By understanding the structure of viral glycoproteins like HCMV gB and RABV-G, we can design next-generation vaccines that focus the immune response on neutralizing epitopes, avoiding the virus's evasion strategies.
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Are you currently facing long drug development cycles, challenges in rational drug design, and difficulty in overcoming immune evasion or drug resistance? Our One-Stop Glycan Crystal & Glycoprotein Crystal Analysis Services help you accelerate drug discovery by providing high-resolution insights into disease mechanisms through advanced structural and functional analysis techniques.
Glycoproteins are a class of proteins with attached glycans that play critical roles in a vast array of biological processes, from viral entry and immune recognition to cell-cell adhesion and protein quality control. Understanding the three-dimensional structure of these proteins is paramount for rational drug design. Creative Biolabs is a leader in applying structural biology to solve a wide range of biological challenges. Our expertise and advanced technology platform provide key advantages that accelerate your research and development. At Creative Biolabs, we believe that understanding a problem at the atomic level is the first step to a lasting solution. Our Glycoprotein Crystal Analysis Services provide you with the precise molecular blueprint of your target. Our service provides high-resolution insights into these complex molecules. Our process is designed to be a clear, step-by-step collaboration, delivering actionable data and structural insights. We provide you with the data, revealing hidden vulnerabilities in pathogens and disease-related proteins.
A high-resolution structure of a glycoprotein is not just a scientific curiosity; it is a critical tool for rational drug design. It allows researchers to visualize the active site of an enzyme (like α1,2-mannosidase), understand how a virus evades the immune system (e.g., the glycan shield on HCMV gB), or map the binding site for a neutralizing antibody. This knowledge moves drug discovery from a laborious, low-yield process of random screening to a targeted, high-efficiency approach. Creative Biolabs' service is a complete, end-to-end solution.
Fig.1 Detailed process for glycoprotein crystal analysis.
The applications of our service are vast and have the potential to revolutionize therapeutic development.
By understanding the structure of viral glycoproteins like HCMV gB and RABV-G, we can design next-generation vaccines that focus the immune response on neutralizing epitopes, avoiding the virus's evasion strategies.
Our service is crucial for mapping the binding sites of neutralizing antibodies. For example, understanding the bipartite epitope of the 523-11 antibody on RABV-G provides a blueprint for creating more potent and broadly neutralizing antibodies.
By visualizing the conformational flexibility of drug efflux pumps like P-gp, we can rationally design inhibitors that block their functions.
The literature details the groundbreaking discovery of the crystal structure of the human cytomegalovirus (HCMV) glycoprotein B (gB) ectodomain. This is the first time the atomic-level structure of a protein from this specific family of viruses, known as betaherpesviruses, has been determined. The study reveals that HCMV gB is a large, spike-like trimer that takes on a postfusion conformation. This structural similarity with glycoproteins from other herpesviruses, such as Herpes Simplex virus (HSV-1) and Epstein-Barr virus (EBV), officially classifies HCMV gB as a member of the class III viral fusogens, which are proteins responsible for facilitating a virus's merger with a host cell membrane. A key focus of the research is how the structure of HCMV gB compares to its HSV-1 and EBV counterparts. While all three share a similar overall architecture, the study highlights that each protein has a distinct domain arrangement. For instance, the way the domains are positioned relative to one another in the HCMV gB structure is different from how they are positioned in the HSV-1 and EBV structures. These subtle but significant differences are a form of structural plasticity, suggesting that although the proteins share a common function as fusogens, each virus has evolved to fine-tune its gB for virus-specific functional needs. The research also shows that HCMV gB is heavily coated in carbohydrate chains, or glycans, which act as a shield to help the virus evade the human immune system. This glycan layer is strategically placed to protect sites that would generate powerful neutralizing antibodies, while leaving other sites, which produce less effective antibodies, exposed to the immune system.
Fig.2 Comparative structures of gB from three different herpesviruses.1
We specialize in challenging targets. Our extensive experience with proteins like P-gp and viral glycoproteins, combined with advanced techniques such as co-crystallization with antibodies, allows us to overcome issues with stability and aggregation. We invite you to share the details of your protein, and our team will develop a tailored strategy.
The timeline is highly dependent on the protein's complexity. A straightforward project may be completed in as little as 12 weeks, while a more challenging target requiring extensive optimization could take longer. We provide a detailed project plan with estimated timelines after our initial consultation.
We strongly encourage it! Co-crystallization with a specific binder, like a neutralizing antibody, is a powerful strategy for stabilizing a protein and revealing its epitope at the atomic level, which can accelerate both vaccine and antibody development. Contact us to discuss how we can leverage your materials.
Atomic-level Insight
"Using Creative Biolabs' service in our research has significantly improved our understanding of viral immune evasion, allowing us to focus our vaccine development efforts on the most critical antigenic sites. The detailed report of the glycan shield was invaluable."- J**n, Intermediate researcher.
Solving the Solubility Challenge
"Using Creative Biolabs' service in our research has significantly improved our ability to work with a difficult-to-crystallize membrane protein. Their approach to stabilizing the protein for structural determination saved us months of trial-and-error."- M**k, Scientist.
To achieve your goals, you may require additional support beyond structural analysis. We offer a full suite of complementary services designed to provide a seamless workflow.
The structural elucidation of glycoproteins is no longer a scientific curiosity-it is a critical step towards solving significant clinical challenges. At Creative Biolabs, we are leveraging these precise, atomic-level insights to accelerate the discovery and development of breakthrough therapeutics. Our focus on structure-based design is the key to creating a new generation of medicines. Please contact us to inquire about more details.
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