Abstract：
:Human respiratory syncytial virus (HRSV) is a leading pathogen causing lower respiratory tract infections in infants and young children worldwide. In line with the development of an effective vaccine against HRSV, a domain of the fusion (F) glycoprotein of HRSV was produced and its immunogenicity and antigenic properties, namely the effect of deficient glycosylation was examined. A His-tagged recombinant F (rF) protein was expressed in Escherichia coli, solubilized with 8 mol/l urea, purified by the Ni-NTA affinity chromatography and used for the raising of a polyclonal antibody in rabbits. The non-glycosylated rF protein proved to be a strong immunogen that induced a polyclonal antibody that was able to recognize also the glycosylated F1 subunit of native HRSV. The other way around, a polyclonal antibody prepared against the native HRSV was able to react with the rF protein. These results indicated that glycosylation was not necessary for the F domain aa 212-574 in order to be recognized by the specific polyclonal antibody.
journal_name
Acta Viroljournal_title
Acta virologicaauthors
Lim SH,Jahanshiri F,Jalilian FA,Rahim RA,Sekawi Z,Yusoff Kdoi
10.4149/av_2010_03_181subject
Has Abstractpub_date
2010-01-01 00:00:00pages
181-7issue
3eissn
0001-723Xissn
1336-2305journal_volume
54pub_type
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