{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T19:29:33Z","timestamp":1789673373375,"version":"4.0.1"},"reference-count":29,"publisher":"American Society for Microbiology","issue":"8","license":[{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2006,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The capsule of\n            <jats:italic>Bacillus anthracis<\/jats:italic>\n            , composed of poly-\u03b3-\n            <jats:sc>d<\/jats:sc>\n            -glutamic acid (\u03b3DPGA), is an essential virulence factor of\n            <jats:italic>B. anthracis<\/jats:italic>\n            . The capsule inhibits innate host defense through its antiphagocytic action. \u03b3DPGA is a poor immunogen, but when covalently bound to a carrier protein, it elicits serum antibodies. To identify the optimal construct for clinical use, synthetic \u03b3DPGAs of different lengths were bound to carrier proteins at different densities. The advantages of the synthetic over the natural polypeptide are the homogeneous chain length and end groups, allowing conjugates to be accurately characterized and standardized and their chemical compositions to be related to their immunogenicities. In the present study, we evaluated, in addition to methods reported by us, hydrazone, oxime, and thioether linkages between \u03b3DPGA and several proteins, including bovine serum albumin, recombinant\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            exotoxin A, recombinant\n            <jats:italic>B. anthracis<\/jats:italic>\n            protective antigen (rPA), and tetanus toxoid (TT). The effects of the dosage and formulation on the immunogenicities of the conjugates were evaluated in mice. All conjugates were immunogenic. The optimal \u03b3DPGA chain length of 10 to 15 amino acids and the density, an average of 15 mol \u03b3DPGA per mol of protein, were confirmed. The thioether bond was the optimal linkage type, and TT and rPA were the best carriers. The optimal dosage was 1.2 to 2.5 \u03bcg of \u03b3DPGA per mouse, and adsorption of the conjugates onto aluminum hydroxide significantly increased the antibody response to the protein with a lesser effect on anti-\u03b3DPGA levels.\n          <\/jats:p>","DOI":"10.1128\/iai.00315-06","type":"journal-article","created":{"date-parts":[[2006,7,22]],"date-time":"2006-07-22T00:24:50Z","timestamp":1153527890000},"page":"4744-4749","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":27,"title":["Additional Conjugation Methods and Immunogenicity of\n            <i>Bacillus anthracis<\/i>\n            Poly-\u03b3-\n            <scp>d<\/scp>\n            -Glutamic Acid-Protein Conjugates"],"prefix":"10.1128","volume":"74","author":[{"given":"Joanna","family":"Kubler-Kielb","sequence":"first","affiliation":[{"name":"Laboratory of Developmental and Molecular Immunity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teh-Yung","family":"Liu","sequence":"additional","affiliation":[{"name":"Laboratory of Developmental and Molecular Immunity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher","family":"Mocca","sequence":"additional","affiliation":[{"name":"Laboratory of Developmental and Molecular Immunity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fathy","family":"Majadly","sequence":"additional","affiliation":[{"name":"Laboratory of Developmental and Molecular Immunity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John B.","family":"Robbins","sequence":"additional","affiliation":[{"name":"Laboratory of Developmental and Molecular Immunity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachel","family":"Schneerson","sequence":"additional","affiliation":[{"name":"Laboratory of Developmental and Molecular Immunity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj1730723"},{"key":"e_1_3_2_3_2","first-page":"677","volume":"50","year":"2001","unstructured":"Centers for Disease Control and Prevention. 2001. Human anthrax associated with an epizootic among livestock\u2014North Dakota, 2000. Morb. Mortal. Wkly. Rep.50:677-680.","journal-title":"Morb. Mortal. Wkly. Rep."},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2004.05.029"},{"key":"e_1_3_2_5_2","first-page":"48","volume":"10","year":"1989","unstructured":"Dick, W. E., and M. Beurret, Jr. 1989. Glycoconjugates of bacterial carbohydrate antigens. A survey and consideration of design and preparation factors. Contrib. Microbiol. Immunol.10:48-114.","journal-title":"Contrib. Microbiol. 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