Isolation and characterization of a human antibody fragment specific for Ts1 toxin from Tityus serrulatus scorpion

2011 ◽  
Vol 139 (1-2) ◽  
pp. 73-79 ◽  
Author(s):  
Itzel Amaro ◽  
Lidia Riaño-Umbarila ◽  
Baltazar Becerril ◽  
Lourival D. Possani
Peptides ◽  
2016 ◽  
Vol 80 ◽  
pp. 9-17 ◽  
Author(s):  
Felipe Augusto Cerni ◽  
Manuela Berto Pucca ◽  
Fernanda Gobbi Amorim ◽  
Karla de Castro Figueiredo Bordon ◽  
Julien Echterbille ◽  
...  

Toxicon ◽  
2020 ◽  
Vol 177 ◽  
pp. S53
Author(s):  
Letícia Acosta ◽  
Karla de Castro Figueiredo Bordon ◽  
Iara Aimê Cardoso ◽  
Carem Gledes Vargas Rechia ◽  
Jan Tytgat ◽  
...  

2006 ◽  
Vol 78 (13) ◽  
pp. 4501-4508 ◽  
Author(s):  
Ruth C. Ladenson ◽  
Dan L. Crimmins ◽  
Yvonne Landt ◽  
Jack H. Ladenson

Toxins ◽  
1978 ◽  
pp. 609-618
Author(s):  
ALEJANDRO C. ALAGÓN ◽  
LOURIVAL D. POSSANI ◽  
BRUCE W. ERICKSON

1994 ◽  
Vol 1199 (1) ◽  
pp. 69-75 ◽  
Author(s):  
Eliane C. Arantes ◽  
Francisco Riccioppo Neto ◽  
Suely V. Sampaio ◽  
Carlos A. Vieira ◽  
JoséR. Giglio

Author(s):  
Leo Hanke ◽  
Laura Vidakovics Perez ◽  
Daniel J. Sheward ◽  
Hrishikesh Das ◽  
Tim Schulte ◽  
...  

AbstractSARS-CoV-2 is the etiologic agent of COVID-19, currently causing a devastating pandemic for which pharmacological interventions are urgently needed. The virus enters host cells through an interaction between the spike glycoprotein and the angiotensin converting enzyme 2 (ACE2) receptor. Directly preventing this interaction presents an attractive possibility for suppressing SARS-CoV-2 replication. Here we report the isolation and characterization of an alpaca-derived single domain antibody fragment, Ty1, that specifically targets the receptor binding domain (RBD) of the SARS-CoV-2 spike, directly preventing ACE2 engagement. The nanobody binds with high affinity in the low nM range to the RBD, occluding ACE2. A cryo-electron microscopy structure of the bound complex at 2.9 Å resolution reveals that Ty1 binds to an epitope on the RBD accessible in both the ‘up’ and ‘down’ conformations and that Ty1 sterically hinders RBD-ACE2 binding. This 12.8 kDa nanobody does not need an Fc domain to neutralize SARS-CoV-2, and can be expressed in high quantities in bacteria, presenting opportunities for manufacturing at scale. Ty1 is therefore an excellent candidate as an intervention against COVID-19.


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