Monoclonal antibodies to a peptide of human rhinovirus type 2 with different specificities recognize the same minimum sequence

Rhinovirus infections and immunisation induce cross-serotype reactive antibodies to VP1

“…Systemic immunisation of mice with RV in Freund's adjuvant did not promote IgA responses despite generating high-titre neutralising IgG responses, suggesting that the route of RV administration and virus replication might be critical for optimal IgA responses. However, Barnett et al have previously demonstrated that IgA-producing hybridomas specific to RV are generated after immunisation of mice with adjuvanted RV peptides (Barnett et al, 1995(Barnett et al, , 1993. Nevertheless, a stronger IgG response in mice may still be biologically significant for RV infection since it is known that secretory IgA protects the upper respiratory tract from influenza but IgG is more important for protection of the lungs (Renegar et al, 2004).…”

A protective anti-peptide antibody against the immunodominant site of the A24 Cruzeiro strain of foot-and-mouth disease virus and its reactivity with other subtype viruses containing the same minimum binding sequence

“…This phenomenon was also observed with the protection data, suggesting that the similar functional affinities of A27 Cundinamarca Colombia/76, A Argentina/79 and A Venceslau Brazil/76 with C1.1, seen in the liquid phase ELISA, did not correlate with similar levels of neutralization or protection. Recently, it has been shown that MAbs to a peptide of HRV2 which recognize the same minimum sequence and with similar functional affinities can have different specificities (Barnett et al, 1993(Barnett et al, , 1995. In this study, it would appear that functional disparity of an anti-peptide antibody with other A strains can also occur, even though these different viruses contain the same minimum binding sequence and show similar affinities.…”

“…This would suggest that the endowment of the functional properties of an antibody is not limited entirely to sequence recognition. There are many examples of amino acid substitutions occurring outside an epitope which sterically affect antibody recognition (Ibrahimi et al, 1979;A1 Moudallal et al, 1982;Cooper et al, 1987;Parry et al, 1990;Barnett et al, 1995). Moreover, recent crystallographic evidence has also shown that flanking amino acids, outside the minimum binding epitope as defined by a set of overlapping peptides (Hastings et al, 1990), are nevertheless important in the interactions between peptide and antibody (Tormo et al, 1994).…”

“…Comparison of the sequences comprising 149-154 of VPI of a number of A subtype viruses (Weddell et al, 1985;Beck & Strohmaier, 1987) revealed that this region was reasonably conserved within a region of hypervariability, and often included only a single amino acid change. Based on this and also the observation that a single mutational change within an epitope may also enhance binding and neutralization by an antibody (Ferguson et al, 1986;Barnett et al, 1995) it was decided to determine if C 1.1 could cross-react with other A type strains. Preliminary assessment using a panel of 12-mer peptides encompassing VP1 residues 147-158 representing at least 17 different A strains indicated that almost all of the naturally occurring mutations within the minimum binding sequence abrogated binding.…”

“…Group 1, antibodies which recognized and neutralized native virus; group 2, antibodies which bound to intact 0001-3605 © 1996 SGM virus particles, but failed to neutralize infectivity; group 3, antibodies which recognized virus only after capsid distortions; and group 4 antibodies, which were peptide specific. Surprisingly, despite having these different biological activities many of the MAbs recognized the same minimum binding sequence (Barnett et al, 1995).…”