Inhibition of a plant virus infection by analogs of melittin.
An approach that enables identification of specific synthetic peptide inhibitors of plant viral infection is reported. Synthetic analogs of melittin that have sequence and structural similarities to an essential domain of tobacco mosaic virus coat protein were found to possess highly specific antiviral activity. This approach involves modification of residues located at positions analogous to those that are critical for virus assembly. The degree of inhibition found correlates well with sequence similarities between the viral capsid protein and the melittin analogs studied as well as with the induced conformational changes that result upon interaction of the peptides and ribonucleic acid.
Marcos
J F
JF
Scripps Research Institute, La Jolla, CA 92037, USA.
Beachy
R N
RN
Houghten
R A
RA
Blondelle
S E
SE
Pérez-Payá
E
E
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry; D002942:Circular Dichroism; D018551:Solanum lycopersicum; D008555:Melitten / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010947:Plants, Toxic; D011487:Protein Conformation; D012367:RNA, Viral / Q000032:analysis / Q000096:biosynthesis / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014026:Nicotiana; D014027:Tobacco Mosaic Virus / Q000187:drug effects* / Q000472:pathogenicity / Q000502:physiology; D017898:Tobamovirus / Q000187:drug effects* / Q000472:pathogenicity / Q000502:physiology; D014771:Virion / Q000502:physiology
D012367:RNA, Viral; D008555:Melitten