Fabrication of virus-like particles with strip-pattern surface: A two-step self-assembly approach

2017 ◽  
Vol 28 (4) ◽  
pp. 839-844 ◽  
Author(s):  
Shuo Zhang ◽  
Chun-Hua Cai ◽  
Zhou Guan ◽  
Jia-Ping Lin ◽  
Xing-Yu Zhu
Keyword(s):  
Self Assembly ◽  
Virus Like Particles ◽  
Strip Pattern

Efficient self-assembly of human papillomavirus type 16 L1 and L1-L2 into virus-like particles.

1993 ◽  
Vol 67 (12) ◽  
pp. 6929-6936 ◽  
Author(s):  
R Kirnbauer ◽  
J Taub ◽  
H Greenstone ◽  
R Roden ◽  
M Dürst ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Self Assembly ◽  
Virus Like Particles ◽  
Human Papillomavirus Type 16

scholarly journals Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System

2021 ◽  
Vol 22 (6) ◽  
pp. 3098
Author(s):  
Aleksander Strugała ◽  
Jakub Jagielski ◽  
Karol Kamel ◽  
Grzegorz Nowaczyk ◽  
Marcin Radom ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Mosaic Virus ◽  
Capsid Protein ◽  
Self Assembly ◽  
Environmental Changes ◽  
Expression System ◽  
Brome Mosaic Virus ◽  
Virus Like Particles ◽  
Assembly Principles ◽  
The Impact

Virus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete. VLP formation is governed by two types of interactions: protein–cargo and protein–protein. These interactions can be modulated by the physicochemical properties of the surroundings. Here, we used brome mosaic virus (BMV) capsid protein produced in an E. coli expression system to study the impact of ionic strength, pH and encapsulated cargo on the assembly of VLPs and their features. We showed that empty VLP assembly strongly depends on pH whereas ionic strength of the buffer plays secondary but significant role. Comparison of VLPs containing tRNA and polystyrene sulfonic acid (PSS) revealed that the structured tRNA profoundly increases VLPs stability. We also designed and produced mutated BMV capsid proteins that formed VLPs showing altered diameters and stability compared to VLPs composed of unmodified proteins. We also observed that VLPs containing unstructured polyelectrolyte (PSS) adopt compact but not necessarily more stable structures. Thus, our methodology of VLP production allows for obtaining different VLP variants and their adjustment to the incorporated cargo.

scholarly journals Self-Assembly and Release of Peste des Petits Ruminants Virus-Like Particles in an Insect Cell-Baculovirus System and Their Immunogenicity in Mice and Goats

PLoS ONE ◽  
2014 ◽  
Vol 9 (8) ◽  
pp. e104791 ◽  
Author(s):  
Wenchao Li ◽  
Hongyan Jin ◽  
Xiukun Sui ◽  
Zhanzhong Zhao ◽  
Chenghuai Yang ◽  
...  
Keyword(s):  
Self Assembly ◽  
Insect Cell ◽  
Peste Des Petits Ruminants ◽  
Virus Like Particles ◽  
Baculovirus System

RNA-assisted self-assembly of monomeric antigens into virus-like particles as a recombinant vaccine platform

Biomaterials ◽  
2021 ◽  
pp. 120650
Author(s):  
Beom Jeung Hwang ◽  
Yohan Jang ◽  
Soon Bin Kwon ◽  
Ji Eun Yu ◽  
Jongkwan Lim ◽  
...  
Keyword(s):  
Self Assembly ◽  
Recombinant Vaccine ◽  
Vaccine Platform ◽  
Virus Like Particles

scholarly journals Conserved Motifs within Ebola and Marburg Virus VP40 Proteins Are Important for Stability, Localization, and Subsequent Budding of Virus-Like Particles

2009 ◽  
Vol 84 (5) ◽  
pp. 2294-2303 ◽  
Author(s):  
Yuliang Liu ◽  
Luis Cocka ◽  
Atsushi Okumura ◽  
Yong-An Zhang ◽  
J. Oriol Sunyer ◽  
...  
Keyword(s):  
Self Assembly ◽  
Mammalian Cells ◽  
Ebola Virus ◽  
Intracellular Localization ◽  
Gel Filtration ◽  
Point Mutations ◽  
Marburg Virus ◽  
Structure Stability ◽  
Wild Type ◽  
Virus Like Particles

ABSTRACT The filovirus VP40 protein is capable of budding from mammalian cells in the form of virus-like particles (VLPs) that are morphologically indistinguishable from infectious virions. Ebola virus VP40 (eVP40) contains well-characterized overlapping L domains, which play a key role in mediating efficient virus egress. L domains represent only one component required for efficient budding and, therefore, there is a need to identify and characterize additional domains important for VP40 function. We demonstrate here that the 96LPLGVA101 sequence of eVP40 and the corresponding 84LPLGIM89 sequence of Marburg virus VP40 (mVP40) are critical for efficient release of VP40 VLPs. Indeed, deletion of these motifs essentially abolished the ability of eVP40 and mVP40 to bud as VLPs. To address the mechanism by which the 96LPLGVA101 motif of eVP40 contributes to egress, a series of point mutations were introduced into this motif. These mutants were then compared to the eVP40 wild type in a VLP budding assay to assess budding competency. Confocal microscopy and gel filtration analyses were performed to assess their pattern of intracellular localization and ability to oligomerize, respectively. Our results show that mutations disrupting the 96LPLGVA101 motif resulted in both altered patterns of intracellular localization and self-assembly compared to wild-type controls. Interestingly, coexpression of either Ebola virus GP-WT or mVP40-WT with eVP40-ΔLPLGVA failed to rescue the budding defective eVP40-ΔLPLGVA mutant into VLPs; however, coexpression of eVP40-WT with mVP40-ΔLPLGIM successfully rescued budding of mVP40-ΔLPLGIM into VLPs at mVP40-WT levels. In sum, our findings implicate the LPLGVA and LPLGIM motifs of eVP40 and mVP40, respectively, as being important for VP40 structure/stability and budding.

scholarly journals Expression and self-assembly of Heterocapsa circularisquama RNA virus-like particles synthesized in Pichia pastoris

2012 ◽  
Vol 57 (25) ◽  
pp. 3288-3293 ◽  
Author(s):  
YuanZheng Wu ◽  
Wonduck Kim ◽  
Si-Wouk Kim ◽  
Chi-Yong Eom ◽  
HeTong Yang ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Self Assembly ◽  
Rna Virus ◽  
Virus Like Particles ◽  
Heterocapsa Circularisquama

Mechanism and controlled purification of self-assembly virus like particles in bioprocess

2008 ◽  
Vol 136 ◽  
pp. S203
Author(s):  
Jingxiu Bi ◽  
Zhiguo Su ◽  
Keith King ◽  
Anton Middelberg
Keyword(s):  
Self Assembly ◽  
Virus Like Particles
Sign in / Sign up

Export Citation Format

Share Document