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The antibodies directed against N-terminal heptad-repeat peptide of hRSV fusion protein and its analog-5-Helix inhibit virus infection in vitro


The antibodies directed against N-terminal heptad-repeat peptide of hRSV fusion protein and its analog-5-Helix inhibit virus infection in vitro



Biochemical and Biophysical Research Communications 331(4): 1358-1364



ISSN/ISBN: 0006-291X

PMID: 15883025

DOI: 10.1016/j.bbrc.2005.04.046

Human respiratory syncytial virus (hRSV) membrane fusion is promoted by the formation of a trimer-of-hairpins structure that brings the amino- and carboxyl-terminal regions of fusion (F) protein into close proximity. Two heptad-repeat (HR1 and HR2) regions in F protein play an important role in this process. Our previous study demonstrated that peptides derived from HR1 and HR2 regions of F protein were potent inhibitors of hRSV entry. Here we showed that HR1 peptide and its analog denoted 5-Helix which contained a central coiled-coil formed by three HR1s could induce highly potent antibody response in the immunized rabbits. Both antibodies could recognize F1 domain of the F protein and inhibited hRSV entry with the neutralizing antibody titers of 1:61 and 1:115, respectively. These suggested that 5-Helix could induce potent neutralizing antibody response and the central coiled-coil might be a highly conserved neutralization site for hRSV F protein.

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Accession: 012634997

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