Identification of a conserved neutralization site in the first heptad repeat of the fusion protein of respiratory syncytial virus

Archives of Virology
J P LangedijkJ T van Oirschot

Abstract

A large set of monoclonal antibodies (MAbs) directed against the fusion glycoprotein complex F1F2 of bovine respiratory syncytial virus (BRSV) and several polyclonal sera from infected or vaccinated animals were tested in Pepscan to locate linear epitopes on the F-protein. The polyclonal sera mapped to antigenic sites that correspond exactly to known antigenic sites on the F protein of human RSV. Only the neutralizing MAb 3 could be mapped with Pepscan. MAb 3 reacted with three successive overlapping linear peptides that shared the amino acid sequence 173STNKAVVSLS182. The sequence of this novel neutralization site is conserved in all known BRSV- and human RSV-strains and is located on the N-terminus of F1, adjacent to the hydrophobic, putative fusion-related region. This region is probably part of a central coiled-coil stem that is structurally conserved in paramyxovirus fusion and orthomyxovirus hemagglutinin glycoproteins. This linear conserved epitope may be a potential candidate for a peptide-based vaccine which can induce neutralizing antibodies against all groups and subgroups of RSV. Furthermore, the proposed structural features of the neutralization site may aid in the design of a peptide-based vaccine.

Citations

Apr 1, 2010·Future Microbiology·Robert AndersonJoanne M Langley
Dec 6, 2000·Proceedings of the National Academy of Sciences of the United States of America·X ZhaoP S Kim
Mar 5, 2015·Virus Research·José A Melero, Vicente Mas
Nov 15, 2008·The Journal of General Virology·Nancy D UlbrandtMichael P McCarthy
Oct 19, 2001·Biophysical Journal·G SettanniA Maritan
Nov 29, 2001·Journal of Veterinary Diagnostic Investigation : Official Publication of the American Association of Veterinary Laboratory Diagnosticians, Inc·N Z ElerakyL N Potgieter

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