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Development of an adjuvant-active nonionic block copolymer for use in oil-free subunit vaccines formulations
Nonionic block copolymers, synthesized from repeating units of oxypropylene and oxyethylene, can be designed so that individual copolymers have unique physical properties with differential levels of adjuvant activity. We have designed high molecular weight block copolymers that spontaneously assembl...
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Published in: | Vaccine 1997-04, Vol.15 (5), p.564-570 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Nonionic block copolymers, synthesized from repeating units of oxypropylene and oxyethylene, can be designed so that individual copolymers have unique physical properties with differential levels of adjuvant activity. We have designed high molecular weight block copolymers that spontaneously assemble into 500 nm–3 μm particles when formulated with protein antigens in aqueous solutions at physiological pH. The adjuvant activity of one of these copolymers, termed CRL1005, was compared to selected research adjuvants using ovalbumin (OVA) as the prototype vaccine antigen. Suboptimal doses of OVA were formulated with complete and incomplete Freund's adjuvant (
CFA
IFA
), alum, Quil-A saponins, Ribi Adjuvant System (RAS) or the CRL1005 copolymer and these formulations were used to immunize
C57BL
6
mice. The CRL1005 copolymer appeared to be more potent than either Quil-A or alum and comparable to the RAS formulation, based on the numbers of responding mice and the OVA-specific antibody titers. Alum, RAS and Quil-A all augmented the production of IgG
1 and IgG
2b similarly whereas only the
CFA
IFA
boosted IgG
2a levels significantly. The effect of adjuvants on relative antibody affinity was more variable with the CRL1005 and
CFA
IFA
inducing antibodies with the highest affinity scores. This high molecular weight nonionic copolymer is nontoxic in aqueous formulations and should therefore be compatible with a wide variety of protein or polysaccharide vaccine antigens. |
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ISSN: | 0264-410X 1873-2518 |
DOI: | 10.1016/S0264-410X(97)00209-0 |