Using the crystal structure, computational models of P4A2 Fab in complex with the RBD from (A) Beta, (B) Gamma, (C) Delta, (D) Kappa and (E) BA.1 VOCs were generated. These models show that, for all the VOCs, there are no mutations in the residues that interact with the P4A2 through their side-chain and hence these mutations will not adversely impact P4A2 binding. E484 is mutated to Lys, Gln or Ala in some of the VOCs, but it forms interactions with the P4A2 Fab paratope through the backbone atoms and not through the side chain.