ID: 198
Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the re...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Gonzalez-Motos, Victor [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Übergeordnetes Werk: |
Enthalten in: The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types - McLaughlin, Richard J. ELSEVIER, 2022, the official journal of the International Cytokine Society, Oxford [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:76 ; year:2015 ; number:1 ; pages:100 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.cyto.2015.08.202 |
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| 520 | |a Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. | ||
| 520 | |a Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. | ||
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| 700 | 1 | |a Kalinke, Ulrich |4 oth | |
| 700 | 1 | |a Viejo-Borbolla, Abel |4 oth | |
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10.1016/j.cyto.2015.08.202 doi GBVA2015017000008.pica (DE-627)ELV018713645 (ELSEVIER)S1043-4666(15)00468-8 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Gonzalez-Motos, Victor verfasserin aut ID: 198 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Ritter, Birgit oth Lenac, Tihana oth Jonjic, Stipan oth Arenzana-Seisdedos, Fernando oth Kalinke, Ulrich oth Viejo-Borbolla, Abel oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:100 https://doi.org/10.1016/j.cyto.2015.08.202 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 100 045F 570 |
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10.1016/j.cyto.2015.08.202 doi GBVA2015017000008.pica (DE-627)ELV018713645 (ELSEVIER)S1043-4666(15)00468-8 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Gonzalez-Motos, Victor verfasserin aut ID: 198 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Ritter, Birgit oth Lenac, Tihana oth Jonjic, Stipan oth Arenzana-Seisdedos, Fernando oth Kalinke, Ulrich oth Viejo-Borbolla, Abel oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:100 https://doi.org/10.1016/j.cyto.2015.08.202 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 100 045F 570 |
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10.1016/j.cyto.2015.08.202 doi GBVA2015017000008.pica (DE-627)ELV018713645 (ELSEVIER)S1043-4666(15)00468-8 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Gonzalez-Motos, Victor verfasserin aut ID: 198 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Ritter, Birgit oth Lenac, Tihana oth Jonjic, Stipan oth Arenzana-Seisdedos, Fernando oth Kalinke, Ulrich oth Viejo-Borbolla, Abel oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:100 https://doi.org/10.1016/j.cyto.2015.08.202 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 100 045F 570 |
| allfieldsGer |
10.1016/j.cyto.2015.08.202 doi GBVA2015017000008.pica (DE-627)ELV018713645 (ELSEVIER)S1043-4666(15)00468-8 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Gonzalez-Motos, Victor verfasserin aut ID: 198 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Ritter, Birgit oth Lenac, Tihana oth Jonjic, Stipan oth Arenzana-Seisdedos, Fernando oth Kalinke, Ulrich oth Viejo-Borbolla, Abel oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:100 https://doi.org/10.1016/j.cyto.2015.08.202 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 100 045F 570 |
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10.1016/j.cyto.2015.08.202 doi GBVA2015017000008.pica (DE-627)ELV018713645 (ELSEVIER)S1043-4666(15)00468-8 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Gonzalez-Motos, Victor verfasserin aut ID: 198 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. Ritter, Birgit oth Lenac, Tihana oth Jonjic, Stipan oth Arenzana-Seisdedos, Fernando oth Kalinke, Ulrich oth Viejo-Borbolla, Abel oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:100 https://doi.org/10.1016/j.cyto.2015.08.202 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 100 045F 570 |
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Enthalten in The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types Oxford [u.a.] volume:76 year:2015 number:1 pages:100 |
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Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. |
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Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. |
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Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV. |
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