ZHU WuYang; LI JiangJiao; LIANG GuoDong

doi:10.3967/0895-3988.2011.01.011

How does Cellular Heparan Sulfate Function in Viral Pathogenicity?

文章导航 > Biomedical and Environmental Sciences > 2011 > 24(1): 81-87

ZHU WuYang, LI JiangJiao, LIANG GuoDong. How does Cellular Heparan Sulfate Function in Viral Pathogenicity?[J]. Biomedical and Environmental Sciences, 2011, 24(1): 81-87. doi: 10.3967/0895-3988.2011.01.011

Citation:

ZHU WuYang, LI JiangJiao, LIANG GuoDong. How does Cellular Heparan Sulfate Function in Viral Pathogenicity?[J]. Biomedical and Environmental Sciences, 2011, 24(1): 81-87. doi: 10.3967/0895-3988.2011.01.011

doi: 10.3967/0895-3988.2011.01.011

基金项目: the National Natural Science Foundation of China(30970160)%the Major Science and Technology Project for Infectious Disease(2008ZX10004-001%2009ZX10004-705)%the Development Grant of the State Key Laboratory for Infectious Disease Prevention and Control(2008SKLID105)

How does Cellular Heparan Sulfate Function in Viral Pathogenicity?

Department of Viral Encephalitis, Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention and State Key Laboratory for Infectious Disease Prevention and ControlSKLID, Beijing 100052, China

Funds: the National Natural Science Foundation of China(30970160)%the Major Science and Technology Project for Infectious Disease(2008ZX10004-001%2009ZX10004-705)%the Development Grant of the State Key Laboratory for Infectious Disease Prevention and Control(2008SKLID105)

摘要: Heparan sulfate (HS) is ubiquitously expressed on the surfaces and in the extracellular matrix of virtually all cell types, making it an ideal receptor for viral infection. Compared with wild-type viruses,cell culture-adapted laboratory strains exhibit more efficient binding to cellular HS receptors. HS-binding viruses are typically cleared faster from the circulation and cause lower viremia than their non-HS-binding counterparts, suggesting that the HS-binding phenotype is a tissue culture adaptation that lowers virus fitness in vivo. However, when inoculated intracranially, efficient cell attachment through HS binding can contribute to viral neurovirulence. The primary aim of this review is to discuss the roles of HS binding in viral pathogenicity, including peripheral virulence and neurovirulence.Understanding how heparan sulfate functions during virus infection in vivo may prove critical for elucidating the molecular mechanism of viral pathogenesis, and may contribute to the development of therapeutics targeting HS.
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Abstract: Heparan sulfate (HS) is ubiquitously expressed on the surfaces and in the extracellular matrix of virtually all cell types, making it an ideal receptor for viral infection. Compared with wild-type viruses,cell culture-adapted laboratory strains exhibit more efficient binding to cellular HS receptors. HS-binding viruses are typically cleared faster from the circulation and cause lower viremia than their non-HS-binding counterparts, suggesting that the HS-binding phenotype is a tissue culture adaptation that lowers virus fitness in vivo. However, when inoculated intracranially, efficient cell attachment through HS binding can contribute to viral neurovirulence. The primary aim of this review is to discuss the roles of HS binding in viral pathogenicity, including peripheral virulence and neurovirulence.Understanding how heparan sulfate functions during virus infection in vivo may prove critical for elucidating the molecular mechanism of viral pathogenesis, and may contribute to the development of therapeutics targeting HS.
- Heparan sulfate /
- Viral pathogenicity /
- Receptor

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How does Cellular Heparan Sulfate Function in Viral Pathogenicity?

doi: 10.3967/0895-3988.2011.01.011

刊出日期: 2011-02-20

关键词:

Heparan sulfate /

Viral pathogenicity /

Receptor

摘要: Heparan sulfate (HS) is ubiquitously expressed on the surfaces and in the extracellular matrix of virtually all cell types, making it an ideal receptor for viral infection. Compared with wild-type viruses,cell culture-adapted laboratory strains exhibit more efficient binding to cellular HS receptors. HS-binding viruses are typically cleared faster from the circulation and cause lower viremia than their non-HS-binding counterparts, suggesting that the HS-binding phenotype is a tissue culture adaptation that lowers virus fitness in vivo. However, when inoculated intracranially, efficient cell attachment through HS binding can contribute to viral neurovirulence. The primary aim of this review is to discuss the roles of HS binding in viral pathogenicity, including peripheral virulence and neurovirulence.Understanding how heparan sulfate functions during virus infection in vivo may prove critical for elucidating the molecular mechanism of viral pathogenesis, and may contribute to the development of therapeutics targeting HS.

English Abstract

How does Cellular Heparan Sulfate Function in Viral Pathogenicity?

Department of Viral Encephalitis, Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention and State Key Laboratory for Infectious Disease Prevention and ControlSKLID, Beijing 100052, China

Publish Date: 2011-02-20

Keywords:

Abstract: Heparan sulfate (HS) is ubiquitously expressed on the surfaces and in the extracellular matrix of virtually all cell types, making it an ideal receptor for viral infection. Compared with wild-type viruses,cell culture-adapted laboratory strains exhibit more efficient binding to cellular HS receptors. HS-binding viruses are typically cleared faster from the circulation and cause lower viremia than their non-HS-binding counterparts, suggesting that the HS-binding phenotype is a tissue culture adaptation that lowers virus fitness in vivo. However, when inoculated intracranially, efficient cell attachment through HS binding can contribute to viral neurovirulence. The primary aim of this review is to discuss the roles of HS binding in viral pathogenicity, including peripheral virulence and neurovirulence.Understanding how heparan sulfate functions during virus infection in vivo may prove critical for elucidating the molecular mechanism of viral pathogenesis, and may contribute to the development of therapeutics targeting HS.

Citation: