The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D

Proceedings of the National Academy of Sciences of the United States of America - Tập 95 Số 26 - Trang 15700-15705 - 1998
Francesca Cocchi1, Marc Lopez1, Laura Menotti1, Mustapha Aoubala1, Patrice Dubreuil1, Gabriella Campadelli‐Fiume1
1Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy; and Institute of Cancer Biology and Immunology, Institut National de la Santé et de la Recherche Médicale U.119, 27 bd Leï Roure, 13009 Marseille, France

Tóm tắt

The herpesvirus entry mediator C (HveC), previously known as poliovirus receptor-related protein 1 (PRR1), and the herpesvirus Ig-like receptor (HIgR) are the bona fide receptors employed by herpes simplex virus-1 and -2 (HSV-1 and -2) for entry into the human cell lines most frequently used in HSV studies. They share an identical ectodomain made of one V and two C2 domains and differ in transmembrane and cytoplasmic regions. Expression of their mRNA in the human nervous system suggests possible usage of these receptors in humans in the path of neuron infection by HSV. Glycoprotein D (gD) is the virion component that mediates HSV-1 entry into cells by interaction with cellular receptors. We report on the identification of the V domain of HIgR/PRR1 as a major functional region in HSV-1 entry by several approaches. First, the epitope recognized by mAb R1.302 to HIgR/PRR1, capable of inhibiting infection, was mapped to the V domain. Second, a soluble form of HIgR/PRR1 consisting of the single V domain competed with cell-bound full-length receptor and blocked virion infectivity. Third, the V domain was sufficient to mediate HSV entry, as an engineered form of PRR1 in which the two C2 domains were deleted and the V domain was retained and fused to its transmembrane and cytoplasmic regions was still able to confer susceptibility, although at reduced efficiency relative to full-length receptor. Consistently, transfer of the V domain of HIgR/PRR1 to a functionally inactive structural homologue generated a chimeric receptor with virus-entry activity. Finally, the single V domain was sufficient for in vitro physical interaction with gD. The in vitro binding was specific as it was competed both by antibodies to the receptor and by a mAb to gD with potent neutralizing activity for HSV-1 infectivity.

Từ khóa


Tài liệu tham khảo

10.1073/pnas.91.12.5406

10.1016/S0092-8674(00)81363-X

10.1126/science.280.5369.1618

10.1006/viro.1998.9218

10.1128/JVI.72.12.9992-10002.1998

10.1016/0378-1119(94)00842-G

10.1016/0378-1119(95)00180-E

10.1128/jvi.62.8.2596-2604.1988

10.1128/jvi.66.1.341-348.1992

10.1128/jvi.67.4.2285-2297.1993

10.1128/jvi.62.5.1486-1494.1988

10.1128/jvi.62.1.159-167.1988

10.1128/jvi.64.12.6070-6079.1990

10.1006/viro.1994.1098

10.1073/pnas.93.5.1836

10.1128/jvi.64.6.2569-2576.1990

10.1128/jvi.71.4.2940-2946.1997

10.1016/0168-1702(91)90024-P

10.1006/smvy.1993.1012

M Lopez, F Jordier, F Bardin, L Coulombel, C Chabannon, P Dubreuil Leukocyte Typing VI, White Cells Differentiation Antigens, eds T Kishomoto, H Kikutani, A von dem Borne, D Y Mason, M Miyasaka, A Moretta, K Okumura, S Shaw, T A Springer, K Sugumura, et al. (Garland, New York), pp. 1081–1083 (1997).

10.1128/iai.29.2.724-732.1980

10.1182/blood.V92.12.4602.424k21_4602_4611

N Maroc, R Rottapel, O Rosnet, S Marchetto, C Lavezzi, P Mannoni, D Birnbaum, P Dubreuil Oncogene 8, 909–918 (1993).

10.1128/jvi.70.6.3815-3822.1996

10.1084/jem.174.3.561

10.1128/JVI.72.5.3595-3601.1998

10.1128/JVI.72.9.7064-7074.1998

10.1128/jvi.62.9.3274-3280.1988

10.1038/334159a0

10.1016/0092-8674(89)90690-9

10.1073/pnas.87.13.5001

10.1128/jvi.65.1.440-444.1991

10.1073/pnas.88.10.4104

10.1073/pnas.88.9.3598

10.1006/viro.1994.1493

10.1128/JVI.72.5.3578-3586.1998

R J Whitley Virology, eds B N Fields, D M Knipe, P Howley, R M Chanock, M S Hirsch, J L Melnick, T P Monath, B Roizman (Raven, New York), pp. 2297–2342 (1996).

Thông tin
Thông tin xuất bản

Proceedings of the National Academy of Sciences of the United States of America

Tập 95 Số 26

15700-15705

Thông tin tác giả