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dc.contributor.authorChunya Puttikhunten_US
dc.contributor.authorPrapapun Ong-ajchaowlerden_US
dc.contributor.authorTanapan Prommoolen_US
dc.contributor.authorSutha Sangiambuten_US
dc.contributor.authorJanjuree Netsawangen_US
dc.contributor.authorThawornchai Limjindapornen_US
dc.contributor.authorPrida Malasiten_US
dc.contributor.authorWatchara Kasinrerken_US
dc.contributor.otherFaculty of Medicine, Siriraj Hospital, Mahidol Universityen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherChiang Mai Universityen_US
dc.contributor.otherArmed Forces Research Institute of Medical Sciences, Thailanden_US
dc.identifier.citationArchives of Virology. Vol.154, No.8 (2009), 1211-1221en_US
dc.description.abstractWe 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.en_US
dc.rightsMahidol Universityen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleProduction and characterization of anti-dengue capsid antibodies suggesting the N terminus region covering the first 20 amino acids of dengue virus capsid protein is predominantly immunogenic in miceen_US
Appears in Collections:Scopus 2006-2010

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