ppat.1010994.s002.pdf (910.09 kB)
Mutations in RBD associated with different VOCs do not affect binding to P4A2 Fab.
journal contribution
posted on 2022-12-12, 18:38 authored by Hilal Ahmad Parray, Naveen Narayanan, Sonal Garg, Zaigham Abbas Rizvi, Tripti Shrivastava, Sachin Kushwaha, Janmejay Singh, Praveenkumar Murugavelu, Anbalagan Anantharaj, Farha Mehdi, Nisha Raj, Shivam Singh, Jyotsna Dandotiya, Asha Lukose, Deepti Jamwal, Sandeep Kumar, Adarsh K. Chiranjivi, Samridhi Dhyani, Nitesh Mishra, Sanjeev Kumar, Kamini Jakhar, Sudipta Sonar, Anil Kumar Panchal, Manas Ranjan Tripathy, Shirlie Roy Chowdhury, Shubbir Ahmed, Sweety Samal, Shailendra Mani, Sankar Bhattacharyya, Supratik Das, Subrata Sinha, Kalpana Luthra, Gaurav Batra, Devinder Sehgal, Guruprasad R. Medigeshi, Chandresh Sharma, Amit Awasthi, Pramod Kumar Garg, Deepak T. Nair, Rajesh KumarUsing 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.
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