Single Particle Cryo-EM for Coronavirus-like Particle
Because viral particles are generally small (between tens and hundreds
of nanometers in diameter), the traditional optical microscope is difficult
to meet the needs of their morphological observation, which makes high-resolution
electron microscopy (EM) an important means of current virology research.
It can be utilized to study the structure and surface composition of viral
particles, and the viral structure information with the near-atomic resolution
is useful in the discovery and design of vaccines and antiviral drugs.
Leveraging advanced cryo-electron microscopy (cryo-EM) imaging platform
and powerful data processing software, Creative Biostructure supports the observation and characterization of coronavirus-like
particles and/or the complex of virus-like particle (VLP) with other biomolecule
using single-particle cryo-EM technology.
Application of Single Particle Cryo-EM in Virology
Cryo-EM has been utilized to study virus morphology for decades, resolving
the three-dimensional (3D) structure of viruses such as Zika, Ebola, and
coronavirus. Due to the tremendous progress of electronic detectors and
image processing technology in recent years, cryo-EM single-particle analysis
has gradually become one of the main approaches for determining the 3D
structure of biological samples, especially an essential tool in the study
of virus structure and dynamics. In the early stage of novel coronavirus
(SARS-CoV-2) outbreak, scientists obtain significant advances in the structure
and behavior of novel coronavirus using this technology, including a series
of biophysical information of viral particles and the process of viral
infection.
Some studies on the structure of complexes of viral particles and antibodies
are essential to better understand the molecular mechanism behind antigen-antibody
interactions. Moreover, cryo-EM single-particle analysis technology is
increasingly used in epitope mapping to define specific binding sites.
These studies accelerate the discovery and development of more specific
and effective vaccines or antiviral therapeutics.
Figure 1. Coronavirus structure mapped with cryo-EM.
Our Single Particle Cryo-EM Services for Coronavirus-like Particle
For coronaviruses without strong infectivity, we can support the use of
this technology to obtain the biophysical information of the virus, including
its morphology and outer-shell proteins, as well as to observe the interaction
mode of viral particles and receptors. Considering safety issues,
we do not support the observation of native coronavirus samples that can
cause large-scale human infections, such as SARS-CoV and novel coronavirus.
We can use cryo-EM single-particle analysis technology to visualize coronavirus-like
particles. VLP is a multi-protein structure assembled from native viral
structural proteins. It has the structure and conformation of native viruses,
but does not contain any genetic material, so it is non-infectious and
easy to handle. VLP is becoming an increasingly common tool for drug delivery
system development, antibody screening, and
vaccine development
. The service allows the 3D structure reconstruction of your coronavirus-like
particles to characterize these nanoscale VLPs. To expand other applications,
we can also use this technology to observe the interaction between VLP
and other biomolecules (such as neutralizing antibody). We can design and
develop custom coronavirus-like particles and provide
off-the-shelf VLP products of the family Coronaviridae
.
Creative Biostructure has been optimizing our cryo-EM single-particle analysis technology.
We have extensive experience in sample preparation, imaging, data collection,
data processing, and structural analysis. In addition to the visualization
of coronavirus-like particles, we provide specialized
services for the 3D structural analysis of proteins involved in coronavirus
infection
. Please feel free to contact us for more details.
Contact us to discuss your project!
Reference
-
Wrapp D.; et al . Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science . 2020, 367(6483): 1260-1263.
