Home Acta Virologica 2010 Acta Virologica Vol.54, No.3, p.181-187, 2010

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Founded: 1957
ISSN 0001-723X
E-ISSN 1336-2305

Published in English

Impact Factor = 1.82

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Acta Virologica Vol.54, No.3, p.181-187, 2010

Title: Glycosylation is not necessary for recognition of the fusion glycoprotein domain of the Human respiratory syncytial virus by a polyclonal antibody
Author: S. H. E. Lim, F. Jahanshiri, F. A. Jalilian, R. A. Rahim, Z. Sekawi, K. Yusoff

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.

Keywords: Human respiratory syncytial virus; fusion protein; F1 subunit; recombinant protein; glycosylation; polyclonal antibody
Year: 2010, Volume: 54, Issue: 3 Page From: 181, Page To: 187
Price: 16.80 €

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