title: Herpes simplex virus types 1 and 2 differ in their interaction with heparan sulfate.
abstract: Cell surface heparan sulfate (HS) serves as an initial receptor for many different viruses, including herpes simplex virus types 1 and 2 (HSV-1 and 2, respectively). Glycoproteins C and B (gC and gB) are the major components of the viral envelope that mediate binding to HS. In this study, purified gB and gC homologous proteins as well as purified HSV-1 and HSV-2 virions were compared for the ability to bind isolated HS receptor molecules. HSV-1 gC and HSV-2 gC bound comparable amounts of HS. Similarly, HSV-1 gB and its HSV-2 counterpart showed no difference in the HS-binding capabilities. Despite the similar HS-binding potentials of gB and gC homologs, HSV-1 virions bound more HS than HSV-2 particles. Purified gC and gB proteins differed with respect to sensitivity of their interaction with HS to increased concentrations of sodium chloride in the order gB-2 > gB-1 > gC-1 > gC-2. The corresponding pattern for binding of whole HSV virions to cells in the presence of increased ionic strength of the medium was HSV-2 gC-neg1 > HSV-1 gC(-)39 > HSV-1 KOS 321 > HSV-2 333. These results relate the HS-binding activities of individual glycoproteins with the cell-binding abilities of whole virus particles. In addition, these data suggest a greater contribution of electrostatic forces for binding of gB proteins and gC-negative mutants compared with binding of gC homologs and wild-type HSV strains. Binding of wild-type HSV-2 virions was the least sensitive to increased ionic strength of the medium, suggesting that the less extensive binding of HS molecules by HSV-2 than by HSV-1 can be compensated for by a relatively weak contribution of electrostatic forces to the binding. Furthermore, gB and gC homologs exhibited different patterns of sensitivity of binding to cells to inhibition with selectively N-, 2-O-, and 6-O-desulfated heparin compounds. The O-sulfate groups of heparin were found to be more important for interaction with gB-1 than gB-2. These results indicate that HSV-1 and HSV-2 differ in their interaction with HS.
authors.affiliation: Department of Clinical Virology, University of Göteborg, S-413 46 Göteborg, Sweden.
authors.forename: E
authors.initials: E
authors.lastname: Trybala
authors.forename: J A
authors.initials: JA
authors.lastname: Liljeqvist
authors.forename: B
authors.initials: B
authors.lastname: Svennerholm
authors.forename: T
authors.initials: T
authors.lastname: Bergström
mesh_terms: D014644:Genetic Variation; D006023:Glycoproteins / Q000737:chemistry; D006497:Heparan Sulfate; D018259:Herpesvirus 1, Human / Q000737:chemistry* / Q000235:genetics; D018258:Herpesvirus 2, Human / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D014759:Viral Envelope Proteins / Q000737:chemistry*
chemical_list: D006023:Glycoproteins; D006497:Heparan Sulfate; D014759:Viral Envelope Proteins