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| {{Hepatitis C}}
| | #REDIRECT [[Hepatitis C virus]] |
| {{CMG}}
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| ==Overview==
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| The hepatitis C virus (HCV) is the causative agent of hepatitis C. It is a member of the genus ''[[Hepacivirus]]'' that belongs to the ''[[Flaviviridae]]'' family. It is an enveloped, single-stranded [[RNA virus]]. The RNA genome acts as a template for viral replication and eventually, protein synthesis. Humans are considered the only natural hosts for HCV. The virus is primarily transmitted by exposure to contaminated blood.
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| ==Viral Characteristics==
| | [[Category:Emergency mdicine]] |
| The hepatitis C virus (HCV) is a member of the genus ''[[Hepacivirus]]'' that belongs to the ''[[Flaviviridae]]'' family. It is an enveloped, [[single-stranded RNA]] virus that measures approximately 60 nm in diameter.
| | [[Category:Disease]] |
| | | [[Category:Up-To-Date]] |
| ==Mode of Transmission==
| | [[Category:Infectious disease]] |
| HCV is primarily transmitted by blood. Exposure to blood is observed primarily in healthcare settings, such as in blood transfusions, surgical procedures, needle injuries, and [[hemodialysis]]. Also, the role of [[intravenous drug use]] has recently emerged as a great risk for viral transmission after the relatively successful control of nosocomial [[HCV transmission]].<ref name="pmid12407572">{{cite journal| author=National Institutes of Health| title=National Institutes of Health Consensus Development Conference Statement: Management of hepatitis C: 2002--June 10-12, 2002. | journal=Hepatology | year= 2002 | volume= 36 | issue= 5 Suppl 1 | pages= S3-20 | pmid=12407572 | doi=10.1053/jhep.2002.37117 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12407572 }} </ref>
| | [[Category:Hepatology]] |
| | | [[Category:Gastroenterology]] |
| ==Life Cycle==
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| Humans are considered the only natural hosts for HCV. The full life cycle of the virus is poorly understood due to difficulty to culture ''in vitro''. The expression of E1-E2, two important envelope [[glycoprotein]] complexes, on the surface of HCV allows the virus to interact with host-cell molecules ([[glycosaminoglycans]]) by acting as ligands for cellular receptors, such as [[tetraspanin CD81]], scavenger receptor class B type I (SR-BI), and mannose binding lectins DC-SIGN and L-SIGN. This interaction is believed to have a crucial role in cell recognition and cellular tropism.<ref name="pmid11602769">{{cite journal| author=Op De Beeck A, Cocquerel L, Dubuisson J| title=Biogenesis of hepatitis C virus envelope glycoproteins. | journal=J Gen Virol | year= 2001 | volume= 82 | issue= Pt 11 | pages= 2589-95 | pmid=11602769 | doi= | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=11602769 }} </ref><ref name="pmid11356980">{{cite journal| author=Penin F, Combet C, Germanidis G, Frainais PO, Deléage G, Pawlotsky JM| title=Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment. | journal=J Virol | year= 2001 | volume= 75 | issue= 12 | pages= 5703-10 | pmid=11356980 | doi=10.1128/JVI.75.12.5703-5710.2001 | pmc=PMC114285 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=11356980 }} </ref><ref name="pmid12867431">{{cite journal| author=Barth H, Schafer C, Adah MI, Zhang F, Linhardt RJ, Toyoda H et al.| title=Cellular binding of hepatitis C virus envelope glycoprotein E2 requires cell surface heparan sulfate. | journal=J Biol Chem | year= 2003 | volume= 278 | issue= 42 | pages= 41003-12 | pmid=12867431 | doi=10.1074/jbc.M302267200 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12867431 }} </ref><ref name="pmid9794763">{{cite journal| author=Pileri P, Uematsu Y, Campagnoli S, Galli G, Falugi F, Petracca R et al.| title=Binding of hepatitis C virus to CD81. | journal=Science | year= 1998 | volume= 282 | issue= 5390 | pages= 938-41 | pmid=9794763 | doi= | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=9794763 }} </ref><ref name="pmid12913001">{{cite journal| author=Bartosch B, Vitelli A, Granier C, Goujon C, Dubuisson J, Pascale S et al.| title=Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. | journal=J Biol Chem | year= 2003 | volume= 278 | issue= 43 | pages= 41624-30 | pmid=12913001 | doi=10.1074/jbc.M305289200 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12913001 }} </ref><ref name="pmid12761383">{{cite journal| author=Hsu M, Zhang J, Flint M, Logvinoff C, Cheng-Mayer C, Rice CM et al.| title=Hepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particles. | journal=Proc Natl Acad Sci U S A | year= 2003 | volume= 100 | issue= 12 | pages= 7271-6 | pmid=12761383 | doi=10.1073/pnas.0832180100 | pmc=PMC165865 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12761383 }} </ref><ref name="pmid12356718">{{cite journal| author=Scarselli E, Ansuini H, Cerino R, Roccasecca RM, Acali S, Filocamo G et al.| title=The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. | journal=EMBO J | year= 2002 | volume= 21 | issue= 19 | pages= 5017-25 | pmid=12356718 | doi= | pmc=PMC129051 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12356718 }} </ref><ref name="pmid12609975">{{cite journal| author=Lozach PY, Lortat-Jacob H, de Lacroix de Lavalette A, Staropoli I, Foung S, Amara A et al.| title=DC-SIGN and L-SIGN are high affinity binding receptors for hepatitis C virus glycoprotein E2. | journal=J Biol Chem | year= 2003 | volume= 278 | issue= 22 | pages= 20358-66 | pmid=12609975 | doi=10.1074/jbc.M301284200 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12609975 }} </ref><ref name="pmid12634366">{{cite journal| author=Pöhlmann S, Zhang J, Baribaud F, Chen Z, Leslie GJ, Lin G et al.| title=Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR. | journal=J Virol | year= 2003 | volume= 77 | issue= 7 | pages= 4070-80 | pmid=12634366 | doi= | pmc=PMC150620 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12634366 }} </ref> The exact mechanism by which viral genome enters the host cell is poorly understood, but it is believed to be via receptor-mediated endocytosis. Then envelope glycoproteins utilize pH-dependent mechanisms to mediate fusion of the [[viral envelope]] using [[endosomal membrane]].<ref name="pmid12913001">{{cite journal| author=Bartosch B, Vitelli A, Granier C, Goujon C, Dubuisson J, Pascale S et al.| title=Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. | journal=J Biol Chem | year= 2003 | volume= 278 | issue= 43 | pages= 41624-30 | pmid=12913001 | doi=10.1074/jbc.M305289200 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12913001 }} </ref><ref name="pmid12761383">{{cite journal| author=Hsu M, Zhang J, Flint M, Logvinoff C, Cheng-Mayer C, Rice CM et al.| title=Hepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particles. | journal=Proc Natl Acad Sci U S A | year= 2003 | volume= 100 | issue= 12 | pages= 7271-6 | pmid=12761383 | doi=10.1073/pnas.0832180100 | pmc=PMC165865 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12761383 }} </ref> As soon as it is released into the cytoplasm, the viral nucleocapsid uncoats by unknown mechanisms.
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| Template [[HCV RNA]] allows viral replication to take place and protein synthesis is thus facilitated. Cap-independent protein translation takes place when [[ribosomal 40S subunit]] binds to [[internal ribosome entry site]] ([[IRES]]).<ref name="pmid1310759">{{cite journal| author=Tsukiyama-Kohara K, Iizuka N, Kohara M, Nomoto A| title=Internal ribosome entry site within hepatitis C virus RNA. | journal=J Virol | year= 1992 | volume= 66 | issue= 3 | pages= 1476-83 | pmid=1310759 | doi= | pmc=PMC240872 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=1310759 }} </ref> IRES is a [[stem-loop structure]] that is located at the [[5' untranslated region]] ([[UTR]]) of the virus and the initial 30-40 [[nucleotides]] of the viral core-encoding region.<ref name="pmid1310759">{{cite journal| author=Tsukiyama-Kohara K, Iizuka N, Kohara M, Nomoto A| title=Internal ribosome entry site within hepatitis C virus RNA. | journal=J Virol | year= 1992 | volume= 66 | issue= 3 | pages= 1476-83 | pmid=1310759 | doi= | pmc=PMC240872 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=1310759 }} </ref> Nonetheless, full polyprotein translation also requires the use of 80S ribosomes and the viral [[3' UTR]], both of which presumably play a role in regulation of the translational process.<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref>
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| [[Translation]] is accompanied by co-translational processes and followed by post-translational processes; all of which yield a total of 10 mature proteins.<ref name="pmid7679746">{{cite journal| author=Grakoui A, Wychowski C, Lin C, Feinstone SM, Rice CM| title=Expression and identification of hepatitis C virus polyprotein cleavage products. | journal=J Virol | year= 1993 | volume= 67 | issue= 3 | pages= 1385-95 | pmid=7679746 | doi= | pmc=PMC237508 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=7679746 }} </ref>
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| The following proteins are produced:
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| ====Structural Proteins:====
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| *Core (C) protein<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref>
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| *Envelope 1 (E1) glycoprotein<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref>
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| *Envelope 2 (E2) glycoprotein<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref>
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| C, E1, and E2 are separated from the remaining 7 non-structural proteins by the activity of p7, a small membrane polypeptide that belongs to viroporin family.<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref> The 3 proteins are released by the activity of signal peptidases mediated by the host cell.
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| ====Non-Structural (NS) Proteins:====
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| *NS2: Zn-dependent [[proteinase]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| *NS3: Serine-dependent [[proteinase]], [[helicase]], and [[NTPase]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| *NS4A: Cofactor NS3 [[proteinase]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| *NS4B: [[Membrane anchor]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| *NS5A: Regulation of [[RNA polymerase]] activity and inhibition of antiviral activity of [[interferon]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| *NS5B: RNA-dependent [[RNA polymerase]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| *p7: Separation of structural from non-structural proteins and possible formation of [[ion channel]]<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref><ref name="pmid14752815">{{cite journal| author=Penin F, Dubuisson J, Rey FA, Moradpour D, Pawlotsky JM| title=Structural biology of hepatitis C virus. | journal=Hepatology | year= 2004 | volume= 39 | issue= 1 | pages= 5-19 | pmid=14752815 | doi=10.1002/hep.20032 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=14752815 }} </ref>
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| Non-structural proteins NS3 to NS5B play an important role in the formation of a replication complex that includes an intracellular "membranous web", at least partially derived from host [[endoplasmic reticulum]].<ref name="pmid12021330">{{cite journal| author=Egger D, Wölk B, Gosert R, Bianchi L, Blum HE, Moradpour D et al.| title=Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. | journal=J Virol | year= 2002 | volume= 76 | issue= 12 | pages= 5974-84 | pmid=12021330 | doi= | pmc=PMC136238 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=12021330 }} </ref> The replication complex is responsible for synthesis template negative-strand RNA and consequent synthesis of its positive-strand counterpart. These RNA molecules are then enclosed in new [[virion]]s.
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| ===Formation of Nucleocapsid and Envelope===
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| New HCV nucleocapsid is formed by the action of core [[protein C]] along with viral genomic positive-strand RNA.<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref> The envelope of the newly formed nucleocapsid is later formed by budding action into the lumen of the [[endoplasmic reticulum]]. Nonetheless, envelope [[glycoproteins]] do not yet mature early on at this stage. When new virions are exported outside the host cell, via cellular secretory mechanisms, glycoproteins of the envelope finally mature.<ref name="pmid15036326">{{cite journal| author=Pawlotsky JM| title=Pathophysiology of hepatitis C virus infection and related liver disease. | journal=Trends Microbiol | year= 2004 | volume= 12 | issue= 2 | pages= 96-102 | pmid=15036326 | doi=10.1016/j.tim.2003.12.005 | pmc= | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15036326 }} </ref>
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| ==References==
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