What is it about?

Env, the major surface protein of HIV-1, is the primary target of the immune response elicited against HIV-1 and is therefore an important candidate for vaccine design. Vaccines confer protective immunity by eliciting neutralizing antibodies that not only bind to a virus but also prevent further infection. The knowledge of target sites (epitopes) of neutralizing antibodies on the viral surface is therefore a prerequisite for the design of effective vaccines. We have devised a high-throughput methodology to rapidly identify epitopes of monoclonal and polyclonal neutralizing HIV-1 antibodies on Env, at single-residue resolution. The methodology is useful for both design and testing of HIV-1 vaccines and can be readily extended to identify neutralizing epitopes in emerging viral infections.

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Why is it important?

Our work describes an exciting new method for rapid identification of binding sites (epitopes) of neutralizing antibodies, directly on infectious HIV-1 viruses. Neutralizing antibodies not only bind to the virus, but also prevent further infection. This is a significant improvement over other indirect epitope mapping methods (which require the use of purified proteins or cell surface display) and represents a major advance in the field. Using our approach, neutralizing antibody epitopes can be accurately mapped in a highly parallelizable manner, without the need for advanced instrumentation used in other techniques such as X-ray crystallography and cryo-EM.


Our high-throughput approach, when applied to antibodies obtained from an HIV-infected patient, indicated the presence of two distinct epitopes on the envelope protein. This was challenging to identify using low-throughput approaches used in the past.

Rohini Datta
Stanford University

Read the Original

This page is a summary of: A facile method of mapping HIV-1 neutralizing epitopes using chemically masked cysteines and deep sequencing, Proceedings of the National Academy of Sciences, November 2020, Proceedings of the National Academy of Sciences, DOI: 10.1073/pnas.2010256117.
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