Structure and function study of paramyxovirus fusion protein heptad repeat peptides.
Paramyxovirus might adopt a molecular mechanism of membrane fusion similar to that of other class I viruses in which the heptad repeat (HR) regions of fusion protein (F) HR1 and HR2 form a six-helix bundle structure inducing membrane fusion. In this study, we examined the structure and function of HR1 and HR2 from the avian paramyxovirus-2 (APMV-2) F protein. The study showed that APMV-2 HR1 and HR2 formed a stable six-helix bundle. Only a soluble APMV-2 HR2 peptide showed potent and specific virus-cell fusion inhibition activity. Cross-inhibiting activity with APMV-1 (Newcastle disease virus, NDV) was not found. A possible mechanism of membrane fusion inhibition by the paramyxovirus HR2 peptide is discussed.
Wang
Xiao-Jia
XJ
College of Animal Medicine, China Agricultural University, Beijing 100094, China.
Bai
Ya-Duo
YD
Zhang
Guo-Zhong
GZ
Zhao
Ji-Xun
JX
Wang
Ming
M
Gao
George F
GF
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002942:Circular Dichroism; D019281:Dimerization; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013696:Temperature; D014760:Viral Fusion Proteins / Q000737:chemistry*
D010455:Peptides; D011993:Recombinant Fusion Proteins; D014760:Viral Fusion Proteins; D005982:Glutathione Transferase