Chunya PuttikhuntPrapapun Ong-ajchaowlerdTanapan PrommoolSutha SangiambutJanjuree NetsawangThawornchai LimjindapornPrida MalasitWatchara KasinrerkFaculty of Medicine, Siriraj Hospital, Mahidol UniversityMahidol UniversityChiang Mai UniversityArmed Forces Research Institute of Medical Sciences, Thailand2018-09-132018-09-132009-06-30Archives of Virology. Vol.154, No.8 (2009), 1211-1221030486082-s2.0-70349560295https://repository.li.mahidol.ac.th/handle/20.500.14594/27696We produced monoclonal and polyclonal antibodies to the capsid (C) protein of dengue serotype 2 virus (DV2 C). First, a maltose-binding protein fused to DV2 C protein (MBP-C) was overproduced in E. coli. The affinity-purified MBP-C protein was cleaved by factor Xa protease to obtain a recombinant DV2 C protein, which was then used for mouse immunizations. Two hybridoma cell lines producing anti-C Mabs as well as anti-C polyclonal antibody were successfully generated and characterized. Interestingly, all of the generated antibodies specifically recognized the first 20 amino acids of the DV2 C protein, as determined by peptide epitope mapping and via a recombinant DV2 C protein in which this region was deleted. The results suggested that this region is predominantly immunogenic in mice. © Springer-Verlag 2009.Mahidol UniversityImmunology and MicrobiologyArticleSCOPUS10.1007/s00705-009-0426-5