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  11. Avidity And Variable Domain Spacing Strongly Influence The Therapeutic Potency Of Bispecific Antibodies Against Crimean-congo Hemorrhagic Fever Virus

Avidity and variable domain spacing strongly influence the therapeutic potency of bispecific antibodies against Crimean-Congo hemorrhagic fever virus

Albert Wang1, Stephanie R Monticelli2,3, Ariel S Wirchnianski1

  • 1Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.

Mbio
|April 16, 2025

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View abstract on PubMed

Summary
This summary is machine-generated.

New bispecific antibodies targeting Crimean-Congo hemorrhagic fever virus (CCHFV) show improved therapeutic protection. Optimized antibody designs enhance neutralization and efficacy against diverse CCHFV strains, offering a promising avenue for treatment.

Area of Science:

  • Virology and Immunology
  • Infectious Diseases
  • Therapeutic Antibody Development

Background:

  • Crimean-Congo hemorrhagic fever virus (CCHFV) is a lethal tick-borne virus with no approved vaccines or therapeutics.
  • Antibody-based therapies targeting CCHFV glycoproteins (Gn and Gc) are a promising approach.
  • Previous work demonstrated synergistic neutralization and therapeutic protection using a dual variable domain (DVD) bispecific antibody (bsAb), DVD-121-801.

Purpose of the Study:

  • To investigate the molecular requirements for DVD-121-801 activity and optimize its therapeutic efficacy.
  • To explore spacing and avidity requirements of bsAb variants against divergent CCHFV isolates.
  • To identify an improved bsAb variant for further therapeutic development against CCHFV.

Main Methods:

  • Generated and evaluated a panel of bsAb variants of DVD-121-801.
Keywords:
Crimean-Congo hemorrhagic fever virusbispecific antibodyimmunotherapymonoclonal antibody

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  • Assessed variants for neutralization, fusion inhibition, and protection using virus-like particles, authentic viruses, and in vivo challenge studies.
  • Explored the contribution of antibody avidity in protection against CCHFV infection.

    • Main Results:

    • Neutralization potency was largely unaffected by spacing or variable domain identity within the bsAb.
    • A next-generation design (DVD-121-801GS) with longer, flexible linkers showed enhanced breadth of therapeutic protection.
    • The study highlights the importance of antibody avidity in therapeutic efficacy against CCHFV.

    Conclusions:

    • Optimized bsAb variants, particularly DVD-121-801GS, demonstrate improved therapeutic potential against CCHFV.
    • Antibody avidity plays a crucial role in enhancing protection against CCHFV infection.
    • This research leads to an improved bsAb candidate for future CCHFV therapeutic development.