The herpes simplex virus-1 glycoprotein E (gE) mediates IgG binding and cell-to-cell spread through distinct gE domains.
Herpes simplex virus-1 (HSV-1) glycoprotein E (gE) is a multifunctional protein capable of both binding the Fc portion of IgG and mediating cell-to-cell spread of HSV-1. Here we report that the domain on gE involved in IgG binding is distinct from the domain involved in mediating cell-to-cell spread. To do this we have used five mutants of the HSV-1 strain NS: NS-gE(null), a gE deletion virus; rNS-gE(null), a gE rescued virus; NS-gE339, a gE mutant virus with a four amino acid insert at position 339; rNS-gE339, a gE rescue of NS-gE339; and NS-gE406, a gE mutant virus with the same four amino acids inserted at position 406. Using IgG coated sheep red blood cells in rosetting assays, we show that the NS-gE339 does not bind IgG, yet retains the ability to mediate normal cell-to-cell spread. These results demonstrate that the gE domain involved in IgG binding differs from the domain involved in cell-to-cell spread.
Weeks
B S
BS
Department of Medicine, University of Pennsylvania, Philadelphia 19104, USA.
Sundaresan
P
P
Nagashunmugam
T
T
Kang
E
E
Friedman
H M
HM
D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D004912:Erythrocytes; D006651:Histocytochemistry; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000378:metabolism*; D015603:Keratinocytes / Q000821:virology; D016254:Mutagenesis, Insertional; D011485:Protein Binding; D011961:Receptors, Fc / Q000378:metabolism; D012756:Sheep; D018139:Simplexvirus / Q000235:genetics / Q000502:physiology*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000235:genetics / Q000494:pharmacology
D007141:Immunoglobulin Fc Fragments; D011961:Receptors, Fc; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C044768:glycoprotein E, herpes simplex virus type 1