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Mucin-like region o...
Mucin-like region of herpes simplex virus type 1 attachment protein gC modulates the virus-glycosaminoglycan interaction.
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- Altgärde, Noomi, 1983 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Eriksson, Charlotta, 1986 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine,University of Gothenburg
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- Peerboom, Nadia, 1990 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Phan Xuan, Tuan, 1984 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Möller, Stephanie (author)
- Innovent e.V.
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- Schnabelrauch, Matthias (author)
- Innovent e.V.
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- Svedhem, Sofia, 1970 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Trybala, Edward, 1955 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine,University of Gothenburg
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- Bergström, Tomas, 1950 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine,University of Gothenburg
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- Bally, Marta, 1981 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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(creator_code:org_t)
- 2015
- 2015
- English.
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 290:35, s. 21473-21485
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Abstract
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- 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.
Subject headings
- NATURVETENSKAP -- Kemi -- Polymerkemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Polymer Chemistry (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Medicinteknik -- Medicinsk laboratorie- och mätteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Medical Engineering -- Medical Laboratory and Measurements Technologies (hsv//eng)
- NATURVETENSKAP -- Biologi -- Cellbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Cell Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Immunologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Immunology (hsv//eng)
Keyword
- Herpesvirus
- glycosaminoglycan
- glycoprotein
- surface plasmon resonance (SPR)
- carbohydrate-binding protein
- mucin-like region
- glycosylation
- mucin-like region
Publication and Content Type
- ref (subject category)
- art (subject category)
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Altgärde, Noomi, ...
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Eriksson, Charlo ...
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Peerboom, Nadia, ...
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Phan Xuan, Tuan, ...
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Möller, Stephani ...
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Schnabelrauch, M ...
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show more...
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Svedhem, Sofia, ...
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Trybala, Edward, ...
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Bergström, Tomas ...
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Bally, Marta, 19 ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
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and Polymer Chemistr ...
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- ENGINEERING AND TECHNOLOGY
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ENGINEERING AND ...
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and Medical Engineer ...
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and Medical Laborato ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Cell Biology
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Medical Biotechn ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Immunology
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Journal of Biolo ...
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University of Gothenburg
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Chalmers University of Technology