دورية أكاديمية

Design of antibody-reactive peptides from discontinuous parts of scorpion toxins.

التفاصيل البيبلوغرافية
العنوان: Design of antibody-reactive peptides from discontinuous parts of scorpion toxins.
المؤلفون: Alvarenga, L., Moreau, V., Felicori, L., Nguyen, Cong Tu, Duarte, C., Chavez-Olortegui, C., Molina, F., Martin-Eauclaire, M.-F., Granier, C.
المساهمون: EDF (EDF), Transfert Sol-Plante et Cycle des Eléments Minéraux dans les Ecosystèmes Cultivés (TCEM), Institut National de la Recherche Agronomique (INRA)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB), Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines Lyon (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)
المصدر: ISSN: 0264-410X.
بيانات النشر: HAL CCSD
Elsevier
سنة النشر: 2010
المجموعة: Université de Lyon: HAL
مصطلحات موضوعية: Amino Acid Sequence, Animals, Antibodies, Neutralizing, Antitoxins, Cross Reactions, Epitope Mapping, Epitopes, Mice, Inbred C57BL, Molecular Sequence Data, Neutralization Tests, Tertiary, Rabbits, Scorpion Venoms, Scorpions, Models, Molecular, Protein Structure, MESH: Amino Acid Sequence, MESH: Animals, MESH: Molecular Sequence Data, MESH: Neutralization Tests, MESH: Protein Structure, MESH: Rabbits, MESH: Scorpion Venoms, MESH: Scorpions, MESH: Antibodies, MESH: Antitoxins, MESH: Cross Reactions
الوصف: International audience ; The Amm VIII protein was previously isolated from the venom of the scorpion Androctonus mauretanicus mauretanicus. Despite 87% identity with AaH II, the most toxic alpha-type scorpion toxin, Amm VIII is not toxic to mice. However, antisera against Amm VIII protect mice from AaH II lethal action. Here, we report that the Amm VIII protein elicits antibodies that only recognize discontinuous-type epitopes since we could not observe any antibody binding to overlapping 12-mer peptides covering the whole Amm VIII sequence. By using a new bioinformatic tool, 24 peptides mimicking discontinuous regions of Amm VIII were designed in silico, then prepared by Spot synthesis. Seven of these discontinuous-continuous peptides were recognized by anti-Amm VIII antibodies. Analysis of the 3D location of the segments that compose the antigenically reactive discontinuous-continuous peptides, allowed us to group those antigenic segments into three regions of Amm VIII, putatively corresponding to discontinuous antigenic regions of alpha-type scorpion toxins. Anti-Amm VIII antibodies were also found to cross-react towards several of the discontinuous-continuous peptides designed from the AaH II structure, pointing to a possible involvement of the corresponding discontinuous epitopes in the capacity displayed by anti-Amm VIII antibodies to neutralize AaH II. Altogether, our results show that it is possible to design antibody-reactive peptides from discontinuous parts of scorpion toxins. The position of the reactive segments in the structural context of scorpion toxins highlights the antigenic properties of the Amm VIII anatoxin and concurs to explain the capacity of anti-Amm VIII antibodies to neutralize the potent AaH II toxin.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/19962461; hal-00482304; https://hal.science/hal-00482304Test; PRODINRA: 248103; PUBMED: 19962461; WOS: 000274943300020
DOI: 10.1016/j.vaccine.2009.10.135
الإتاحة: https://doi.org/10.1016/j.vaccine.2009.10.135Test
https://hal.science/hal-00482304Test
رقم الانضمام: edsbas.9AF0F33E
قاعدة البيانات: BASE