The rabbit or sheep polyclonal p53 antibodies (CM1, SaPu, respectively) raised against recombinant full-length human p53 protein recognise all p53 isoforms, although Δ133p53 β and Δ133p53 γ are weakly revealed by polyclonal antibodies as these isoforms have lost most immunogenic domains of p53.
Further analysis led to selection of the most likely immunogenic domains.
Further, molecular computer aided modeling led to selection of the most likely immunogenic domains.
E2, the most immunogenic envelope glycoprotein, contains four antigenic domains, from A to D [ 4- 6] located within the N-terminal region of the protein.
Thus, HO-3, just like the great majority of EpCAM-specific antibodies, targets EpCAM mainly within the EGF like domains, which represent the most immunogenic components of this protein (Balzar et al, 1999).
The carboxyl terminal autophosphorylation domain was retained because it is the most unique and possibly most immunogenic portion of the HER2 molecule with the least homology to other members of the HER family.
Naturally, evolutionary pressure has selected the most immunogenic antigens to be the most versatile.
Initially, whole proteome of CHIKV was retrieved from database and perused to identify the most immunogenic protein.
An alternative approach could involve technologies that, instead of decellularizing the organ, would preserve most of the parenchymal integrity and target the most immunogenic components of an organ.
