Interaction of polylysine with the cellular receptor for herpes simplex virus type 1.
We earlier reported that neomycin blocked reversibly the binding of herpes simplex virus type 1 (HSV-1) to the receptor of BHK cells, while the binding of HSV-2 to the receptor was unaffected. We could not determine whether the effect was on the virus particle, the receptor, or both. We have now tested several other cationic substances, and report that polylysine (and polyarginine) block the binding of HSV-1 to the receptor by interfering with the cellular receptor function; higher molecular weight polylysines were more potent than those of lower molecular weight. Polylysine and neomycin showed additive effects. In vitro, polylysine showed the same strong binding to the plasma membrane phosphoinositides as did neomycin. Together these data suggest that the drugs may have a common target in the cell membrane. The HSV-1 and HSV-2 virus particles were unaffected by the drugs, as was the cellular HSV-2 receptor.
Langeland
N
N
Department of Biochemistry, University of Bergen, Norway.
Moore
L J
LJ
Holmsen
H
H
Haarr
L
L
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000187:drug effects* / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism; D009355:Neomycin / Q000378:metabolism / Q000494:pharmacology; D010455:Peptides / Q000378:metabolism / Q000494:pharmacology; D010716:Phosphatidylinositols / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D011107:Polylysine / Q000378:metabolism / Q000494:pharmacology*; D011991:Receptors, Virus / Q000187:drug effects* / Q000378:metabolism; D018139:Simplexvirus / Q000378:metabolism*; D013997:Time Factors
D008563:Membrane Lipids; D010455:Peptides; D010716:Phosphatidylinositols; D010743:Phospholipids; D011991:Receptors, Virus; D011107:Polylysine; C015462:polyarginine; D009355:Neomycin