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Mucin-like region of herpes simplex virus type 1 attachment protein gC modulates the virus-glycosaminoglycan interaction.

Noomi Altgärde (Institutionen för teknisk fysik, Biologisk fysik) ; Charlotta Eriksson ; Nadia Peerboom (Institutionen för teknisk fysik, Biologisk fysik) ; Tuan Phan-Xuan (Institutionen för teknisk fysik, Kondenserade materiens fysik ; SuMo Biomaterials) ; Stephanie Möller ; Matthias Schnabelrauch ; Sofia Svedhem (Institutionen för teknisk fysik, Biologisk fysik) ; Edward Trybala ; Tomas Bergström ; Marta Bally (Institutionen för teknisk fysik, Biologisk fysik)
Journal of Biological Chemistry (0021-9258). Vol. 290 (2015), 35, p. 21473-21485.
[Artikel, refereegranskad vetenskaplig]

Glycoprotein C (gC) mediates the attachment of herpes simplex virus type 1 (HSV-1) to susceptible host cells by interacting with glycosaminoglycans (GAGs) on the cell surface. gC contains a mucin-like region located near the GAG-binding site, which may affect the binding activity. Here, we address this issue by studying an HSV-1 mutant lacking the mucin- like domain in gC and the corresponding purified mutant protein (gCΔmuc), in cell culture and GAG-binding assays, respectively. The mutant virus exhibited two functional alterations as compared to native HSV-1, i.e. decreased sensitivity to GAG-based inhibitors of virus attachment to cells, and reduced release of viral particles from the surface of infected cells. Kinetic and equilibrium binding characteristics of purified gC were assessed using surface plasmon resonance-based sensing together with a surface platform consisting of end-on immobilized GAGs. Both native gC and gCΔmuc bound via the expected binding region to chondroitin sulfate and sulfated hyaluronan but not to the non-sulfated hyaluronan, confirming binding specificity. In contrast to native gC, gCΔmuc exhibited a decreased affinity for GAGs and a slower dissociation, indicating that once formed, the gCΔmuc-GAG complex is more stable. It was also found that a larger number of gCΔmuc bound to a single GAG chain, compared to native gC. Taken together, our data suggest that the mucin-like region of HSV-1 gC is involved in the modulation of the GAG-binding activity, a feature of importance both for unrestricted virus entry into the cells and release of newly produced viral particles from infected cells.

Nyckelord: Herpesvirus, glycosaminoglycan, glycoprotein, surface plasmon resonance (SPR), carbohydrate-binding protein, mucin-like region, glycosylation


Background: Herpes simplex virus attachment protein gC comprises a glycosaminoglycan- binding site and a mucin-like region. Results: Removal of the mucin-like region modifies gC interaction with glycosaminoglycans. Conclusion: The mucin-like region balances the gC-glycosaminoglycan interaction during virus binding to and release from target cells. Significance: The finding might be of relevance for similar proteins on other GAG-binding viruses.



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Denna post skapades 2015-08-04. Senast ändrad 2016-10-17.
CPL Pubid: 220134

 

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Institutioner (Chalmers)

Institutionen för teknisk fysik, Biologisk fysik (2007-2015)
Institutionen för biomedicin, avdelningen för infektionssjukdomar (GU)
Institutionen för teknisk fysik, Kondenserade materiens fysik (1900-2015)
SuMo Biomaterials

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Livsvetenskaper
Materialvetenskap
Polymerkemi
Biokemi och molekylärbiologi
Cellbiologi
Immunologi
Medicinsk teknik
Medicinsk bioteknologi

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Virus-cell membrane interactions - Binding studies of Herpes Simplex Virus using surface-sensitive techniques