Nucleocapsid protein-specific monoclonal antibodies protect mice against Crimean-Congo hemorrhagic fever virus

Aura R. Garrison (), Vanessa Moresco, Xiankun Zeng, Curtis R. Cline, Michael D. Ward, Keersten M. Ricks, Scott P. Olschner, Lisa H. Cazares, Elif Karaaslan, Collin J. Fitzpatrick, Éric Bergeron, Scott D. Pegan and Joseph W. Golden ()
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Aura R. Garrison: United States Army Medical Research Institute of Infectious Diseases
Vanessa Moresco: University of California Riverside
Xiankun Zeng: United States Army Medical Research Institute of Infectious Diseases
Curtis R. Cline: United States Army Medical Research Institute of Infectious Diseases
Michael D. Ward: United States Army Medical Research Institute of Infectious Diseases
Keersten M. Ricks: United States Army Medical Research Institute of Infectious Diseases
Scott P. Olschner: United States Army Medical Research Institute of Infectious Diseases
Lisa H. Cazares: United States Army Medical Research Institute of Infectious Diseases
Elif Karaaslan: Centers for Disease Control and Prevention
Collin J. Fitzpatrick: United States Army Medical Research Institute of Infectious Diseases
Éric Bergeron: Centers for Disease Control and Prevention
Scott D. Pegan: University of California Riverside
Joseph W. Golden: United States Army Medical Research Institute of Infectious Diseases

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Crimean-Congo hemorrhagic fever virus (CCHFV) is a WHO priority pathogen. Antibody-based medical countermeasures offer an important strategy to mitigate severe disease caused by CCHFV. Most efforts have focused on targeting the viral glycoproteins. However, glycoproteins are poorly conserved among viral strains. The CCHFV nucleocapsid protein (NP) is highly conserved between CCHFV strains. Here, we investigate the protective efficacy of a CCHFV monoclonal antibody targeting the NP. We find that an anti-NP monoclonal antibody (mAb-9D5) protected female mice against lethal CCHFV infection or resulted in a significant delay in mean time-to-death in mice that succumbed to disease compared to isotype control animals. Antibody protection is independent of Fc-receptor functionality and complement activity. The antibody bound NP from several CCHFV strains and exhibited robust cross-protection against the heterologous CCHFV strain Afg09-2990. Our work demonstrates that the NP is a viable target for antibody-based therapeutics, providing another direction for developing immunotherapeutics against CCHFV.

Date: 2024
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DOI: 10.1038/s41467-024-46110-4

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