TY - JOUR
T1 - Epitope-Analyzer
T2 - A structure-based webtool to analyze broadly neutralizing epitopes
AU - Montiel-Garcia, Daniel
AU - Rojas-Labra, Oscar
AU - Santoyo-Rivera, Nelly
AU - Reddy, Vijay S.
N1 - Publisher Copyright:
© 2022 Elsevier Inc.
PY - 2022/3
Y1 - 2022/3
N2 - The antigenic epitope regions of pathogens (e.g., viruses) are recognized by antibodies (Abs) and subsequently cleared by the host immune system, thereby protecting us from disease. Some of these epitopes are conserved among different variants or subgroups of pathogens (e.g., Influenza (FLU) viruses, Coronaviruses), hence can be targeted for potential broad-neutralization. Here we report a web-based tool, Epitope Analyzer (EA), that rapidly identifies conformational epitope and paratope residues in an antigen–antibody complex structure. Furthermore, the tool provides the ways and means to analyze broadly neutralizing epitopes by comparing the equivalent epitope residues in similar antigen structures. The similarity in the epitope residues between (multiple) pairs of similar antigen molecules suggest the presence of conserved epitopes that can be targeted by broadly neutralizing antibodies. These details can be used as a guide in developing effective treatments, such as the design of novel vaccines and formulation of cocktail of broadly neutralizing antibodies, against multiple variants or subgroups of viruses. The web application can be freely accessed from the URL, http://viperdb.scripps.edu/ea.php.
AB - The antigenic epitope regions of pathogens (e.g., viruses) are recognized by antibodies (Abs) and subsequently cleared by the host immune system, thereby protecting us from disease. Some of these epitopes are conserved among different variants or subgroups of pathogens (e.g., Influenza (FLU) viruses, Coronaviruses), hence can be targeted for potential broad-neutralization. Here we report a web-based tool, Epitope Analyzer (EA), that rapidly identifies conformational epitope and paratope residues in an antigen–antibody complex structure. Furthermore, the tool provides the ways and means to analyze broadly neutralizing epitopes by comparing the equivalent epitope residues in similar antigen structures. The similarity in the epitope residues between (multiple) pairs of similar antigen molecules suggest the presence of conserved epitopes that can be targeted by broadly neutralizing antibodies. These details can be used as a guide in developing effective treatments, such as the design of novel vaccines and formulation of cocktail of broadly neutralizing antibodies, against multiple variants or subgroups of viruses. The web application can be freely accessed from the URL, http://viperdb.scripps.edu/ea.php.
KW - Broadly neutralizing antibodies
KW - Epitope conservation
KW - Epitopes
KW - Paratopes
KW - Vaccine design
UR - http://www.scopus.com/inward/record.url?scp=85124328998&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85124328998&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2022.107839
DO - 10.1016/j.jsb.2022.107839
M3 - Article
C2 - 35134530
AN - SCOPUS:85124328998
SN - 1047-8477
VL - 214
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 1
M1 - 107839
ER -