Specificity and affinity of binding of herpes simplex virus type 2 glycoprotein B to glycosaminoglycans.

@article{Williams1997SpecificityAA,
  title={Specificity and affinity of binding of herpes simplex virus type 2 glycoprotein B to glycosaminoglycans.},
  author={Richard K. Williams and Stephen E. Straus},
  journal={Journal of virology},
  year={1997},
  volume={71 2},
  pages={
          1375-80
        }
}
Herpes simplex virus type 2 (HSV-2) interacts with cell surface glycosaminoglycans during virus attachment. Glycoprotein B of HSV-2 can potentially mediate the interaction between the virion and cell surface glycosaminoglycans. To determine the specificity, kinetics, and affinity of these interactions, we used plasmon resonance-based biosensor technology to measure HSV-2 glycoprotein binding to glycosaminoglycans in real time. The recombinant soluble ectodomain of HSV-2 gB (gB2) but not the… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 32 REFERENCES

Characterization of cell-binding properties of bovine herpesvirus 1 glycoproteins B, C, and D: identification of a dual cell-binding function of gB

Y. Li, L. A. Babiuk, X. Liang
  • J. Virol
  • 1995
VIEW 1 EXCERPT

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