Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development

An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfa...
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Gespeichert in:

Autor*in:	Dominik D. Kaltenbach [verfasserIn] Dinesh Jaishankar [verfasserIn] Meng Hao [verfasserIn] Jacob C. Beer [verfasserIn] Michael V. Volin [verfasserIn] Umesh R. Desai [verfasserIn] Vaibhav Tiwari [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry

Übergeordnetes Werk:	In: Frontiers in Pharmacology - Frontiers Media S.A., 2010, 9(2018)
Übergeordnetes Werk:	volume:9 ; year:2018

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fphar.2018.01315

Katalog-ID:	DOAJ016972597

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520			\|a An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies.
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allfields	10.3389/fphar.2018.01315 doi (DE-627)DOAJ016972597 (DE-599)DOAJd4129ca7849d4e06b24ed1eec72a4bec DE-627 ger DE-627 rakwb eng RM1-950 Dominik D. Kaltenbach verfasserin aut Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies. heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry Therapeutics. Pharmacology Dinesh Jaishankar verfasserin aut Meng Hao verfasserin aut Jacob C. Beer verfasserin aut Michael V. Volin verfasserin aut Umesh R. Desai verfasserin aut Vaibhav Tiwari verfasserin aut In Frontiers in Pharmacology Frontiers Media S.A., 2010 9(2018) (DE-627)642889392 (DE-600)2587355-6 16639812 nnns volume:9 year:2018 https://doi.org/10.3389/fphar.2018.01315 kostenfrei https://doaj.org/article/d4129ca7849d4e06b24ed1eec72a4bec kostenfrei https://www.frontiersin.org/article/10.3389/fphar.2018.01315/full kostenfrei https://doaj.org/toc/1663-9812 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018
spelling	10.3389/fphar.2018.01315 doi (DE-627)DOAJ016972597 (DE-599)DOAJd4129ca7849d4e06b24ed1eec72a4bec DE-627 ger DE-627 rakwb eng RM1-950 Dominik D. Kaltenbach verfasserin aut Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies. heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry Therapeutics. Pharmacology Dinesh Jaishankar verfasserin aut Meng Hao verfasserin aut Jacob C. Beer verfasserin aut Michael V. Volin verfasserin aut Umesh R. Desai verfasserin aut Vaibhav Tiwari verfasserin aut In Frontiers in Pharmacology Frontiers Media S.A., 2010 9(2018) (DE-627)642889392 (DE-600)2587355-6 16639812 nnns volume:9 year:2018 https://doi.org/10.3389/fphar.2018.01315 kostenfrei https://doaj.org/article/d4129ca7849d4e06b24ed1eec72a4bec kostenfrei https://www.frontiersin.org/article/10.3389/fphar.2018.01315/full kostenfrei https://doaj.org/toc/1663-9812 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018
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allfieldsGer	10.3389/fphar.2018.01315 doi (DE-627)DOAJ016972597 (DE-599)DOAJd4129ca7849d4e06b24ed1eec72a4bec DE-627 ger DE-627 rakwb eng RM1-950 Dominik D. Kaltenbach verfasserin aut Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies. heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry Therapeutics. Pharmacology Dinesh Jaishankar verfasserin aut Meng Hao verfasserin aut Jacob C. Beer verfasserin aut Michael V. Volin verfasserin aut Umesh R. Desai verfasserin aut Vaibhav Tiwari verfasserin aut In Frontiers in Pharmacology Frontiers Media S.A., 2010 9(2018) (DE-627)642889392 (DE-600)2587355-6 16639812 nnns volume:9 year:2018 https://doi.org/10.3389/fphar.2018.01315 kostenfrei https://doaj.org/article/d4129ca7849d4e06b24ed1eec72a4bec kostenfrei https://www.frontiersin.org/article/10.3389/fphar.2018.01315/full kostenfrei https://doaj.org/toc/1663-9812 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018
allfieldsSound	10.3389/fphar.2018.01315 doi (DE-627)DOAJ016972597 (DE-599)DOAJd4129ca7849d4e06b24ed1eec72a4bec DE-627 ger DE-627 rakwb eng RM1-950 Dominik D. Kaltenbach verfasserin aut Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies. heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry Therapeutics. Pharmacology Dinesh Jaishankar verfasserin aut Meng Hao verfasserin aut Jacob C. Beer verfasserin aut Michael V. Volin verfasserin aut Umesh R. Desai verfasserin aut Vaibhav Tiwari verfasserin aut In Frontiers in Pharmacology Frontiers Media S.A., 2010 9(2018) (DE-627)642889392 (DE-600)2587355-6 16639812 nnns volume:9 year:2018 https://doi.org/10.3389/fphar.2018.01315 kostenfrei https://doaj.org/article/d4129ca7849d4e06b24ed1eec72a4bec kostenfrei https://www.frontiersin.org/article/10.3389/fphar.2018.01315/full kostenfrei https://doaj.org/toc/1663-9812 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018
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topic_facet	heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry Therapeutics. Pharmacology
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authorswithroles_txt_mv	Dominik D. Kaltenbach @@aut@@ Dinesh Jaishankar @@aut@@ Meng Hao @@aut@@ Jacob C. Beer @@aut@@ Michael V. Volin @@aut@@ Umesh R. Desai @@aut@@ Vaibhav Tiwari @@aut@@
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callnumber-first	R - Medicine
author	Dominik D. Kaltenbach
spellingShingle	Dominik D. Kaltenbach misc RM1-950 misc heparan sulfate misc herpes simplex virus misc heparanse misc sulfotranferases misc heparan mimetic misc viral entry misc Therapeutics. Pharmacology Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development
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topic_title	RM1-950 Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development heparan sulfate herpes simplex virus heparanse sulfotranferases heparan mimetic viral entry
topic	misc RM1-950 misc heparan sulfate misc herpes simplex virus misc heparanse misc sulfotranferases misc heparan mimetic misc viral entry misc Therapeutics. Pharmacology
topic_unstemmed	misc RM1-950 misc heparan sulfate misc herpes simplex virus misc heparanse misc sulfotranferases misc heparan mimetic misc viral entry misc Therapeutics. Pharmacology
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title	Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development
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title_full	Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development
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title_sort	sulfotransferase and heparanase: remodeling engines in promoting virus infection and disease development
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title_auth	Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development
abstract	An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies.
abstractGer	An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies.
abstract_unstemmed	An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies.
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title_short	Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development
url	https://doi.org/10.3389/fphar.2018.01315 https://doaj.org/article/d4129ca7849d4e06b24ed1eec72a4bec https://www.frontiersin.org/article/10.3389/fphar.2018.01315/full https://doaj.org/toc/1663-9812
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Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development

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