PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B

Cell. 2008 Mar 21;132(6):935-44. doi: 10.1016/j.cell.2008.01.043.


Glycoprotein B (gB) is one of the essential components for infection by herpes simplex virus-1 (HSV-1). Although several cellular receptors that associate with glycoprotein D (gD), such as herpes virus entry mediator (HVEM) and Nectin-1, have been identified, specific molecules that mediate HSV-1 infection by associating with gB have not been elucidated. Here, we found that paired immunoglobulin-like type 2 receptor (PILR) alpha associates with gB, and cells transduced with PILRalpha become susceptible to HSV-1 infection. Furthermore, HSV-1 infection of human primary cells expressing both HVEM and PILRalpha was blocked by either anti-PILRalpha or anti-HVEM antibody. Our results demonstrate that cellular receptors for both gB and gD are required for HSV-1 infection and that PILRalpha plays an important role in HSV-1 infection as a coreceptor that associates with gB. These findings uncover a crucial aspect of the mechanism underlying HSV-1 infection.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / metabolism
  • CHO Cells
  • Cell Line
  • Cells, Cultured
  • Cricetinae
  • Cricetulus
  • Herpes Simplex / metabolism*
  • Herpes Simplex / virology
  • Herpesvirus 1, Human / metabolism*
  • Humans
  • Membrane Glycoproteins / metabolism*
  • Receptors, Immunologic / metabolism*
  • Receptors, Virus / metabolism*
  • Transfection
  • Viral Envelope Proteins / metabolism*


  • Antibodies, Monoclonal
  • Membrane Glycoproteins
  • PILRA protein, human
  • Receptors, Immunologic
  • Receptors, Virus
  • Viral Envelope Proteins
  • glycoprotein B, Simplexvirus