Back

Immunogenicity and Structure of Stabilized HIV-1 Clade-C Env from pediatric Elite-neutralizer complexed with autologous bNAb

Singh, S.; Kumar, S.; Chatterjee, A.; Malhotra, L.; Pervez, M.; Rahman, A.; Andrabi, I.; Mondal, B.; Katpara, S.; Sharma, S.; Bhakri, H.; Gaur, A.; Bansal, T.; Iyer, V.; Hussain, A. W.; Ahmed, S.; Kumar, R.; Ethayathulla, A. S.; Lodha, R.; Dutta, S.; Luthra, K.

2025-12-02 immunology
10.1101/2025.04.26.649701 bioRxiv
Show abstract

The envelope (Env) glycoprotein derived from circulating viruses in elite-neutralizers (who naturally develop broadly neutralizing antibodies (bNAbs)), serves as potential template for HIV-1 vaccine design. Herein, we report the structure and immunogenicity of soluble clade-C HIV-1 Env trimer (330) derived from a pediatric elite-neutralizer (AIIMS_330). Using SOSIP, NFL and ferritin-nanoparticle (NP) platforms, we engineered immunogens that preserved native-like Env conformation, exhibited high thermostability and nanomolar affinity for diverse bNAbs, with minimal reactivity to non-neutralizing antibodies. Cryo-EM structure solved at 5 [A] resolution of 330-SOSIP trimer-autologous bNAb 44m complex revealed interactions at GDIR motif, N332 supersite along with additional contacts at E293, K337, K446 and glycans N326, N442, N448, as compared to our previously reported BG505-44m structure. Rabbit immunizations with soluble and NP-displayed formats elicited autologous, and heterologous neutralization of tier-1 clade-C viruses. Herein we define a structurally resolved HIV-1 clade C Env that supports multivalent vaccine strategies and provides mechanistic insights toward rational HIV-1 immunogen design.

Matching journals

The top 5 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.