We have previously shown that immunization with solid matrix-antigen-antibody (SMAA) complexes induces both vigorous humoral and cell-mediated immune responses and have suggested that this method of vaccination may be developed for use in humans, and potentially as a vaccine against AIDS. Here we demonstrate that a small oligopeptide can act as a tag for the construction of SMAA complexes using a tagspecific monoclonal antibody and tag-linked antigens. We show that a 14-amino acid oligopeptide, present in the phospho (P) and V proteins of simian virus 5 (SV5), retains its antigenicity when attached to the C terminus of three 'foreign' proteins [p27 and gp110 of simian immunodeficiency virus (SIV) and glutathione S-transferase] such that these proteins can be incorporated into SMAA complexes using a monoclonal antibody (MAb) that was originally raised against the native SV5 P and V proteins. Mice were immunized with SMAA complexes containing recombinant p27-TAG and MAbs have been isolated that recognized native SIV p27. The significance of these results in terms of the development of SMAA complexes as human vaccines is discussed.

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A group specific linear epitope with the sequence -FNPVY- was detected in the tail region of the adenovirus fibre by using a monoclonal antibody (Mab) and selection with a hexapeptide phage expression library. A synthetic peptide with sequence DTFNPVYPYDTE from adenovirus type 2 (Ad2) was shown by preincubation with the Mab to block its binding to fibre. A biotinylated form of this peptide bound to the monomeric fibre and not to the dimeric and trimeric forms. On the other hand the monoclonal antibodies bound to the monomeric, dimeric and trimeric forms of the fibre.

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Adenoviruses (Ads) have a complex architecture with at least 12 structural proteins. The major protein, the hexon, is the main component of the capsid and there are a number of other capsomeres which complete the capsid and link with the core of the virus (Stewart et al., 1993). The latter consists of the viral double-stranded DNA genome in association with a number of other proteins -the principal ones being proteins VII and V as well as the small peptide mµ. The spatial organization of the core has been the subject of a number of studies, sometimes with conflicting conclusions (for reviews see Nermut, 1984 ;Vayda et al., 1983). Protein VII is a highly basic protein very tightly attached to the viral DNA and most likely plays a role analogous to histones in cellular chromatin. However, very little is known of its structure and function although some