Viral Protein Structure Detection
To understand the mechanism of virus infection for potential drug target discovery and structure-based drug design, it is essential to determine the three-dimensional (3D) structure of proteins. Besides cryo-EM, we also offer two other major techniques commonly used for macromolecular structure determination, including X-ray crystallography and nuclear magnetic resonance (NMR). Similar to cryo-EM, the other two approaches can be used to determine the structure of a protein or complexes at atomic or near-atomic resolution. Furthermore, they can also resolve the structure of isolated proteins or complexes in isolated states. As an international contract research organization (CRO) providing viral proteomic, metabolomic and other analysis services, we can offer these major techniques for structural determination of viral structural proteins/non-structural proteins, antigen-antibody complexes as well as host proteins. Notably, we also provide protein expression and purification solutions, which greatly facilitate researchers to obtain sufficient quantities of proteins for structural studies.
Service offering
For the last decades, X-ray crystallography has remained the most powerful approach for determining virus structures at atomic resolution. Information provided by the method has deeply and extensively changed our view of the viral world. In turn, the ever-increasing studies of the complexity and size of the virus structures greatly promote the methodological and conceptual developments of X-ray crystallography. Based on a professional team of scientists and years of experience in crystallography services, Creative Proteomics is committed to providing custom X-ray crystallography services for virus research. Our service can help customers to investigate the individual protein crystal structure as well as protein-protein complexes.
Fig1. Viral capsid structure obtained by X-ray crystallography. (A) Poliovirus capsid with T53 symmetry. (B) Hepatitis B virus capsid with T54 symmetry. (Ryu, W. S., 2016)
Recent advances in cryo-electron microscopy (cryo-EM) sample preparation, microscopy and detector technology, automated data collection, and image processing have made it possible to achieve near-atomic resolution in a reproducible manner. Cryo-electron microscopy includes two major 3D cryo-EM analysis strategies, namely single particle analysis (SPA) and cryo-electron tomography (cryo-ET). Among them, SPA is increasingly becoming an essential technique for the structural determination of viral protein and complexes.
The cryo-EM has been applied to help in to help understand the aspects of virus biology, including,
- Analyses of glycoproteins of enveloped viruses, such as SIV and HIV-1.
- Analyses of the retroviral capsid during viral assembly and maturation.
- Analyses of the virus intasome.
Fig2. Cross-section and two cut-away views of a hepatitis B virus (HBV) virion was obtained by cryo-electron microscope. (Ryu, W. S., 2016)
Over the past years, supported by the state-of-the-art nuclear magnetic resonance (NMR) spectroscopy platform, Creative Proteomics has provided customers with high-quality three-dimensional structure analysis services of viruses. Our solution NMR and solid-state NMR services can help customers to investigate the structures and functions of viral transmembrane proteins, the dynamic and inhibition properties of membrane proteins, and the path of viral proteins through their interactions and maturation steps during the viral life cycle. Importantly, our experienced and professional scientists are capable of providing the best strategies according to our global customers' specific project needs.
If you are interested in our services, please don't hesitate to Contact us. We are glad to cooperate with you and witness your success!
References
- Mak, J., & De Marco, A. (2018). "Recent advances in retroviruses via cryo-electron microscopy." Retrovirology, 15(1), 1-10.
- Ryu, W. S. (2016). "Molecular virology of human pathogenic viruses." Academic Press.
* For research use only.
