Influence of particle size and antigen binding on effectiveness of aluminum salt adjuvants in a model lysozyme vaccine.
It has been suggested that agglomeration of aluminum salt adjuvant particles during freezing and drying can cause loss of immunogenicity of vaccines formulated with such adjuvants. In this study, we tested this hypothesis and examined the immune response in a murine model to various liquid, freeze-thawed, and lyophilized vaccine formulations, using lysozyme as a model antigen. The various processing techniques and excipient levels resulted in a wide range of particle size distributions (PSDs) and antigen-adjuvant binding levels. Anti-lysozyme titers were independent of the PSD for vaccines adjuvanted with either aluminum hydroxide or aluminum phosphate and also were unaffected by the level of antigen binding to the adjuvant.
Clausi
Amber
A
Department of Chemical and Biological Engineering, Center for Pharmaceutical Biotechnology, ECCH 111, Campus Box 424, University of Colorado, Boulder, Colorado, USA.
Cummiskey
Jessica
J
Merkley
Scott
S
Carpenter
John F
JF
Braun
Latoya Jones
LJ
Randolph
Theodore W
TW
D000276:Adjuvants, Immunologic / Q000737:chemistry*; D000535:Aluminum / Q000737:chemistry*; D000818:Animals; D000941:Antigens / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D005612:Freeze Drying; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D009113:Muramidase / Q000737:chemistry*; D010316:Particle Size; D012492:Salts / Q000737:chemistry; D014612:Vaccines / Q000737:chemistry* / Q000276:immunology
D000276:Adjuvants, Immunologic; D000941:Antigens; D012492:Salts; D014612:Vaccines; D000535:Aluminum; D009113:Muramidase