdpw</recordid><startdate>20131001</startdate><enddate>20131001</enddate><creator>Hassett, Kimberly J.</creator><creator>Cousins, Megan C.</creator><creator>Rabia, Lilia A.</creator><creator>Chadwick, Chrystal M.</creator><creator>O’Hara, Joanne M.</creator><creator>Nandi, Pradyot</creator><creator>Brey, Robert N.</creator><creator>Mantis, Nicholas J.</creator><creator>Carpenter, John F.</creator><creator>Randolph, Theodore W.</creator><general>Elsevier B.V</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>7T5</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20131001</creationdate><title>Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization</title><author>Hassett, Kimberly J. ; Cousins, Megan C. ; Rabia, Lilia A. ; Chadwick, Chrystal M. ; O’Hara, Joanne M. ; Nandi, Pradyot ; Brey, Robert N. ; Mantis, Nicholas J. ; Carpenter, John F. ; Randolph, Theodore W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-434bb9c7b6e8fbc76e46794d93b89a618df995c2ac15d1f96989654198d3a13f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adjuvant</topic><topic>Adjuvants, Immunologic - chemistry</topic><topic>Adjuvants, Immunologic - pharmacology</topic><topic>Adjuvants, Pharmaceutic - chemistry</topic><topic>Adjuvants, Pharmaceutic - pharmacology</topic><topic>Aggregation</topic><topic>Aluminum</topic><topic>Aluminum Hydroxide - chemistry</topic><topic>Animals</topic><topic>Antibodies, Neutralizing - immunology</topic><topic>Antibody Formation - immunology</topic><topic>Biodefense</topic><topic>Buffers</topic><topic>Chemistry, Pharmaceutical - methods</topic><topic>Drug Stability</topic><topic>Drug Storage</topic><topic>Excipients - chemistry</topic><topic>Female</topic><topic>Freeze drying</topic><topic>Freeze Drying - methods</topic><topic>Hot Temperature</topic><topic>Lyophilization</topic><topic>Mice</topic><topic>Particle Size</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - immunology</topic><topic>Ricin</topic><topic>Ricin - chemistry</topic><topic>Ricin - immunology</topic><topic>Stability</topic><topic>Transition Temperature</topic><topic>Trehalose - chemistry</topic><topic>Vaccine</topic><topic>Vaccines, Subunit - chemistry</topic><topic>Vaccines, Subunit - immunology</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hassett, Kimberly J.</creatorcontrib><creatorcontrib>Cousins, Megan C.</creatorcontrib><creatorcontrib>Rabia, Lilia A.</creatorcontrib><creatorcontrib>Chadwick, Chrystal M.</creatorcontrib><creatorcontrib>O’Hara, Joanne M.</creatorcontrib><creatorcontrib>Nandi, Pradyot</creatorcontrib><creatorcontrib>Brey, Robert N.</creatorcontrib><creatorcontrib>Mantis, Nicholas J.</creatorcontrib><creatorcontrib>Carpenter, John F.</creatorcontrib><creatorcontrib>Randolph, Theodore W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Toxicology 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>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>European journal of pharmaceutics and biopharmaceutics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hassett, Kimberly J.</au><au>Cousins, Megan C.</au><au>Rabia, Lilia A.</au><au>Chadwick, Chrystal M.</au><au>O’Hara, Joanne M.</au><au>Nandi, Pradyot</au><au>Brey, Robert N.</au><au>Mantis, Nicholas J.</au><au>Carpenter, John F.</au><au>Randolph, Theodore W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization</atitle><jtitle>European journal of pharmaceutics and biopharmaceutics</jtitle><addtitle>Eur J Pharm Biopharm</addtitle><date>2013-10-01</date><risdate>2013</risdate><volume>85</volume><issue>2</issue><spage>279</spage><epage>286</epage><pages>279-286</pages><issn>0939-6411</issn><eissn>1873-3441</eissn><abstract>Lyophilization was used to prepare dry, glassy solid vaccine formulations of recombinant ricin toxin A-chain containing suspensions of colloidal aluminum hydroxide adjuvant. Four lyophilized formulations were prepared by using combinations of rapid or slow cooling during lyophilization and one of two buffers, histidine or ammonium acetate. Trehalose was used as the stabilizing excipient. Aggregation of the colloidal aluminum hydroxide suspension was reduced in formulations processed with a rapid cooling rate. Aluminum hydroxide particle size distributions, glass transition temperatures, water contents, and immunogenicities of lyophilized vaccines were independent of incubation time at 40°C for up to 15weeks. Mice immunized with reconstituted ricin toxin subunit A (RTA) vaccines produced RTA-specific antibodies and toxin-neutralizing antibodies (TNAs) regardless of the length of high temperature vaccine storage or the degree of aluminum adjuvant aggregation that occurred during lyophilization. In murine studies, lyophilized formulations of vaccines conferred protection against exposure to lethal doses of ricin, even after the lyophilized formulations had been stored at 40°C for 4weeks. A corresponding liquid formulation of vaccine stored at 40°C elicited RTA-specific antibody titers but failed to confer immunity during a ricin challenge.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>23583494</pmid><doi>10.1016/j.ejpb.2013.03.029</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adjuvant Adjuvants, Immunologic - chemistry Adjuvants, Immunologic - pharmacology Adjuvants, Pharmaceutic - chemistry Adjuvants, Pharmaceutic - pharmacology Aggregation Aluminum Aluminum Hydroxide - chemistry Animals Antibodies, Neutralizing - immunology Antibody Formation - immunology Biodefense Buffers Chemistry, Pharmaceutical - methods Drug Stability Drug Storage Excipients - chemistry Female Freeze drying Freeze Drying - methods Hot Temperature Lyophilization Mice Particle Size Recombinant Proteins - chemistry Recombinant Proteins - immunology Ricin Ricin - chemistry Ricin - immunology Stability Transition Temperature Trehalose - chemistry Vaccine Vaccines, Subunit - chemistry Vaccines, Subunit - immunology Water - chemistry |
| title | Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization |
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