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Sanyou's STAL helps researchers to explore the forefront of Life Sciences with high-impact literature publication
Time:2023.05.27 Author:Sanyou Bio From:Sanyou Bio

"Since the establishment of Super-Trillion Innovative Antibody Library (STAL), Sanyou has collaborated with or assisted scientists in publishing dozens of articles,of which 41 have a cumulative impact factor of 412.32, 14 papers have an impact factor greater than 10 and the  highest impact factor is 47.728.


We have made an inventory of some high-quality papers to demonstrate how the STAL help researchers to conduct in-depth studies and explore the forefront of life sciences."


Representative Paper


No.1

Title: Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study

-Journal: Science

-IF: 47.728

-PMID: 34554826

-Publication Date:2021.1

-Conclusion and Significance: Based on different epitopes, the authors divided 186 monoclonal antibodies that bind the receptor-binding domain (RBD) of SARS-CoV-2 from global sources into 7 categories, and analyzed the binding conformation and blocking neutralization effects of monoclonal antibodies from different categories.

-Contribution or Participation: The Collaborative institutions include the Centrer for Infectious Diseases and Vaccine Research in La Jolla Institute for Immunology, the Duke Human Vaccine Institute at Duke University,etc.Sanyou Biopharma is the joint signature party. Sanyou obtained antibodies targeting the Spike protein of different mutant strains through the screening of its super trillion antibody libraries and selected antibody molecules with the bestin vitroperformance for structural analysis and was selected as a typical type of antibody.

-Experimental Result Graph:


No.2

Title: Rational development of a human antibody cocktail that deploys multiple functions to confer Pan-SARS-CoVs protection

-Journal:Cell research

-IF:25.617

-PMID:33262452

-Publication Date: September 2021

-Conclusion and Significance: The authors obtained the antibody P17 with high blocking activity that specifically targets the RDB region and does not compete with the H014 antibody by screening the Sanyou Super-Trillion series Innovative Antibody Library. The preventive and therapeutic efficacy of the combined use of P17 and H014 was further verified byin vitroexperiments. Additionally, in terms of structure, through Cryo-EM, the authors analyzed the tertiary complex structure of the SARS-CoV-2 S trimer, P17 and H014, elucidating the synergy caused by the different epitopes between the two effects.

-Contribution or Participation: The collaborative institutions include National Clinical Research Center for Infectious Diseases, Key Laboratory of Infection and Immunity at the Chinese Academy of Sciences, and the Institute of Microbiology and Epidemiology at the Academy of Military Medical Sciences,etc. Sanyou is the co-first author and co-corresponding author. The P17 antibody was screened through Sanyou’s Super-Trillion series Innovative Antibody Library (Fully human naïve antibody library, ST-ST-HuNAL, Fab format). The neutralizing effect of its high affinity and high-blocking effect was determined through Sanyou'sin vitroefficacy platform, which assisted the discovery and identification of COVID-19 antibodies.

-Experimental Result Graph:


No.3

Title: An Engineered IgG–VHH Bispecific Antibody against SARS-CoV-2 and Its Variants

-Journal:Small Method

-IF:14.188

-PMID:36300882

-Publication Date:2022.12

-Conclusion and Significance: The authors initially screened a fully human antibody R15-F7, and a humanized nanobody P14-F8-35, as the raw materials of the bispecific antibody.In vitrofunctional experiments confirmed the strong affinity and blocking activity of the two, and verified the epitope differences between the two through epitope competition. Subsequently, the configuration of the bispecific antibody, SYZJ001, was determined by design, and thein vitroaffinity and blocking activity were verified to be superior to those of the two monoclonal antibodies. The pharmacokinetic studies in mice also indicated a good half-life of the bispecific antibody. Affinity experiments on different mutant strains showed a broad-spectrum blocking effect of the bispecific antibody. Animal experiments further demonstrated the excellent therapeutic efficacy of the bispecific antibody.

-Contribution or Participation: The collaborative institutions include the Institute of Microbiology and Epidemiology at the Academy of Military Medical Sciences,etc. Sanyou is the co-first author and co-corresponding author. Both the humanized nanobody, P14-F8-35 and the fully human antibody R15-F7, are neutralizing antibodies screened from Sanyou’s Super-Trillion series Innovative Antibody Library (Fully human naïve antibody library and alpaca trillion antibody library). Furthermore, the configuration design and functional validation of the bispecific antibody were also completed by Sanyou’s platform, which provided sufficient raw materials for the structure analysis of the complex.

-Experimental Result Graph:



Paper List