Sandbox Reserved 1794: Difference between revisions

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== HBV Binding and Infection==

NTCP is the only [https://rupress.org/jcb/article/195/7/1071/54877/The-cell-biology-of-receptor-mediated-virus entry receptor] into the liver for HBV. <Ref name = "Asami"/> The [https://en.wikipedia.org/wiki/Myristoylation myristolated] PreS1 domain of HBV binds to NTCP through a <scene name='95/952721/Hbv_patch/2'>hydrophobic patch</scene> containing ~~~~residues 157-165 on the open pore surface. <Ref name = "Asami"/> These residues form part of the tunnel resulting in HBV binding and bile salt transport directly competing and interfering with one another. <Ref name = "Asami"/> Another hydrophobic patch consisting of ~~~~residues 84-87 found on the N-terminus of NTCP does not overlap with bile salt binding and may be used for the development of [https://en.wikipedia.org/wiki/Antiviral_drug antivirals] that don't inhibit bile uptake <Ref name = "Park"/>. Other minor variations within NTCP provide species specificity for HBV or virus resistance, such as mutant S267F found in East Asia. <Ref name = "Park"/>

NTCP is the only [https://rupress.org/jcb/article/195/7/1071/54877/The-cell-biology-of-receptor-mediated-virus entry receptor] into the liver for HBV. <Ref name = "Asami"/> The [https://en.wikipedia.org/wiki/Myristoylation myristolated] PreS1 domain of HBV binds to NTCP through a <scene name='95/952721/Hbv_patch/2'>hydrophobic patch</scene> containing residues 157-165 on the open pore surface. <Ref name = "Asami"/> These residues form part of the tunnel resulting in HBV binding and bile salt transport directly competing and interfering with one another. <Ref name = "Asami"/> Another hydrophobic patch consisting of residues 84-87 found on the N-terminus of NTCP does not overlap with bile salt binding and may be used for the development of [https://en.wikipedia.org/wiki/Antiviral_drug antivirals] that don't inhibit bile uptake <Ref name = "Park"/>. Other minor variations within NTCP provide species specificity for HBV or virus resistance, such as mutant S267F found in East Asia. <Ref name = "Park"/>

The exact mechanism by which NTCP mediates viral internalization is still yet to be determined; however, current studies speculate it works through [https://en.wikipedia.org/wiki/Viral_entry#Entry_via_endocytosis endocytosis.] <Ref name = "Herrscher"> Herrscher C, Roingeard P, Blanchard E. Hepatitis B Virus Entry into Cells. Cells. 2020 Jun 18;9(6):1486. doi: 10.3390/cells9061486. PMID: 32570893; PMCID: PMC7349259. </ref> Once HBV is bound the NTCP/HBV complex is taken into the cell where viral contents are dumped into the cytoplasm to then begin [https://en.wikipedia.org/wiki/Viral_replication viral replication]. It is currently unknown whether HBV also interacts with other receptors or host cell factors, but NTCP alone is not sufficient for infection. <Ref name = "Herrscher"/>

Sandbox Reserved 1794: Difference between revisions

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@@ Line 35: / Line 35: @@
 == HBV Binding and Infection==
-NTCP is the only [https://rupress.org/jcb/article/195/7/1071/54877/The-cell-biology-of-receptor-mediated-virus entry receptor] into the liver for HBV. <Ref name = "Asami"/> The [https://en.wikipedia.org/wiki/Myristoylation myristolated] PreS1 domain of HBV binds to NTCP through a <scene name='95/952721/Hbv_patch/2'>hydrophobic patch</scene> containing <b><font color='#00e080'><b>residues 157-165</b></font> on the open pore surface. <Ref name = "Asami"/> These residues form part of the tunnel resulting in HBV binding and bile salt transport directly competing and interfering with one another. <Ref name = "Asami"/> Another hydrophobic patch consisting of <b><font color='#00e080'><b>residues 84-87</b></font> found on the N-terminus of NTCP does not overlap with bile salt binding and may be used for the development of [https://en.wikipedia.org/wiki/Antiviral_drug antivirals] that don't inhibit bile uptake <Ref name = "Park"/>. Other minor variations within NTCP provide species specificity for HBV or virus resistance, such as mutant S267F found in East Asia. <Ref name = "Park"/>
+NTCP is the only [https://rupress.org/jcb/article/195/7/1071/54877/The-cell-biology-of-receptor-mediated-virus entry receptor] into the liver for HBV. <Ref name = "Asami"/> The [https://en.wikipedia.org/wiki/Myristoylation myristolated] PreS1 domain of HBV binds to NTCP through a <scene name='95/952721/Hbv_patch/2'>hydrophobic patch</scene> containing <font color='#00e080'><b>residues 157-165</b></font> on the open pore surface. <Ref name = "Asami"/> These residues form part of the tunnel resulting in HBV binding and bile salt transport directly competing and interfering with one another. <Ref name = "Asami"/> Another hydrophobic patch consisting of <font color='#00e080'><b>residues 84-87</b></font> found on the N-terminus of NTCP does not overlap with bile salt binding and may be used for the development of [https://en.wikipedia.org/wiki/Antiviral_drug antivirals] that don't inhibit bile uptake <Ref name = "Park"/>. Other minor variations within NTCP provide species specificity for HBV or virus resistance, such as mutant S267F found in East Asia. <Ref name = "Park"/>
 The exact mechanism by which NTCP mediates viral internalization is still yet to be determined; however, current studies speculate it works through [https://en.wikipedia.org/wiki/Viral_entry#Entry_via_endocytosis endocytosis.] <Ref name = "Herrscher"> Herrscher C, Roingeard P, Blanchard E. Hepatitis B Virus Entry into Cells. Cells. 2020 Jun 18;9(6):1486. doi: 10.3390/cells9061486. PMID: 32570893; PMCID: PMC7349259. </ref> Once HBV is bound the NTCP/HBV complex is taken into the cell where viral contents are dumped into the cytoplasm to then begin [https://en.wikipedia.org/wiki/Viral_replication viral replication]. It is currently unknown whether HBV also interacts with other receptors or host cell factors, but NTCP alone is not sufficient for infection. <Ref name = "Herrscher"/>