Publication: C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization
Issued Date
2017-01-02
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ISSN
18727492
01681702
01681702
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2-s2.0-84992166449
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Mahidol University
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SCOPUS
Bibliographic Citation
Virus Research. Vol.227, (2017), 41-48
Suggested Citation
Monsicha Somrit, Atthaboon Watthammawut, Charoonroj Chotwiwatthanakun, Puey Ounjai, Wanida Suntimanawong, Wattana Weerachatyanukul C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization. Virus Research. Vol.227, (2017), 41-48. doi:10.1016/j.virusres.2016.09.017 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/42018
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Title
C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization
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Abstract
© 2016 Elsevier B.V. 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.
