Broad Neutralizing sdAb Discovery Service
Broad neutralizing sdAb may aid the design and development of a vaccine capable of inducing a broadly protective antibody immune response. Based on our advanced platform and professional scientists, experts at Creative Biolabs focus on the discovery and development of broad neutralizing sdAb to meet the specific requirements of our customers all over the world.
Broad Neutralizing sdAb
As the harmful toxin and virus outbreak poses an enormous global risk, a more potent and broad neutralizing antibody vaccine is a certainly valuable tool for future consideration, especially as conserved epitopes are identified for cross-protective antibody responses against future pandemics. Due to common variations in the protein domains, some neutralizing sdAbs are often virus-specific and neutralize related viruses poorly. However, for efficient prevention of viral/toxin infections and cross-protection, simultaneous targeting of multiple epitopes or binding a conserved core structure is a powerful strategy. The generated broad neutralizing sdAb opens possibilities to achieve “best-in-class” and broader neutralization capacity for cross-neutralizing related toxins and viruses. Broad neutralizing sdAb can alter the course of infection in the infected host supporting toxin or virus clearance and protect an uninfected host that is exposed to a broad panel from different subtypes of virus or related toxin. Hence, these best broad neutralizing sdAb candidates may be served as useful therapeutics to offer broad protection against many variants and subtypes of viruses or toxins and to prevent and/or treat related diseases.
Fig.1 sdAb binding to a broadly conserved epitope. (Wrapp, 2020)
Broad Neutralizing sdAb Discovery and Development
The broad neutralizing sdAb comes into the focus of research and is expected to have distinct and superior biophysical and binding properties compared to conventional antibodies. For clinical applications, the effects of these antibodies could be related to their small size (~15 kDa) with full antigen-binding capacity, which allows a more extensive range of interactions with the neutralizing epitopes of protein than conventional antibodies. In particular, sdAb is stable, and the convex shape allows sdAb to preferentially bind to the clefts or cavities of protein, which are frequently inaccessible to traditional antibody formats. sdAb has sufficient inherent solubility/stability to be functional in antigen-binding and extensive sequence homology to human VH.
Combination of one-stop solutions for sdAb development and the strategy of determination of broad neutralizing sdAb, Creative Biolabs can generate a panel of broadly neutralizing sdAb-based molecules protective against broad virus subtypes. Broad neutralizing sdAb recognizing different epitopes with affinities in the low nanomolar range can be identified for all the viruses by a standardized in vitro neutralization assays and in vivo protection assays. Interestingly, the best sdAb candidates which are expressed as multimers (multivalent or multispecific), reveal a broader neutralizing activity and cross-protection capacity. They are much-improved neutralization of a broad panel of viruses carrying envelopes from different subtypes. So that, we can also provide multimeric sdAb constructs that have improved neutralization potency by fusion of sdAb with variable linker lengths. Overall, the high recombinant production yield combined with the broad neutralization capacity for soluble extracellular proteins, including toxins, cytokines, and blood clotting components, make these sdAbs new potential therapeutic candidates for developing effective prevention strategies and therapeutic applications.
Based on the broad neutralization together with the protective properties, the broad neutralizing sdAb is emerging as a new versatile reagent with greatly cross-protection potency for the diagnosis and the therapy of infectious diseases. Creative Biolabs is served as a leading company in the sdAb development market; our scientists possess the enriched experience to find the best-quality broad neutralizing sdAb for our customers all over the world. If you are interested in our service, please feel free to contact us for more details.
Reference
- Wrapp, D.; et al. Structural basis for potent neutralization of beta coronaviruses by single-domain camelid antibodies. Cell. 2020.
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