Document 0820
 DOCN  M9650820
 TI    Characterization of the MN gp120 HIV-1 vaccine: antigen binding to alum.
 DT    9605
 AU    Weissburg RP; Berman PW; Cleland JL; Eastman D; Farina F; Frie S; Lim A;
       Mordenti J; Peterson MR; Yim K; et al; Pharmaceutical R&D, Genentech,
       Inc, South San Francisco,; California 94080, USA.
 SO    Pharm Res. 1995 Oct;12(10):1439-46. Unique Identifier : AIDSLINE
       MED/96117505
 AB    PURPOSE. The characterization of recombinant MN gp120/alum vaccine
       requires the study of the gp120-alum interaction for the successful
       formulation of an alum-based HIV-1 vaccine. METHODS. Several
       observations suggest that the gp120-alum interaction is weak, wherein
       buffer counterions such as phosphate, sulfate, bicarbonate may cause the
       desorption of gp120 from alum. Comparison of gp120 with other proteins
       using particle mobility measurements shows that the weak binding of
       gp120 to alum is not an anomaly. Serum and plasma also cause desorption
       of gp120 from alum with a half-life of only a few minutes, wherein this
       half-life may be faster than the in-vivo recruitment of antigen
       presenting cells to the site of immunization. RESULTS. Immunization of
       guinea pigs, rabbits and baboons with gp120 formulated in alum or saline
       demonstrated that alum provides adjuvant activity for gp120,
       particularly after early immunizations, but the adjuvant effect is
       attenuated after several boosts. CONCLUSIONS. These observations
       indicate that both the antigen and the adjuvant require optimization
       together.
 DE    Adjuvants, Immunologic  Adsorption  *Alum Compounds/CHEMISTRY  Animal
       AIDS Vaccines/*CHEMISTRY/IMMUNOLOGY  Blood  Catalysis  CHO Cells  Guinea
       Pigs  Hamsters  Human  HIV Envelope Protein gp120/CHEMISTRY/*IMMUNOLOGY
       HIV Infections/PREVENTION & CONTROL  HIV-1/*IMMUNOLOGY  Male  Papio
       Rabbits  JOURNAL ARTICLE

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