C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization

- Enzyme hydrolysis or genetic truncation of C-terminal domain of MrNV VLP is still able to form VLP icosahedral conformation.
- Chymotryptic removal of a C-terminal peptide from MrNV VLP and its F344 truncated variant exhibited a drastically reduced ability to interact and internalize into Sf9 cells.
- C-terminal domain is not only exposed on the capsid surface, but also constitutes the central core of the viral capsid protrusion.

We have shown that Macrobrachium rosenbergii nodavirus (MrNV) was able to infect Sf9 cells and that MrNV virus-like particles (MrNV-VLPs) were capable nanocontainers for delivering nucleic acid-based materials. Here, we demonstrated that chymotryptic removal of a C-terminal peptide and its truncated variant (F344-MrNV-VLPs) exhibited a drastically reduced ability to interact and internalize into Sf9 cells. Electron microscopic observations revealed that the loss of C-terminal domain either from enzyme hydrolysis or genetic truncation did not affect the generated MrNV-VLPs' icosahedral conformation, but did drastically affect the VLPs' internalization ability into Sf9 cells. Homology-based modelling of the MrNV capsid with other icosahedral capsid models revealed that this chymotrypsin-sensitive C-terminal domain was not only exposed on the capsid surface, but also constituted the core of the viral capsid protrusion. These results therefore suggest the importance of the C-terminal domain as a structure for targeted cell interaction which is presumably localized at the protruding domain. This work thus provided the functional insights into the role of the MrNV C-terminal domain in viral entry into Sf9 cells and lead to the development of strategies in combatting MrNV infection in susceptible cells.