The antibodies directed against N-terminal heptad-repeat peptide of hRSV fusion protein and its analog-5-Helix inhibit virus infection in vitro.
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.
Ni
Ling
L
Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, PR China.
Zhao
Linqing
L
Gao
George F
GF
Qian
Yuan
Y
Tien
Po
P
D000595:Amino Acid Sequence; D000906:Antibodies / Q000276:immunology*; D000998:Antiviral Agents / Q000502:physiology*; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D007106:Immune Sera; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D010446:Peptide Fragments / Q000276:immunology*; D012136:Respiratory Syncytial Viruses / Q000378:metabolism*; D014760:Viral Fusion Proteins / Q000737:chemistry*
D000906:Antibodies; D000998:Antiviral Agents; D007106:Immune Sera; D010446:Peptide Fragments; D014760:Viral Fusion Proteins