Structural study of adenovirus type 2 fibre using anti-fibre and anti-peptide sera.

Peptides corresponding to the N- and C-extremities of the adenovirus 2 fibre polypeptide were synthesized, coupled to tetanus toxoid and injected into rabbits. Two sera were obtained: the anti-NTT serum and the anti-CTT serum. These sera and an anti-native-fibre serum were used to study fragments generated by hydrochloric acid cleavage of the fibre. The 44-Kd fragment corresponding to the 2/3 N-terminal part of the molecule retained its antigenic reactivity. This is consistent with a shaft structure for this part of the fibre. The anti-peptide sera were used to orientate the fibre, i.e., to determine the site of anchorage of this protein in the penton base. First, immunorevelation of blots of enzymatic digests of native or dissociated penton suggested that the N-extremity of the fibre was involved in the assembly of this protein in the penton base. Second, attempts were made to determine the accessibility of the fibre ends in the penton structure by ELISA assays and by immunorevelation of penton in Western blots. The results agreed with the proposed orientation derived from study of the enzymatic digests. Since the 2 anti-peptide sera and the peptides were unable to affect viral adsorption, it was not possible to determine how the fibre is orientated with respect to the cell receptor. However, the anti-peptide sera were found to inhibit viral production slightly.