Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection.
Herpes simplex virus type 1 (HSV-1) entry into permissive cells involves attachment to cell-surface glycosaminoglycans (GAGs) and fusion of the virus envelope with the cell membrane triggered by the binding of glycoprotein D (gD) to cognate receptors. In this study, we characterized the observation that soluble forms of the gD ectodomain (sgD) can mediate entry of gD-deficient HSV-1. We examined the efficiency and receptor specificity of this activity and used sequential incubation protocols to determine the order and stability of the initial interactions required for entry. Surprisingly, virus binding to GAGs did not increase the efficiency of sgD-mediated entry and gD-deficient virus was capable of attaching to GAG-deficient cells in the absence of sgD. These observations suggested a novel binding interaction that may play a role in normal HSV infection.
Tsvitov
Marianna
M
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, E1246 Biomedical Science Tower, Pittsburgh, PA 15261, USA.
Frampton
Arthur R
AR
Shah
Waris A
WA
Wendell
Steven K
SK
Ozuer
Ali
A
Kapacee
Zoher
Z
Goins
William F
WF
Cohen
Justus B
JB
Glorioso
Joseph C
JC
D000818:Animals; D016466:CHO Cells; D002460:Cell Line; D002522:Chlorocebus aethiops; D006224:Cricetinae; D003412:Cricetulus; D017353:Gene Deletion; D006025:Glycosaminoglycans / Q000172:deficiency; D018259:Herpesvirus 1, Human / Q000235:genetics / Q000502:physiology*; D006801:Humans; D011991:Receptors, Virus / Q000235:genetics / Q000502:physiology*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000235:genetics / Q000502:physiology*; D053585:Virus Attachment; D053586:Virus Internalization
D006025:Glycosaminoglycans; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; C039447:glycoprotein D, Human herpesvirus 1