Lack of detectable interaction between HSV-1 and integrins or tachykinins.
Several viruses are known to utilize cellular integrin molecules to gain entry into cells. Because of the ability of herpes simplex virus type 1 (HSV-1) to disrupt cellular adhesion, as seen particularly in ocular infections, we examined the ability of several peptides, containing known integrin recognition sequences, to interfere with plaque formation of HSV-1 in epithelial cells. We also examined the possible involvement of tachykinins in virus entry. We did not detect any decrease in plaque formation by HSV-1 in the presence of Arg-Gly-Asp, Asp-Gly-Glu-Ala, or EILDV peptides or in the presence of monoclonal antibodies to the human beta1 or beta4 integrin subunit. Substance P or inhibitors of the NK1 or NK2 tachykinin receptors also had no inhibitory effects on HSV-1 plaque formation.
Israel
B A
BA
Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, Wisc. 53706, USA. israelb@svm.vetmed.wisc.edu
Schultz
K T
KT
Murphy
C J
CJ
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002352:Carrier Proteins / Q000494:pharmacology; D002460:Cell Line; D018259:Herpesvirus 1, Human / Q000187:drug effects / Q000254:growth & development* / Q000472:pathogenicity*; D006801:Humans; D016023:Integrins / Q000037:antagonists & inhibitors / Q000502:physiology*; D009842:Oligopeptides / Q000494:pharmacology; D015320:Tachykinins / Q000037:antagonists & inhibitors / Q000502:physiology*; D010948:Viral Plaque Assay
D000911:Antibodies, Monoclonal; D002352:Carrier Proteins; D016023:Integrins; D009842:Oligopeptides; D015320:Tachykinins; C113781:aspartyl-glycyl-glutamyl-alanine; C094697:glutamyl-isoleucyl-leucyl-aspartyl-valine; C047981:arginyl-glycyl-aspartic acid