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Epitope mapping of the outer structural protein VP1 of three different serotypes of foot-and-mouth disease virus
Authors:R H Meloen  S J Barteling
Affiliation:1. School of Chemical Engineering and Material Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul 03722, Republic of Korea;2. College of Pharmacy and Integrated Research Institute for Drug Development, Dongguk University, 32 Dongguk-ro, Goyang, Gyeonggi-do 10326, Republic of Korea;3. Center for Molecular Intelligence, The State University of New York, Korea, 119 Songdomunhwa-ro, Yeonsu-gu, Incheon 21985, Republic of Korea;1. Department of Otorhinolaryngology-Head and Neck Surgery, Chung-Ang University College of Medicine, Seoul, Republic of Korea;2. Department of Otolaryngology-Head and Neck Surgery, Soon Chun Hyang University College of Medicine, Seoul, Republic of Korea;3. CEWIT Center for Systems Biology, State University of New York, Incheon, Republic of Korea;4. Department of Otolaryngology-Head and Neck Surgery, Seoul National University Hospital, Seoul National University College of Medicine, Seoul, Republic of Korea;1. IRTA, Centre de Recerca en Sanitat Animal (CReSA, IRTA-UAB), Campus de la Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain;2. Departament de Ciències Experimentals i de la Salut, Universitat Pompeu Fabra, 08003 Barcelona, Spain;3. Departament d''Agricultura, Ramaderia i Pesca (DARP), Generalitat de Catalunya, Spain;4. Departament de Ciència Animal, ETSEA, Universidad de Lleida, 25198, Spain;5. Centro de Biología molecular “Severo Ochoa” (CSIC-UAM), Cantoblanco, 28049 Madrid, Spain;1. Hubei Insect Resources Utilization and Sustainable Pest Management Key Laboratory, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan, Hubei, 430070, China;2. Institute of Virology, College of Plant Protection, Hunan Agricultural University, Changsha, Hunan, 410128, China;3. College of Natural Resources and Life Science, Dong-A University, Busan, 604-714, Republic of Korea
Abstract:All overlapping hexapeptides of the outer structural protein VP1 of type O1, type A10, and type C1 were reacted with the appropriate anti-virus, anti-viral subunit and anti-VP1 sera. The results suggest that anti-virus sera may contain activities against viral subunit and VP1 as well as against virus. Furthermore the antigenic peptides associated with the intact virion of all three serotypes are found at similar locations on their respective VP1s, and produced neutralizing activities when used for vaccination. The results further offer an explanation for the often observed cross-reactions between serotypes, especially at the level of the viral subunit and VP1. The reliability of predictions of useful peptides from hydrophilicity profiles and secondary structure predictions is questioned. Predictions based on variation profiles appear to be more useful.
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