Eintrag weiter verarbeiten
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells
Gespeichert in:
| Zeitschriftentitel: | Journal of Virology |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | Journal of Virology, 71, 1997, 5, S. 3767-3775 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Morgenstern, K A Landro, J A Hsiao, K Lin, C Gu, Y Su, M S Thomson, J A Morgenstern, K A Landro, J A Hsiao, K Lin, C Gu, Y Su, M S Thomson, J A |
|---|---|
| author |
Morgenstern, K A Landro, J A Hsiao, K Lin, C Gu, Y Su, M S Thomson, J A |
| spellingShingle |
Morgenstern, K A Landro, J A Hsiao, K Lin, C Gu, Y Su, M S Thomson, J A Journal of Virology Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells Virology Insect Science Immunology Microbiology |
| author_sort |
morgenstern, k a |
| spelling |
Morgenstern, K A Landro, J A Hsiao, K Lin, C Gu, Y Su, M S Thomson, J A 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.71.5.3767-3775.1997 <jats:p>The hepatitis C virus (HCV) nonstructural 3 protein (NS3) is a 70-kDa multifunctional enzyme with three known catalytic activities segregated in two somewhat independent domains. The essential machinery of a serine protease is localized in the N-terminal one-third of the protein, and nucleoside triphosphatase (NTPase) and helicase activities reside in the remaining C-terminal region. NS4A is a 54-residue protein expressed immediately downstream of NS3 in the viral polyprotein, and a central stretch of hydrophobic residues in NS4A form an integral structural component of the NS3 serine protease domain. There is no evidence to suggest that the two domains of NS3 are separated by proteolytic processing in vivo. This may reflect economical packaging of essential viral replicative components, but it could also mean that there is functional interdependence between the two domains. In this study, a full-length NS3-NS4A complex was isolated after expression and autoprocessing in transiently transfected COS cells. The protein was used to examine the effects of polynucleotides on the NTPase, helicase, and protease activities. Unlike the previously reported behavior of a separately expressed NS3 helicase domain, the full NS3-NS4A complex demonstrated optimal NTPase activity between pH 7.5 and 8.5. All three NS3-NS4A activities were modulated by polynucleotides, with poly(U) having the most remarkable effect. These findings suggest that the domains within NS3 may influence the activity of one another and that the interplay of HCV genomic elements may regulate the enzyme activities of this complex HCV replicase component.</jats:p> Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells Journal of Virology |
| doi_str_mv |
10.1128/jvi.71.5.3767-3775.1997 |
| facet_avail |
Online Free |
| finc_class_facet |
Medizin Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qdmkuNzEuNS4zNzY3LTM3NzUuMTk5Nw |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qdmkuNzEuNS4zNzY3LTM3NzUuMTk5Nw |
| institution |
DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 |
| imprint |
American Society for Microbiology, 1997 |
| imprint_str_mv |
American Society for Microbiology, 1997 |
| issn |
1098-5514 0022-538X |
| issn_str_mv |
1098-5514 0022-538X |
| language |
English |
| mega_collection |
American Society for Microbiology (CrossRef) |
| match_str |
morgenstern1997polynucleotidemodulationoftheproteasenucleosidetriphosphataseandhelicaseactivitiesofahepatitiscvirusns3ns4acomplexisolatedfromtransfectedcoscells |
| publishDateSort |
1997 |
| publisher |
American Society for Microbiology |
| recordtype |
ai |
| record_format |
ai |
| series |
Journal of Virology |
| source_id |
49 |
| title |
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_unstemmed |
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_full |
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_fullStr |
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_full_unstemmed |
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_short |
Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_sort |
polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis c virus ns3-ns4a complex isolated from transfected cos cells |
| topic |
Virology Insect Science Immunology Microbiology |
| url |
http://dx.doi.org/10.1128/jvi.71.5.3767-3775.1997 |
| publishDate |
1997 |
| physical |
3767-3775 |
| description |
<jats:p>The hepatitis C virus (HCV) nonstructural 3 protein (NS3) is a 70-kDa multifunctional enzyme with three known catalytic activities segregated in two somewhat independent domains. The essential machinery of a serine protease is localized in the N-terminal one-third of the protein, and nucleoside triphosphatase (NTPase) and helicase activities reside in the remaining C-terminal region. NS4A is a 54-residue protein expressed immediately downstream of NS3 in the viral polyprotein, and a central stretch of hydrophobic residues in NS4A form an integral structural component of the NS3 serine protease domain. There is no evidence to suggest that the two domains of NS3 are separated by proteolytic processing in vivo. This may reflect economical packaging of essential viral replicative components, but it could also mean that there is functional interdependence between the two domains. In this study, a full-length NS3-NS4A complex was isolated after expression and autoprocessing in transiently transfected COS cells. The protein was used to examine the effects of polynucleotides on the NTPase, helicase, and protease activities. Unlike the previously reported behavior of a separately expressed NS3 helicase domain, the full NS3-NS4A complex demonstrated optimal NTPase activity between pH 7.5 and 8.5. All three NS3-NS4A activities were modulated by polynucleotides, with poly(U) having the most remarkable effect. These findings suggest that the domains within NS3 may influence the activity of one another and that the interplay of HCV genomic elements may regulate the enzyme activities of this complex HCV replicase component.</jats:p> |
| container_issue |
5 |
| container_start_page |
3767 |
| container_title |
Journal of Virology |
| container_volume |
71 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792337202572689411 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T15:12:36.252Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Polynucleotide+modulation+of+the+protease%2C+nucleoside+triphosphatase%2C+and+helicase+activities+of+a+hepatitis+C+virus+NS3-NS4A+complex+isolated+from+transfected+COS+cells&rft.date=1997-05-01&genre=article&issn=1098-5514&volume=71&issue=5&spage=3767&epage=3775&pages=3767-3775&jtitle=Journal+of+Virology&atitle=Polynucleotide+modulation+of+the+protease%2C+nucleoside+triphosphatase%2C+and+helicase+activities+of+a+hepatitis+C+virus+NS3-NS4A+complex+isolated+from+transfected+COS+cells&aulast=Thomson&aufirst=J+A&rft_id=info%3Adoi%2F10.1128%2Fjvi.71.5.3767-3775.1997&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792337202572689411 |
| author | Morgenstern, K A, Landro, J A, Hsiao, K, Lin, C, Gu, Y, Su, M S, Thomson, J A |
| author_facet | Morgenstern, K A, Landro, J A, Hsiao, K, Lin, C, Gu, Y, Su, M S, Thomson, J A, Morgenstern, K A, Landro, J A, Hsiao, K, Lin, C, Gu, Y, Su, M S, Thomson, J A |
| author_sort | morgenstern, k a |
| container_issue | 5 |
| container_start_page | 3767 |
| container_title | Journal of Virology |
| container_volume | 71 |
| description | <jats:p>The hepatitis C virus (HCV) nonstructural 3 protein (NS3) is a 70-kDa multifunctional enzyme with three known catalytic activities segregated in two somewhat independent domains. The essential machinery of a serine protease is localized in the N-terminal one-third of the protein, and nucleoside triphosphatase (NTPase) and helicase activities reside in the remaining C-terminal region. NS4A is a 54-residue protein expressed immediately downstream of NS3 in the viral polyprotein, and a central stretch of hydrophobic residues in NS4A form an integral structural component of the NS3 serine protease domain. There is no evidence to suggest that the two domains of NS3 are separated by proteolytic processing in vivo. This may reflect economical packaging of essential viral replicative components, but it could also mean that there is functional interdependence between the two domains. In this study, a full-length NS3-NS4A complex was isolated after expression and autoprocessing in transiently transfected COS cells. The protein was used to examine the effects of polynucleotides on the NTPase, helicase, and protease activities. Unlike the previously reported behavior of a separately expressed NS3 helicase domain, the full NS3-NS4A complex demonstrated optimal NTPase activity between pH 7.5 and 8.5. All three NS3-NS4A activities were modulated by polynucleotides, with poly(U) having the most remarkable effect. These findings suggest that the domains within NS3 may influence the activity of one another and that the interplay of HCV genomic elements may regulate the enzyme activities of this complex HCV replicase component.</jats:p> |
| doi_str_mv | 10.1128/jvi.71.5.3767-3775.1997 |
| facet_avail | Online, Free |
| finc_class_facet | Medizin, Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qdmkuNzEuNS4zNzY3LTM3NzUuMTk5Nw |
| imprint | American Society for Microbiology, 1997 |
| imprint_str_mv | American Society for Microbiology, 1997 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
| issn | 1098-5514, 0022-538X |
| issn_str_mv | 1098-5514, 0022-538X |
| language | English |
| last_indexed | 2024-03-01T15:12:36.252Z |
| match_str | morgenstern1997polynucleotidemodulationoftheproteasenucleosidetriphosphataseandhelicaseactivitiesofahepatitiscvirusns3ns4acomplexisolatedfromtransfectedcoscells |
| mega_collection | American Society for Microbiology (CrossRef) |
| physical | 3767-3775 |
| publishDate | 1997 |
| publishDateSort | 1997 |
| publisher | American Society for Microbiology |
| record_format | ai |
| recordtype | ai |
| series | Journal of Virology |
| source_id | 49 |
| spelling | Morgenstern, K A Landro, J A Hsiao, K Lin, C Gu, Y Su, M S Thomson, J A 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.71.5.3767-3775.1997 <jats:p>The hepatitis C virus (HCV) nonstructural 3 protein (NS3) is a 70-kDa multifunctional enzyme with three known catalytic activities segregated in two somewhat independent domains. The essential machinery of a serine protease is localized in the N-terminal one-third of the protein, and nucleoside triphosphatase (NTPase) and helicase activities reside in the remaining C-terminal region. NS4A is a 54-residue protein expressed immediately downstream of NS3 in the viral polyprotein, and a central stretch of hydrophobic residues in NS4A form an integral structural component of the NS3 serine protease domain. There is no evidence to suggest that the two domains of NS3 are separated by proteolytic processing in vivo. This may reflect economical packaging of essential viral replicative components, but it could also mean that there is functional interdependence between the two domains. In this study, a full-length NS3-NS4A complex was isolated after expression and autoprocessing in transiently transfected COS cells. The protein was used to examine the effects of polynucleotides on the NTPase, helicase, and protease activities. Unlike the previously reported behavior of a separately expressed NS3 helicase domain, the full NS3-NS4A complex demonstrated optimal NTPase activity between pH 7.5 and 8.5. All three NS3-NS4A activities were modulated by polynucleotides, with poly(U) having the most remarkable effect. These findings suggest that the domains within NS3 may influence the activity of one another and that the interplay of HCV genomic elements may regulate the enzyme activities of this complex HCV replicase component.</jats:p> Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells Journal of Virology |
| spellingShingle | Morgenstern, K A, Landro, J A, Hsiao, K, Lin, C, Gu, Y, Su, M S, Thomson, J A, Journal of Virology, Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells, Virology, Insect Science, Immunology, Microbiology |
| title | Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_full | Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_fullStr | Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_full_unstemmed | Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_short | Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| title_sort | polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis c virus ns3-ns4a complex isolated from transfected cos cells |
| title_unstemmed | Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells |
| topic | Virology, Insect Science, Immunology, Microbiology |
| url | http://dx.doi.org/10.1128/jvi.71.5.3767-3775.1997 |