CRIS Current Research Information System
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishThe 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).
| Titolo: | 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 | |
| Autore/i: | Menotti L.; Cocchi F.; Campadelli-Fiume G. | |
| Autore/i Unibo: | ||
| Anno: | 2002 | |
| Rivista: | ||
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1006/viro.2002.1620 | |
| 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). | |
| Data stato definitivo: | 2022-02-28T17:30:52Z | |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
File in questo prodotto:
Copyright © 2022