RiVax is a promising recombinant ricin poison A subunit (RTA) antibody antigen that has been demonstrated to be protected and immunogenic in people and successful at securing rhesus macaques against deadly portion aerosolized poison openness. We recently utilized a board of RTA-explicit monoclonal antibodies (MAbs) to illustrate, by rivalry chemical connected immunosorbent test (ELISA), that RiVax inspires comparative serum neutralizer profiles in people and macaques. Be that as it may, the MAb restricting locales on RiVax still can’t seem to be characterized. In this investigation, we utilized hydrogen trade mass spectrometry (HX-MS) to limit the epitopes on RiVax perceived by nine poison killing MAbs and one nonneutralizing MAb. In view of solid security from hydrogen trade, the nine MAbs gathered into four spatially particular epitope groups (specifically, bunches I to IV). Group I MAbs ensured RiVax’s α-helix B (buildups 94 to 107), a distending immunodominant optional structure component known to be an objective of intense poison killing antibodies. 

Reference link- https://cvi.asm.org/content/24/12/e00237-17