Improvement in the UV resistance of baculoviruses by displaying nano-zinc oxide-binding peptides on the surfaces of their occlusion bodies

Appl Microbiol Biotechnol. 2015 Aug;99(16):6841-53. doi: 10.1007/s00253-015-6581-6. Epub 2015 Apr 17.

Abstract

The sensitivity of baculoviruses to UV radiation severely limits their large-scale application as biological insecticides. The polyhedron envelope of a baculovirus, which is composed of carbohydrate and polyhedron envelope protein (PEP), is a significant structure for the stability and persistence of occlusion bodies (OBs) under environmental conditions. The results of this study revealed that the rough pitted surface phenotype of a pep-null Autographa californica multiple nucleopolyhedrovirus (AcMNPV) could not be rescued by any of its homologues, such as Helicoverpa armigera nucleopolyhedrovirus pep or Cydia pomonella granulovirus putative peps. In contrast, the N-terminal and middle flexible region (NM region, 1-167 aa) of AcMNPV PEP were able to form an intact OB envelope. Furthermore, this region was capable of carrying eGFP to the surfaces of the OBs. To improve the UV resistance of AcMNPV OBs, two peptides capable of specifically binding to nano-ZnO were separately fused to the NM region of PEP. Under laboratory conditions, infectivity of the recombinant viruses binding to nano-ZnO particles was about ninefold higher than that without the nano-ZnO particles after UV-B irradiation. Pot experiments revealed that the half-life of the recombinant baculovirus binding nano-ZnO particles was 3.3 ± 0.15 days, which was significantly longer than that of the control virus (0.49 ± 0.06 days). These results therefore represent a new approach for the protection the baculoviral insecticides against UV irradiation in the field.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Baculoviridae / physiology*
  • Baculoviridae / radiation effects*
  • Microbial Viability / radiation effects*
  • Nanoparticles / metabolism
  • Protein Binding
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism
  • Virion / physiology*
  • Virion / radiation effects*
  • Zinc Oxide / metabolism

Substances

  • Recombinant Fusion Proteins
  • Viral Envelope Proteins
  • Zinc Oxide