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

Artikel i vetenskaplig tidskrift
Författare Noomi Altgärde
Charlotta Eriksson
Nadia Peerboom
Tuan Phan-Xuan
Stephanie Möller
Matthias Schnabelrauch
Sofia Svedhem
Edward Trybala
Tomas Bergström
Marta Bally
Publicerad i Journal of Biological Chemistry
Volym 290
Nummer/häfte 35
Sidor 21473-21485
ISSN 0021-9258
Publiceringsår 2015
Publicerad vid Institutionen för biomedicin, avdelningen för infektionssjukdomar
Sidor 21473-21485
Språk en
Länkar dx.doi.org/10.1074/jbc.M115.637363
Ämnesord Herpesvirus, glycosaminoglycan, glycoprotein, surface plasmon resonance (SPR), carbohydrate-binding protein, mucin-like region, glycosylation
Ämneskategorier Polymerkemi, Biokemi och molekylärbiologi, Cellbiologi, Immunologi, Medicinsk teknik, Medicinsk bioteknologi

Sammanfattning

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.

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