Glycosaminoglycan-binding ability is a feature of wild-type strains of herpes simplex virus type 1.
Adaptation of some viruses to replication in cultured cells selects variants that due to alterations in the viral attachment proteins convert to using heparan sulfate (HS) as initial receptor. We report that the nucleotide sequence of herpes simplex virus type 1 (HSV-1) glycoprotein C (gC), a principal attachment component of the virus, remained unchanged during adaptation of wild-type strains to cultured cells. Likewise, amino acid residues critical for binding of gC to HS were conserved in viral strains that replicated in vivo in different human tissues. Moreover wild-type HSV-1 strains derived directly from clinical specimens were, similar to their cell culture propagated progeny viruses and common laboratory strains, sensitive to heparin and demonstrated impairment in their ability to infect HS/chondroitin sulfate deficient cells. These results demonstrate that the HS-binding ability is a feature of wild-type strains of HSV-1.
Trybala
Edward
E
Department of Clinical Virology, Göteborg University, Guldhedsgatan 10B, S-413 46 Göteborg, Sweden.
Roth
Anette
A
Johansson
Maria
M
Liljeqvist
Jan-Ake
JA
Rekabdar
Elham
E
Larm
Olle
O
Bergström
Tomas
T
D000222:Adaptation, Physiological; D000818:Animals; D002522:Chlorocebus aethiops; D006025:Glycosaminoglycans / Q000378:metabolism*; D006497:Heparan Sulfate / Q000378:metabolism; D006561:Herpes Simplex / Q000821:virology*; D018259:Herpesvirus 1, Human / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity*; D006801:Humans; D007739:L Cells; D051379:Mice; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism
D006025:Glycosaminoglycans; D006497:Heparan Sulfate; D014759:Viral Envelope Proteins; C038535:glycoprotein gC, herpes simplex virus type 1