A novel intracellularly expressed NS5B-specific nanobody suppresses bovine viral diarrhea virus replication

Vet Microbiol. 2020 Jan:240:108449. doi: 10.1016/j.vetmic.2019.108449. Epub 2019 Oct 12.

Abstract

Bovine viral diarrhea virus (BVDV) infection causes significant economic losses to the cattle industry worldwide and still represents a huge pressure on agricultural production. Thus, the development of novel anti-BVDV strategies are urgently needed. The nonstructural protein 5 (NS5B) of BVDV is essential for viral replication. Further, the camel single-domain antibody (nanobody) represents a promising antiviral approach with the advantages of small size, stable structure, high specificity and solubility, and the recognition of specific epitopes. However, no NS5B-specific nanobodies against BVDV have been reported. In this study, NS5B-specific nanobodies were isolated from a phage display library of variable domains of Camellidae heavy chain-only antibodies (VHHs). Further, an MDBK cell line stably expressing Nb1 was established to explore antiviral activity. Results showed that Nb1 could markedly suppress BVDV replication and interact with the BVDV NS5B protein. This suggests that nanobodies have potential for the development of novel antiviral drugs against BVDV infection.

Keywords: Antiviral effect; BVDV; Intrabody; NS5B; Nanobody.

MeSH terms

  • Animals
  • Antiviral Agents / immunology
  • Antiviral Agents / isolation & purification
  • Binding Sites, Antibody
  • Camelus / immunology
  • Cattle
  • Cell Line
  • Cell Surface Display Techniques
  • Cytoplasm / immunology
  • Diarrhea Viruses, Bovine Viral / immunology
  • Diarrhea Viruses, Bovine Viral / physiology*
  • Immunoglobulin Heavy Chains / immunology*
  • Immunoglobulin Heavy Chains / isolation & purification
  • Male
  • Single-Domain Antibodies / genetics
  • Single-Domain Antibodies / immunology*
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / immunology*
  • Virus Replication*

Substances

  • Antiviral Agents
  • Immunoglobulin Heavy Chains
  • Single-Domain Antibodies
  • Viral Nonstructural Proteins