The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches

Abstract As a result of smallpox immunization programs that ended more than 40 years ago, a significant portion of the world's population is not immune. Moreover, due to the lack of anti‐monkeypox drugs and vaccines against monkeypox, the spread of this virus may be the beginning of another cha...

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Main Authors: Sadeq Shabani, Mohsen Rashidi, Shakila Radgoudarzi, Ali Jebali
Format: Article
Language:English
Published: Wiley 2023-04-01
Series:Immunity, Inflammation and Disease
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Online Access:https://doi.org/10.1002/iid3.834
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author Sadeq Shabani
Mohsen Rashidi
Shakila Radgoudarzi
Ali Jebali
author_facet Sadeq Shabani
Mohsen Rashidi
Shakila Radgoudarzi
Ali Jebali
author_sort Sadeq Shabani
collection DOAJ
description Abstract As a result of smallpox immunization programs that ended more than 40 years ago, a significant portion of the world's population is not immune. Moreover, due to the lack of anti‐monkeypox drugs and vaccines against monkeypox, the spread of this virus may be the beginning of another challenge. In this study, novel antibodies against monkeypox virus were modeled based on a heavy chain of human antibody and a small peptide fragment. Docking of modeled antibodies with C19L protein showed the range of docking energy, and root‐mean‐square deviation (RMSD) was from −124 to −154 kcal/mL and 4–6 angstrom, respectively. Also, docking of modeled antibodies‐C19L complex with gamma Fc receptor type I illustrated the range of docking energy, and RMSD was from −132 to −155 kcal/ml and 5–7 angstrom, respectively. Moreover, molecular dynamics simulation showed that antibody 62 had the highest stability with the lowest energy level and RMSD. Interestingly, no modeled antibodies had immunogenicity, allergenicity, and toxicity. Although all of them had good stability, only antibodies 25, 28, 54, and 62 had a half‐life of >10 h. Moreover, the interaction between C19L protein and anti‐C19L antibodies (wild‐type and synthetic) was evaluated by the SPR method. We found that KD in synthetic antibodies was lower than wild antibody. In terms of δH°, TδS°, and δG°, the results were consistent with binding parameters. Here, the lowest value of thermodynamic parameters was obtained for antibody 62. These data show that the synthetic antibodies, especially antibody 62, had a higher affinity than the wild‐type antibody.
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spelling doaj-art-e15d7190f6924e15a3e2d0579eccfd2a2025-08-20T03:06:26ZengWileyImmunity, Inflammation and Disease2050-45272023-04-01114n/an/a10.1002/iid3.834The validation of artificial anti‐monkeypox antibodies by in silico and experimental approachesSadeq Shabani0Mohsen Rashidi1Shakila Radgoudarzi2Ali Jebali3Department of Biological Sciences Florida International University Miami Florida USADepartment Pharmacology, Faculty of Medicine Mazandaran University of Medical Sciences Sari IranI.M. Sechenov First Moscow State Medical University (Первый МГМУ им) Moscow RussiaDepartment of Medical Nanotechnology, Faculty of Advanced Sciences and Technology, Tehran Medical Science Islamic Azad University Tehran IranAbstract As a result of smallpox immunization programs that ended more than 40 years ago, a significant portion of the world's population is not immune. Moreover, due to the lack of anti‐monkeypox drugs and vaccines against monkeypox, the spread of this virus may be the beginning of another challenge. In this study, novel antibodies against monkeypox virus were modeled based on a heavy chain of human antibody and a small peptide fragment. Docking of modeled antibodies with C19L protein showed the range of docking energy, and root‐mean‐square deviation (RMSD) was from −124 to −154 kcal/mL and 4–6 angstrom, respectively. Also, docking of modeled antibodies‐C19L complex with gamma Fc receptor type I illustrated the range of docking energy, and RMSD was from −132 to −155 kcal/ml and 5–7 angstrom, respectively. Moreover, molecular dynamics simulation showed that antibody 62 had the highest stability with the lowest energy level and RMSD. Interestingly, no modeled antibodies had immunogenicity, allergenicity, and toxicity. Although all of them had good stability, only antibodies 25, 28, 54, and 62 had a half‐life of >10 h. Moreover, the interaction between C19L protein and anti‐C19L antibodies (wild‐type and synthetic) was evaluated by the SPR method. We found that KD in synthetic antibodies was lower than wild antibody. In terms of δH°, TδS°, and δG°, the results were consistent with binding parameters. Here, the lowest value of thermodynamic parameters was obtained for antibody 62. These data show that the synthetic antibodies, especially antibody 62, had a higher affinity than the wild‐type antibody.https://doi.org/10.1002/iid3.834anti‐monkeypox antibodyheavy chainin silicopeptide fragment
spellingShingle Sadeq Shabani
Mohsen Rashidi
Shakila Radgoudarzi
Ali Jebali
The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
Immunity, Inflammation and Disease
anti‐monkeypox antibody
heavy chain
in silico
peptide fragment
title The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
title_full The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
title_fullStr The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
title_full_unstemmed The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
title_short The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
title_sort validation of artificial anti monkeypox antibodies by in silico and experimental approaches
topic anti‐monkeypox antibody
heavy chain
in silico
peptide fragment
url https://doi.org/10.1002/iid3.834
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