dc.contributor.author |
Somrit M. |
|
dc.contributor.author |
Watthammawut A. |
|
dc.contributor.author |
Chotwiwatthanakun C. |
|
dc.contributor.author |
Ounjai P. |
|
dc.contributor.author |
Suntimanawong W. |
|
dc.contributor.author |
Weerachatyanukul W. |
|
dc.date.accessioned |
2021-04-05T03:22:34Z |
|
dc.date.available |
2021-04-05T03:22:34Z |
|
dc.date.issued |
2017 |
|
dc.identifier.issn |
1681702 |
|
dc.identifier.other |
2-s2.0-84992166449 |
|
dc.identifier.uri |
https://ir.swu.ac.th/jspui/handle/123456789/13167 |
|
dc.identifier.uri |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84992166449&doi=10.1016%2fj.virusres.2016.09.017&partnerID=40&md5=da5a0f7085439faf0471a76389b8d021 |
|
dc.description.abstract |
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. © 2016 Elsevier B.V. |
|
dc.subject |
chymotrypsin |
|
dc.subject |
Article |
|
dc.subject |
carboxy terminal sequence |
|
dc.subject |
cell interaction |
|
dc.subject |
controlled study |
|
dc.subject |
flow cytometry |
|
dc.subject |
insect cell culture |
|
dc.subject |
Macrobrachium rosenbergii |
|
dc.subject |
Nodaviridae |
|
dc.subject |
nonhuman |
|
dc.subject |
priority journal |
|
dc.subject |
protein hydrolysis |
|
dc.subject |
SF9 cell line |
|
dc.subject |
shrimp |
|
dc.subject |
virus attachment |
|
dc.subject |
virus capsid |
|
dc.subject |
virus entry |
|
dc.subject |
virus like agent |
|
dc.subject |
amino acid sequence |
|
dc.subject |
animal |
|
dc.subject |
chemistry |
|
dc.subject |
host pathogen interaction |
|
dc.subject |
metabolism |
|
dc.subject |
molecular model |
|
dc.subject |
Nodaviridae |
|
dc.subject |
Palaemonidae |
|
dc.subject |
physiology |
|
dc.subject |
protein conformation |
|
dc.subject |
protein domain |
|
dc.subject |
Sf9 cell line |
|
dc.subject |
ultrastructure |
|
dc.subject |
virology |
|
dc.subject |
virus assembly |
|
dc.subject |
virus capsid |
|
dc.subject |
Amino Acid Sequence |
|
dc.subject |
Animals |
|
dc.subject |
Capsid |
|
dc.subject |
Flow Cytometry |
|
dc.subject |
Host-Pathogen Interactions |
|
dc.subject |
Models, Molecular |
|
dc.subject |
Nodaviridae |
|
dc.subject |
Palaemonidae |
|
dc.subject |
Protein Conformation |
|
dc.subject |
Protein Interaction Domains and Motifs |
|
dc.subject |
Sf9 Cells |
|
dc.subject |
Virus Assembly |
|
dc.subject |
Virus Attachment |
|
dc.subject |
Virus Internalization |
|
dc.title |
C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization |
|
dc.type |
Article |
|
dc.rights.holder |
Scopus |
|
dc.identifier.bibliograpycitation |
Virus Research. Vol 227, (2017), p.41-48 |
|
dc.identifier.doi |
10.1016/j.virusres.2016.09.017 |
|