Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites
- PMID: 1699353
- DOI: 10.1016/0042-6822(90)90269-w
Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites
Abstract
Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus has been performed. Distinct clusters of amino acid substitutions conferring resistance to neutralization at each of the four previously defined antigenic sites (McCahon et al., 1989, J. Gen. Virol. 70, 639-645) have been identified. One site corresponds to the well-known 140-160 region of VP1, a second site is also on VP1, one site is on VP2, and the fourth site is on VP3. All of the amino acid substitutions identified are located on the surface of the virus. Despite the differences in three-dimensional structure between FMDV and other picornaviruses the neutralizing antigenic sites occur in analogous positions on the capsid surface.
Similar articles
-
The structure and antigenicity of a type C foot-and-mouth disease virus.Structure. 1994 Feb 15;2(2):123-39. doi: 10.1016/s0969-2126(00)00014-9. Structure. 1994. PMID: 8081743
-
Monoclonal antibodies to an Indian strain of type A foot-and-mouth disease virus.Acta Virol. 1999 Aug;43(4):219-25. Acta Virol. 1999. PMID: 10749367
-
Amino acid changes outside the G-H loop of capsid protein VP1 of type O foot-and-mouth disease virus confer resistance to neutralization by antipeptide G-H serum.Vaccine. 1993;11(3):359-62. doi: 10.1016/0264-410x(93)90199-8. Vaccine. 1993. PMID: 7680514
-
Foot-and-mouth disease and its antigens.Adv Exp Med Biol. 1985;185:27-46. doi: 10.1007/978-1-4684-7974-4_2. Adv Exp Med Biol. 1985. PMID: 2416203 Review.
-
The structure of an immunodominant loop on foot and mouth disease virus, serotype O1, determined under reducing conditions.Arch Virol Suppl. 1994;9:51-8. doi: 10.1007/978-3-7091-9326-6_6. Arch Virol Suppl. 1994. PMID: 8032279 Review.
Cited by
-
Towards improvements in foot-and-mouth disease vaccine performance.Acta Vet Scand. 2020 May 20;62(1):20. doi: 10.1186/s13028-020-00519-1. Acta Vet Scand. 2020. PMID: 32434544 Free PMC article. Review.
-
Complete genome characterization of foot-and-mouth disease virus My-466 belonging to the novel lineage O/ME-SA/SA-2018.Heliyon. 2024 Feb 20;10(5):e26716. doi: 10.1016/j.heliyon.2024.e26716. eCollection 2024 Mar 15. Heliyon. 2024. PMID: 39790372 Free PMC article.
-
Tracking the Antigenic Evolution of Foot-and-Mouth Disease Virus.PLoS One. 2016 Jul 22;11(7):e0159360. doi: 10.1371/journal.pone.0159360. eCollection 2016. PLoS One. 2016. PMID: 27448206 Free PMC article.
-
The Use of Distinctive Monoclonal Antibodies in FMD VLP- and P1-Based Blocking ELISA for the Seromonitoring of Vaccinated Swine.Int J Mol Sci. 2022 Aug 1;23(15):8542. doi: 10.3390/ijms23158542. Int J Mol Sci. 2022. PMID: 35955678 Free PMC article.
-
Distinctive features of foot-and-mouth disease virus, a member of the picornavirus family; aspects of virus protein synthesis, protein processing and structure.Prog Biophys Mol Biol. 1993;60(3):241-60. doi: 10.1016/0079-6107(93)90016-d. Prog Biophys Mol Biol. 1993. PMID: 8396787 Free PMC article. Review. No abstract available.