Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha.
Herpes simplex virus 1 (HSV-1) enters cells either via fusion of the virion envelope and host cell plasma membrane or via endocytosis, depending on the cell type. In the study reported here, we investigated a viral entry pathway dependent on the paired immunoglobulin-like type 2 receptor alpha (PILRalpha), a recently identified entry coreceptor for HSV-1 that associates with viral envelope glycoprotein B (gB). Experiments using inhibitors of endocytic pathways and ultrastructural analyses of Chinese hamster ovary (CHO) cells transduced with PILRalpha showed that HSV-1 entry into these cells was via virus-cell fusion at the cell surface. Together with earlier observations that HSV-1 uptake into normal CHO cells and those transduced with a receptor for HSV-1 envelope gD is mediated by endocytosis, these results indicated that expression of PILRalpha produced an alternative HSV-1 entry pathway in CHO cells. We also showed that human and murine PILRalpha were able to mediate entry of pseudorabies virus, a porcine alphaherpesvirus, but not of HSV-2. These results indicated that viral entry via PILRalpha appears to be conserved but that there is a PILRalpha preference among alphaherpesviruses.
Arii
Jun
J
Department of Infectious Disease Control, Division of Viral Infection, International Research Center for Infectious Diseases, The University of Tokyo, Tokyo, Japan.
Uema
Masashi
M
Morimoto
Tomomi
T
Sagara
Hiroshi
H
Akashi
Hiroomi
H
Ono
Etsuro
E
Arase
Hisashi
H
Kawaguchi
Yasushi
Y
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D018138:Alphaherpesvirinae / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D006224:Cricetinae; D004705:Endocytosis; D007963:Leukocytes, Mononuclear / Q000276:immunology; D018950:Lipopolysaccharide Receptors / Q000276:immunology; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D008854:Microscopy, Electron; D011485:Protein Binding; D011971:Receptors, Immunologic / Q000235:genetics / Q000378:metabolism*; D019076:Transgenes; D053586:Virus Internalization
D018950:Lipopolysaccharide Receptors; D008562:Membrane Glycoproteins; C412263:PILRA protein, human; D011971:Receptors, Immunologic; D000255:Adenosine Triphosphate