Enhancement of bovine leukemia virus-induced syncytia formation by di- and tripeptides.
Short hydrophobic peptides were previously shown to inhibit infectivity of para- and orthomyxoviruses. We tested the ability of a series of di- and tripeptides to interfere with cell fusion induced by bovine leukemia virus (BLV). Peptides containing a hydrophobic contribution and/or a positive net charge strongly enhanced syncytia formation induced by BLV on CC81 indicator cells. The size of the multinucleated cells was strongly increased (up to 10-fold) in the presence of the enhancer peptides whereas no effect was observed on the indicator cells in the absence of BLV. The peptides thus amplified the fusion process initiated by BLV envelope glycoproteins. The effect was dose-dependent at concentrations ranging from 20 to 640 microM and did not result from an increased expression of BLV proteins. The peptides did not compete with anti-gp51 monoclonal antibodies for the recognition of eight well-defined epitopes of gp51. We consequently hypothesize that the enhancer peptides interact with the membrane of BLV-producing cells and/or indicator cells and propose a model based on molecular modeling.
Laboratory of Molecular Biology and Animal Physiology, Faculty of Agronomy, Gembloux, Belgium.
V
V
Vonèche
I
I
Callebaut
B
B
Lambrecht
R
R
Brasseur
A
A
Burny
D
D
Portetelle
D000595:Amino Acid Sequence; D002459:Cell Fusion / Q000187:drug effects*; D001909:Leukemia Virus, Bovine / Q000472:pathogenicity*; D008563:Membrane Lipids / Q000737:chemistry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D008563:Membrane Lipids; D009842:Oligopeptides