scholarly journals Linear epitope mapping of peanut allergens demonstrates individualized and persistent antibody-binding patterns

2016 ◽  
Vol 138 (6) ◽  
pp. 1728-1730 ◽  
Author(s):  
Christian S. Hansen ◽  
Martin Dufva ◽  
Katrine L. Bøgh ◽  
Eric Sullivan ◽  
Jigar Patel ◽  
...  
2009 ◽  
Vol 395 (1) ◽  
pp. 100-107 ◽  
Author(s):  
Xiaojun Lu ◽  
Michael R. DeFelippis ◽  
Lihua Huang

HIV Protocols ◽  
2003 ◽  
pp. 293-308
Author(s):  
Lawrence D. Loomis-Price

Author(s):  
Tingting Li ◽  
Xiaojian Han ◽  
Yingming Wang ◽  
Chenjian Gu ◽  
Jianwei Wang ◽  
...  

AbstractThe spread of SARS-CoV-2 confers a serious threat to the public health without effective intervention strategies1–3. Its variant carrying mutated Spike (S) protein D614G (SD614G) has become the most prevalent form in the current global pandemic4,5. We have identified a large panel of potential neutralizing antibodies (NAbs) targeting the receptor-binding domain (RBD) of SARS-CoV-2 S6. Here, we focused on the top 20 potential NAbs for the mechanism study. Of them, the top 4 NAbs could individually neutralize both authentic SARS-CoV-2 and SD614G pseudovirus efficiently. Our epitope mapping revealed that 16/20 potent NAbs overlapped the same steric epitope. Excitingly, we found that one of these potent NAbs (58G6) exclusively bound to a linear epitope on S-RBD (termed as 58G6e), and the interaction of 58G6e and the recombinant ACE2 could be blocked by 58G6. We confirmed that 58G6e represented a key site of vulnerability on S-RBD and it could positively react with COVID-19 convalescent patients’ plasma. We are the first, as far as we know, to provide direct evidences of a linear epitope that can be recognized by a potent NAb against SARS-CoV-2 S-RBD. This study paves the way for the applications of these NAbs and the potential safe and effective vaccine design.


1996 ◽  
Vol 26 (6) ◽  
pp. 514-521 ◽  
Author(s):  
J. G. ROUTSIAS ◽  
A. G. TZIOUFAS ◽  
M. SAKARELLOS-DAITSIOTIS ◽  
C. SAKARELLOS ◽  
H. M. MOUTSOPOULOS

Blood ◽  
1996 ◽  
Vol 87 (7) ◽  
pp. 2702-2713 ◽  
Author(s):  
S Elliott ◽  
T Lorenzini ◽  
D Chang ◽  
J Barzilay ◽  
E Delorme ◽  
...  

We have isolated and mapped the rHuEPO epitopes for three noncompeting anti-EPO monoclonal antibodies (MoAbs). The MoAb 9G8A recognizes a linear epitope that includes amino acids 13, 16, and 17. MoAb F12 recognizes a conformational epitope that includes amino acids 31 through 33, 86 through 91, and 138. MoAb D11 recognizes a conformational epitope that includes amino acids 64 through 78 and 99 through 110. MoAb D11 neutralizes rHuEPO activity which suggests that its epitope may contain the receptor binding domain. Analysis of the effect of mutations on folding allowed the identification of buried residues, alpha-helical, and non alpha-helical regions. This data along with epitope mapping data of anti rHuEPO monoclonals was used to model rHuEPO protein structure. A model consistent with the data is a 4-helix bundle with short and long interconnecting loops.


2005 ◽  
Vol 6 (6) ◽  
pp. 3419-3424 ◽  
Author(s):  
Aren E. Gerdon ◽  
David W. Wright ◽  
David E. Cliffel

1997 ◽  
Vol 19 (1) ◽  
pp. 58-65 ◽  
Author(s):  
L D Loomis-Price ◽  
M Levi ◽  
P R Burnett ◽  
J E van Hamont ◽  
R A Shafer ◽  
...  

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