Invention Title:

ANTIGEN BINDING PROTEINS

Publication number:

US20240166728

Publication date:
Section:

Chemistry; metallurgy

Class:

C07K16/1063

Inventors:

Applicant:

Drawings (4 of 9)

Smart overview of the Invention

Antigen binding proteins designed to target the Human Immunodeficiency Virus (HIV) envelope protein show promise in the treatment and prevention of HIV infection. These proteins specifically bind to two critical regions on the HIV envelope glycoprotein 120 (gp120): the V3 loop region and the CD4 binding site. This dual binding capability could enhance their effectiveness against the virus.

Significance of HIV Treatment

HIV remains a significant global health issue, having led to over 40 million deaths and affecting millions worldwide. The virus primarily attacks CD4-positive T cells, compromising the immune system and making individuals susceptible to various opportunistic infections. Current treatment methods, such as antiretroviral therapy (ART), are effective but come with challenges including daily medication adherence, side effects, and the risk of drug resistance.

Potential of Broadly Neutralizing Antibodies

Broadly neutralizing antibodies (bNAbs) are being explored as a potential solution for long-term HIV management. While individual bNAbs have shown limited success due to the emergence of resistant virus strains, combinations of these antibodies are under investigation. The development of new therapies that are both long-acting and effective against a wide range of HIV strains is crucial for improving patient outcomes.

Key Aspects of Antigen Binding Proteins

The patent application outlines several innovative aspects of these antigen binding proteins. Key features include:

  • Binding to multiple epitopes on gp120.
  • Creation of bispecific proteins that combine anti-V3 bNAb with CD4 domains.
  • Pharmaceutical compositions and methods for using these proteins in clinical settings.

Research Findings and Applications

Figures included in the application provide data on the efficacy of these bispecific molecules against various HIV strains. The findings suggest that modifications in linker lengths and thermal stability can significantly impact their pharmacokinetics and antiviral activity. Overall, these advancements in antigen binding proteins may lead to more effective strategies for preventing and treating HIV infections.