scholarly journals Peer Review #2 of "High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA (v0.1)"

2018 ◽  
Keyword(s):  
High Resolution ◽  
Peer Review ◽  
Crystal Structures ◽  
Receptor Binding ◽  
Clostridium Botulinum ◽  
Botulinum Neurotoxin ◽  
Binding Domain ◽  
Receptor Binding Domain

scholarly journals Structural insights into the functional role of the Hcn sub-domain of the receptor-binding domain of the botulinum neurotoxin mosaic serotype C/D

Biochimie ◽  
2013 ◽  
Vol 95 (7) ◽  
pp. 1379-1385 ◽  
Author(s):  
Yanfeng Zhang ◽  
Anna S. Gardberg ◽  
Thomas E. Edwards ◽  
Banumathi Sankaran ◽  
Howard Robinson ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Functional Role ◽  
Botulinum Neurotoxin ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Structural Insights

scholarly journals Computational Prediction of the Epitopes of HA1 Protein of Influenza Viruses to its Neutralizing Antibodies

Antibodies ◽  
2018 ◽  
Vol 8 (1) ◽  
pp. 2
Author(s):  
Xiaoyan Zeng ◽  
Fiona Legge ◽  
Chao Huang ◽  
Xiao Zhang ◽  
Yongjun Jiao ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Crystal Structures ◽  
Receptor Binding ◽  
Neutralizing Antibodies ◽  
Computational Prediction ◽  
Binding Domain ◽  
Influenza Viruses ◽  
New Method ◽  
Receptor Binding Domain ◽  
Antibody Recognition

In this work, we have used a new method to predict the epitopes of HA1 protein of influenza virus to several antibodies HC19, CR9114, BH151 and 4F5. While our results reproduced the binding epitopes of H3N2 or H5N1 for the neutralizing antibodies HC19, CR9114, and BH151 as revealed from the available crystal structures, additional epitopes for these antibodies were also suggested. Moreover, the predicted epitopes of H5N1 HA1 for the newly developed antibody 4F5 are located at the receptor binding domain, while previous study identified a region 76-WLLGNP-81 as the epitope. The possibility of antibody recognition of influenza virus via different mechanism by binding to different epitopes of an antigen is also discussed.

scholarly journals Botulinum Neurotoxin Devoid of Receptor Binding Domain Translocates Active Protease

2008 ◽  
Vol 4 (12) ◽  
pp. e1000245 ◽  
Author(s):  
Audrey Fischer ◽  
Darren J. Mushrush ◽  
D. Borden Lacy ◽  
Mauricio Montal
Keyword(s):  
Receptor Binding ◽  
Botulinum Neurotoxin ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Active Protease

scholarly journals High resolution linear epitope mapping of the receptor binding domain of SARS-CoV-2 spike protein in COVID-19 mRNA vaccine recipients.

2021 ◽  
Author(s):  
Yuko Nitahara ◽  
Yu Nakagama ◽  
Natsuko Kaku ◽  
Katherine Candray ◽  
Yu Michimuko ◽  
...  
Keyword(s):  
High Resolution ◽  
Receptor Binding ◽  
Messenger Rna ◽  
Natural Infection ◽  
Neutralizing Antibody ◽  
Binding Domain ◽  
Spike Protein ◽  
Linear Epitope ◽  
Receptor Binding Domain ◽  
Population Immunity

The prompt rollout of the coronavirus disease (COVID-19) messenger RNA (mRNA) vaccine facilitated population immunity, which shall become more dominant than natural infection-induced immunity. At the beginning of the vaccine era, the initial epitope profile in naive individuals will be the first step to build an optimal host defense system towards vaccine-based population immunity. In this study, the high-resolution linear epitope profiles between Pfizer-BioNTech COVID-19 mRNA vaccine recipients and COVID-19 patients were delineated by using microarrays mapped with overlapping peptides of the receptor binding domain (RBD) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein. The vaccine-induced antibodies targeting RBD had broader distribution across the RBD than that induced by the natural infection. The relatively lower neutralizing antibody titers observed in vaccine-induced sera could attribute to less efficient epitope selection and maturation of the vaccine-induced humoral immunity compared to the infection-induced. Furthermore, additional mutation panel assays showed that the vaccine-induced rich epitope variety targeting the RBD may aid antibodies to escape rapid viral evolution, which could grant an advantage to the vaccine immunity.

High-Resolution NMR Structure of the Chemically-Synthesized Melanocortin Receptor Binding Domain AGRP(87−132) of the Agouti-Related Protein†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (51) ◽  
pp. 15520-15527 ◽  
Author(s):  
Joseph C. McNulty ◽  
Darren A. Thompson ◽  
Kimberly A. Bolin ◽  
Jill Wilken ◽  
Gregory S. Barsh ◽  
...  
Keyword(s):  
High Resolution ◽  
Receptor Binding ◽  
Binding Domain ◽  
Nmr Structure ◽  
Melanocortin Receptor ◽  
Receptor Binding Domain ◽  
Related Protein ◽  
High Resolution Nmr ◽  
Agouti Related Protein

scholarly journals High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4552 ◽  
Author(s):  
Jonathan R. Davies ◽  
Gavin S. Hackett ◽  
Sai Man Liu ◽  
K. Ravi Acharya
Keyword(s):  
Receptor Binding ◽  
Clostridium Botulinum ◽  
Toxin Production ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Crystal Forms ◽  
Multiple Receptors ◽  
Botulinum Neurotoxins ◽  
Translocation Domain ◽  
Existing Structure

The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (HN) and a receptor-binding domain (HC). Here we report the crystal structure of HC/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our HC/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of HC/A1. This may have implications for receptor-binding and future recombinant toxin production.

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