Differences in the N termini of herpes simplex virus type 1 and 2 gDs that influence functional interactions with the human entry receptor Nectin-2 and an entry receptor expressed in Chinese hamster ovary cells.
Amino acid differences at seven positions in the N termini of the glycoproteins D (gDs) specified by herpes simplex virus type 1 (HSV-1) and HSV-2 are largely responsible for the significantly higher cell fusion activity of HSV-2 gD with Chinese hamster ovary cells expressing human nectin-2 or only an endogenous hamster receptor.
Zago
Anna
A
Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Spear
Patricia G
PG
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000502:physiology*; D006224:Cricetinae; D006801:Humans; D008561:Membrane Fusion; D008958:Models, Molecular; D008969:Molecular Sequence Data; D000075983:Nectins; D010957:Plasmids / Q000235:genetics; D017434:Protein Structure, Tertiary; D011991:Receptors, Virus / Q000235:genetics / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*
D015815:Cell Adhesion Molecules; D000075983:Nectins; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; C039447:glycoprotein D, Human herpesvirus 1; C040570:glycoprotein D-herpes simplex virus type 2