2016
DOI: 10.1002/btpr.2409
|View full text |Cite
|
Sign up to set email alerts
|

Virus‐like particle of Macrobrachium rosenbergii nodavirus produced in Spodoptera frugiperda (Sf9) cells is distinctive from that produced in Escherichia coli

Abstract: Macrobrachium rosenbergii nodavirus (MrNV) is a virus native to giant freshwater prawn. Recombinant MrNV capsid protein has been produced in Escherichia coli, which self-assembled into virus-like particles (VLPs). However, this recombinant protein is unstable, degrading and forming heterogenous VLPs. In this study, MrNV capsid protein was produced in insect Spodoptera frugiperda (Sf9) cells through a baculovirus system. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) revealed that the… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

3
25
0

Year Published

2017
2017
2024
2024

Publication Types

Select...
4
2
2
1

Relationship

3
6

Authors

Journals

citations
Cited by 24 publications
(28 citation statements)
references
References 33 publications
3
25
0
Order By: Relevance
“…Moreover, high pH (2–12) and thermal (up to 45°C) stability were reported for recombinant MrNv‐VLPs produced in a eukaryotic system (Kueh et al . ). Other recombinant VLPs structures have been produced in eukaryotic systems (Lin et al .…”
Section: Applications Of Encapsulation Technology In Aquaculture – Camentioning
confidence: 97%
See 1 more Smart Citation
“…Moreover, high pH (2–12) and thermal (up to 45°C) stability were reported for recombinant MrNv‐VLPs produced in a eukaryotic system (Kueh et al . ). Other recombinant VLPs structures have been produced in eukaryotic systems (Lin et al .…”
Section: Applications Of Encapsulation Technology In Aquaculture – Camentioning
confidence: 97%
“…) and eukaryotic (Kueh et al . ) systems and proved the capability of VLPs in packaging both RNA and DNA molecules. Moreover, high pH (2–12) and thermal (up to 45°C) stability were reported for recombinant MrNv‐VLPs produced in a eukaryotic system (Kueh et al .…”
Section: Applications Of Encapsulation Technology In Aquaculture – Camentioning
confidence: 99%
“…Apart from the MrNV VLPs produced in E. coli, we have also produced the MrNV capsid protein in Sf9 cells through baculovirus expression system (Kueh et al, 2017). This eukaryotic produced MrNV capsid protein self-assembles into VLPs significantly larger than their prokaryotic counterparts.…”
Section: Virus-like Particlesmentioning
confidence: 99%
“…Recombinant MrNV capsid protein produced in Escherichia coli and Spodoptera frugiperda (both Sf9 and Sf21) assembles into icosahedral virus-like particles (VLPs) although these were found to be morphologically different under transmission electron microscopy analysis [14,15]. Negative stained VLPs expressed in E. coli and Sf9 were measured to have diameters of ~30 and 40 nm, respectively [14,15]. The self-assembly/disassembly capability of the MrNV capsid protein has been exploited to develop nano-carriers for DNA and double stranded RNA [16,17].…”
Section: Introductionmentioning
confidence: 99%