"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
