The nsp2 proteins of mouse hepatitis virus and SARS coronavirus are dispensable for viral replication.
Identifieur interne : 003C58 ( Main/Exploration ); précédent : 003C57; suivant : 003C59The nsp2 proteins of mouse hepatitis virus and SARS coronavirus are dispensable for viral replication.
Auteurs : Rachel L. Graham [États-Unis] ; Amy C. Sims ; Ralph S. Baric ; Mark R. DenisonSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Cadres ouverts de lecture, Cysteine endopeptidases (), Cysteine endopeptidases (physiologie), Délétion de gène, Génome viral, Lignée cellulaire, Microscopie confocale, Microscopie de fluorescence, Polyprotéines (), Réplication virale, Spécificité d'espèce, Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (physiologie), Virus du SRAS (génétique), Virus du SRAS (physiologie).
- MESH :
- génétique : Virus de l'hépatite murine, Virus du SRAS.
- physiologie : Cysteine endopeptidases, Virus de l'hépatite murine, Virus du SRAS.
- Animaux, Cadres ouverts de lecture, Cysteine endopeptidases, Délétion de gène, Génome viral, Lignée cellulaire, Microscopie confocale, Microscopie de fluorescence, Polyprotéines, Réplication virale, Spécificité d'espèce.
English descriptors
- KwdEn :
- Animals, Cell Line, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (physiology), Gene Deletion, Genome, Viral, Microscopy, Confocal, Microscopy, Fluorescence, Murine hepatitis virus (genetics), Murine hepatitis virus (physiology), Open Reading Frames, Polyproteins (chemistry), SARS Virus (genetics), SARS Virus (physiology), Species Specificity, Virus Replication.
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Polyproteins.
- chemical , physiology : Cysteine Endopeptidases.
- genetics : Murine hepatitis virus, SARS Virus.
- physiology : Murine hepatitis virus, SARS Virus.
- Animals, Cell Line, Gene Deletion, Genome, Viral, Microscopy, Confocal, Microscopy, Fluorescence, Open Reading Frames, Species Specificity, Virus Replication.
Abstract
The results presented here demonstrate that the MHV and SARS-CoV nsp2 proteins are not required for the production of infectious virus, for polyprotein expression or processing, or for viral replication complex formation in cell culture. The nsp2 protein domain resides in a region of the coronavirus replicase that is relatively nonconserved across coronaviruses. In fact, the size and amino acid sequence variability of nsp2 across the different coronaviruses has led some investigators to speculate that the nsp2 protein, along with the nsp1 and nsp3 proteins, may play host- and/or cell-specific roles in the virus life cycle. While this may be the case, it should be noted that nsp2, in some form, exists in all coronaviruses studied to date and likely plays a pivotal role in the viral life cycle. A previous study from our laboratory identified a coronavirus replicase protein that plays an important role in viral pathogenesis. Such may prove to be the case for nsp2, as well. Alternatively, beacuse nsp2 exists as a detectable precursor protein nsp2-3 prior to processing of nsp2 and nsp3 into mature proteins, nsp2 may play a critical adaptor/regulatory role for nsp3 function. Importantly, the viruses produced in this study provide a system by which the role of the nsp2 protein in viral infection can be characterized.
DOI: 10.1007/978-0-387-33012-9_10
PubMed: 17037506
Affiliations:
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Le document en format XML
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Baric</name></author><author><name sortKey="Denison, Mark R" sort="Denison, Mark R" uniqKey="Denison M" first="Mark R" last="Denison">Mark R. 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Graham</name><affiliation wicri:level="1"><nlm:affiliation>Vanderbilt University, Nashville, Tennessee 37232, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Vanderbilt University, Nashville, Tennessee 37232</wicri:regionArea><wicri:noRegion>Tennessee 37232</wicri:noRegion></affiliation></author><author><name sortKey="Sims, Amy C" sort="Sims, Amy C" uniqKey="Sims A" first="Amy C" last="Sims">Amy C. Sims</name></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name></author><author><name sortKey="Denison, Mark R" sort="Denison, Mark R" uniqKey="Denison M" first="Mark R" last="Denison">Mark R. Denison</name></author></analytic><series><title level="j">Advances in experimental medicine and biology</title><idno type="ISSN">0065-2598</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (physiology)</term><term>Gene Deletion</term><term>Genome, Viral</term><term>Microscopy, Confocal</term><term>Microscopy, Fluorescence</term><term>Murine hepatitis virus (genetics)</term><term>Murine hepatitis virus (physiology)</term><term>Open Reading Frames</term><term>Polyproteins (chemistry)</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Species Specificity</term><term>Virus Replication</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cadres ouverts de lecture</term><term>Cysteine endopeptidases ()</term><term>Cysteine endopeptidases (physiologie)</term><term>Délétion de gène</term><term>Génome viral</term><term>Lignée cellulaire</term><term>Microscopie confocale</term><term>Microscopie de fluorescence</term><term>Polyprotéines ()</term><term>Réplication virale</term><term>Spécificité d'espèce</term><term>Virus de l'hépatite murine (génétique)</term><term>Virus de l'hépatite murine (physiologie)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Polyproteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Cysteine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus de l'hépatite murine</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Virus de l'hépatite murine</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Gene Deletion</term><term>Genome, Viral</term><term>Microscopy, Confocal</term><term>Microscopy, Fluorescence</term><term>Open Reading Frames</term><term>Species Specificity</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cadres ouverts de lecture</term><term>Cysteine endopeptidases</term><term>Délétion de gène</term><term>Génome viral</term><term>Lignée cellulaire</term><term>Microscopie confocale</term><term>Microscopie de fluorescence</term><term>Polyprotéines</term><term>Réplication virale</term><term>Spécificité d'espèce</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The results presented here demonstrate that the MHV and SARS-CoV nsp2 proteins are not required for the production of infectious virus, for polyprotein expression or processing, or for viral replication complex formation in cell culture. The nsp2 protein domain resides in a region of the coronavirus replicase that is relatively nonconserved across coronaviruses. In fact, the size and amino acid sequence variability of nsp2 across the different coronaviruses has led some investigators to speculate that the nsp2 protein, along with the nsp1 and nsp3 proteins, may play host- and/or cell-specific roles in the virus life cycle. While this may be the case, it should be noted that nsp2, in some form, exists in all coronaviruses studied to date and likely plays a pivotal role in the viral life cycle. A previous study from our laboratory identified a coronavirus replicase protein that plays an important role in viral pathogenesis. Such may prove to be the case for nsp2, as well. Alternatively, beacuse nsp2 exists as a detectable precursor protein nsp2-3 prior to processing of nsp2 and nsp3 into mature proteins, nsp2 may play a critical adaptor/regulatory role for nsp3 function. Importantly, the viruses produced in this study provide a system by which the role of the nsp2 protein in viral infection can be characterized.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name><name sortKey="Denison, Mark R" sort="Denison, Mark R" uniqKey="Denison M" first="Mark R" last="Denison">Mark R. Denison</name><name sortKey="Sims, Amy C" sort="Sims, Amy C" uniqKey="Sims A" first="Amy C" last="Sims">Amy C. Sims</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Graham, Rachel L" sort="Graham, Rachel L" uniqKey="Graham R" first="Rachel L" last="Graham">Rachel L. Graham</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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