The site on nectin1 receptor required for herpes simplex virus (HSV) entry into the cell was previously mapped to the 64-94 region, encompassing the predicted CC′C″ region of the immunoglobulin V domain. Within it lies a minimal HSV entry site (residues 77-94). Here we transferred the 65-76 region (C strand and CC′ loop) and portions, or single amino acids, thereof to nectin2, a homolog nonfunctional for wt HSV-1 entry. Replacement of the seven- or of three-amino-acid-long stretches from nectin1 to nectin2 (amino acids 69-75, 69-71, or 72-75) transferred wt HSV-1 and BHV-1 entry activity and enhanced HSV-2, PrV, and HSV-HSV(U21) entry to levels observed with nectin1. Thus, the CC′ ridge is sufficient to mediate wt HSV entry at a reduced level and responsible for the wide virus range of the receptor. Altogether the HSV entry site appears to be composed of contiguous synergistic regions, 64-76 and 77-94, each independently capable of mediating virus entry at reduced efficiency. © 2002 Elsevier Science (USA).

Menotti L., Cocchi F., Campadelli-Fiume G. (2002). Critical residues in the CC′ ridge of the human nectin1 receptor V domain enable herpes simplex virus entry into the cell and act synergistically with the downstream region. VIROLOGY, 301(1), 6-12 [10.1006/viro.2002.1620].

Critical residues in the CC′ ridge of the human nectin1 receptor V domain enable herpes simplex virus entry into the cell and act synergistically with the downstream region

Menotti L.;Cocchi F.;Campadelli-Fiume G.
2002

Abstract

The site on nectin1 receptor required for herpes simplex virus (HSV) entry into the cell was previously mapped to the 64-94 region, encompassing the predicted CC′C″ region of the immunoglobulin V domain. Within it lies a minimal HSV entry site (residues 77-94). Here we transferred the 65-76 region (C strand and CC′ loop) and portions, or single amino acids, thereof to nectin2, a homolog nonfunctional for wt HSV-1 entry. Replacement of the seven- or of three-amino-acid-long stretches from nectin1 to nectin2 (amino acids 69-75, 69-71, or 72-75) transferred wt HSV-1 and BHV-1 entry activity and enhanced HSV-2, PrV, and HSV-HSV(U21) entry to levels observed with nectin1. Thus, the CC′ ridge is sufficient to mediate wt HSV entry at a reduced level and responsible for the wide virus range of the receptor. Altogether the HSV entry site appears to be composed of contiguous synergistic regions, 64-76 and 77-94, each independently capable of mediating virus entry at reduced efficiency. © 2002 Elsevier Science (USA).
2002
Menotti L., Cocchi F., Campadelli-Fiume G. (2002). Critical residues in the CC′ ridge of the human nectin1 receptor V domain enable herpes simplex virus entry into the cell and act synergistically with the downstream region. VIROLOGY, 301(1), 6-12 [10.1006/viro.2002.1620].
Menotti L.; Cocchi F.; Campadelli-Fiume G.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/874060
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