ppat.1010994.s011.pdf (900.47 kB)
Epitopes of different broadly neutralizing antibodies.
journal contribution
posted on 2022-12-12, 18:39 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 KumarThe surface of the spike-RBD is displayed and the epitope for different mAbs are shown in red colour. The mAbs JMB2002 and S3H3 are not shown here because the epitopes for these two antibodies are outside the RBD. The epitopes of 87G7, 510A5, Cov2-2196, NCV2SG48, NCV2SG53, S2E12, S2K146 and ZWD12 showed some overlap with that of P4A2 but only P4A2 mAb possesses a hydrophobic cleft into which the 486Phe residue is buried. Based on available information, P4A2 forms multiple interactions with its cognate epitope on spike-RBD and multiple residues present in this epitope are critical for interaction with ACE2.
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