Structural analysis of peptides that interact with Newcastle disease virus.
A peptide with the sequence CTLTTKLYC has previously been identified to inhibit the propagation of Newcastle disease virus (NDV) in embryonated chicken eggs and tissue culture. NDV has been classified into two main groups: the velogenic group, and mesogenic with lentogenic strains as the other group based on its dissociation constants. In this study the peptide, CTLTTKLYC, displayed on the pIII protein of a filamentous M13 phage was synthesized and mutated in order to identify the amino acid residues involved in the interactions with NDV. Mutations of C1 and K6 to A1 and A6 did not affect the binding significantly, but substitution of Y8 with A8 dramatically reduced the interaction. This suggests that Y8 plays an important role in the peptide-virus interaction. The three-dimensional structure of the peptide was determined using circular dichroism (CD), nuclear magnetic resonance (NMR), and molecular modeling. The peptide exhibited two possible conformers. One that consists of consecutive beta-turns around T2-L3-T4-T5 and K6-L7-Y8-C9. The other conformer exhibited a beta-hairpin bend type of structure with a bend around L3-T4-T5-K6.
Chia
Suet Lin
SL
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Malaysia.
Tan
Wen Siang
WS
Shaari
Khozirah
K
Abdul Rahman
Noorsaadah
N
Yusoff
Khatijah
K
Satyanarayanajois
Seetharama D
SD
D000998:Antiviral Agents / Q000737:chemistry; D017104:Bacteriophage M13 / Q000378:metabolism; D001483:Base Sequence; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009522:Newcastle disease virus / Q000378:metabolism*; D009841:Oligonucleotides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012984:Software
D000998:Antiviral Agents; D009841:Oligonucleotides; D010455:Peptides