Poly(gamma-D-glutamic acid) protein conjugates induce IgG antibodies in mice to the capsule of Bacillus anthracis: a potential addition to the anthrax vaccine.
Identifieur interne : 003239 ( Main/Merge ); précédent : 003238; suivant : 003240Poly(gamma-D-glutamic acid) protein conjugates induce IgG antibodies in mice to the capsule of Bacillus anthracis: a potential addition to the anthrax vaccine.
Auteurs : Rachel Schneerson [États-Unis] ; Joanna Kubler-Kielb ; Teh-Yung Liu ; Zhong-Dong Dai ; Stephen H. Leppla ; Alfred Yergey ; Peter Backlund ; Joseph Shiloach ; Fathy Majadly ; John B. RobbinsSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2003.
Descripteurs français
- KwdFr :
- Acide polyglutamique (), Acide polyglutamique (administration et posologie), Acide polyglutamique (immunologie), Animaux, Anticorps antibactériens (biosynthèse), Antigènes bactériens (), Antigènes bactériens (administration et posologie), Bacillus anthracis (immunologie), Femelle, Immunoglobuline G (biosynthèse), Maladie du charbon (), Maladie du charbon (immunologie), Souris, Toxines bactériennes (), Toxines bactériennes (administration et posologie), Toxines bactériennes (immunologie), Vaccins anticharbonneux (), Vaccins anticharbonneux (administration et posologie), Vaccins conjugués (), Vaccins conjugués (administration et posologie).
- MESH :
- administration et posologie : Acide polyglutamique, Antigènes bactériens, Toxines bactériennes, Vaccins anticharbonneux, Vaccins conjugués.
- biosynthèse : Anticorps antibactériens, Immunoglobuline G.
- immunologie : Acide polyglutamique, Bacillus anthracis, Maladie du charbon, Toxines bactériennes.
- Acide polyglutamique, Animaux, Antigènes bactériens, Femelle, Maladie du charbon, Souris, Toxines bactériennes, Vaccins anticharbonneux, Vaccins conjugués.
English descriptors
- KwdEn :
- Animals, Anthrax (immunology), Anthrax (prevention & control), Anthrax Vaccines (administration & dosage), Anthrax Vaccines (chemistry), Antibodies, Bacterial (biosynthesis), Antigens, Bacterial (administration & dosage), Antigens, Bacterial (chemistry), Bacillus anthracis (immunology), Bacterial Toxins (administration & dosage), Bacterial Toxins (chemistry), Bacterial Toxins (immunology), Female, Immunoglobulin G (biosynthesis), Mice, Polyglutamic Acid (administration & dosage), Polyglutamic Acid (chemistry), Polyglutamic Acid (immunology), Vaccines, Conjugate (administration & dosage), Vaccines, Conjugate (chemistry).
- MESH :
- chemical , administration & dosage : Anthrax Vaccines, Antigens, Bacterial, Bacterial Toxins, Polyglutamic Acid, Vaccines, Conjugate.
- chemical , biosynthesis : Antibodies, Bacterial, Immunoglobulin G.
- chemical , chemistry : Anthrax Vaccines, Antigens, Bacterial, Bacterial Toxins, Polyglutamic Acid, Vaccines, Conjugate.
- immunology : Anthrax, Bacillus anthracis, Bacterial Toxins, Polyglutamic Acid.
- prevention & control : Anthrax.
- Animals, Female, Mice.
Abstract
Both the protective antigen (PA) and the poly(gamma-d-glutamic acid) capsule (gamma dPGA) are essential for the virulence of Bacillus anthracis. A critical level of vaccine-induced IgG anti-PA confers immunity to anthrax, but there is no information about the protective action of IgG anti-gamma dPGA. Because the number of spores presented by bioterrorists might be greater than encountered in nature, we sought to induce capsular antibodies to expand the immunity conferred by available anthrax vaccines. The nonimmunogenic gamma dPGA or corresponding synthetic peptides were bound to BSA, recombinant B. anthracis PA (rPA), or recombinant Pseudomonas aeruginosa exotoxin A (rEPA). To identify the optimal construct, conjugates of B. anthracis gamma dPGA, Bacillus pumilus gamma dLPGA, and peptides of varying lengths (5-, 10-, or 20-mers), of the d or l configuration with active groups at the N or C termini, were bound at 5-32 mol per protein. The conjugates were characterized by physico-chemical and immunological assays, including GLC-MS and matrix-assisted laser desorption ionization time-of-flight spectrometry, and immunogenicity in 5- to 6-week-old mice. IgG anti-gamma dPGA and antiprotein were measured by ELISA. The highest levels of IgG anti-gamma dPGA were elicited by decamers of gamma dPGA at 10 -20 mol per protein bound to the N- or C-terminal end. High IgG anti-gamma dPGA levels were elicited by two injections of 2.5 microg of gamma dPGA per mouse, whereas three injections were needed to achieve high levels of protein antibodies. rPA was the most effective carrier. Anti-gamma dPGA induced opsonophagocytic killing of B. anthracis tox-, cap+. gamma dPGA conjugates may enhance the protection conferred by PA alone. gamma dPGA-rPA conjugates induced both anti-PA and anti-gamma dPGA.
DOI: 10.1073/pnas.1633512100
PubMed: 12857944
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pubmed:12857944Le document en format XML
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A critical level of vaccine-induced IgG anti-PA confers immunity to anthrax, but there is no information about the protective action of IgG anti-gamma dPGA. Because the number of spores presented by bioterrorists might be greater than encountered in nature, we sought to induce capsular antibodies to expand the immunity conferred by available anthrax vaccines. The nonimmunogenic gamma dPGA or corresponding synthetic peptides were bound to BSA, recombinant B. anthracis PA (rPA), or recombinant Pseudomonas aeruginosa exotoxin A (rEPA). To identify the optimal construct, conjugates of B. anthracis gamma dPGA, Bacillus pumilus gamma dLPGA, and peptides of varying lengths (5-, 10-, or 20-mers), of the d or l configuration with active groups at the N or C termini, were bound at 5-32 mol per protein. The conjugates were characterized by physico-chemical and immunological assays, including GLC-MS and matrix-assisted laser desorption ionization time-of-flight spectrometry, and immunogenicity in 5- to 6-week-old mice. IgG anti-gamma dPGA and antiprotein were measured by ELISA. The highest levels of IgG anti-gamma dPGA were elicited by decamers of gamma dPGA at 10 -20 mol per protein bound to the N- or C-terminal end. High IgG anti-gamma dPGA levels were elicited by two injections of 2.5 microg of gamma dPGA per mouse, whereas three injections were needed to achieve high levels of protein antibodies. rPA was the most effective carrier. Anti-gamma dPGA induced opsonophagocytic killing of B. anthracis tox-, cap+. gamma dPGA conjugates may enhance the protection conferred by PA alone. gamma dPGA-rPA conjugates induced both anti-PA and anti-gamma dPGA.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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