Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells
Identifieur interne : 000D88 ( Main/Exploration ); précédent : 000D87; suivant : 000D89Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells
Auteurs : Jean Kaoru Millet ; Gary R. WhittakerSource :
- Virology [ 0042-6822 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- physiology : Cell Membrane, SARS Virus.
- Humans, Membrane Fusion, Viral Envelope Proteins, Virus Internalization.
Abstract
During viral entry, enveloped viruses require the fusion of their lipid envelope with host cell membranes. For coronaviruses, this critical step is governed by the virally-encoded spike (S) protein, a class I viral fusion protein that has several unique features. Coronavirus entry is unusual in that it is often biphasic in nature, and can occur at or near the cell surface or in late endosomes. Recent advances in structural, biochemical and molecular biology of the coronavirus S protein has shed light on the intricacies of coronavirus entry, in particular the molecular triggers of coronavirus S-mediated membrane fusion. Furthermore, characterization of the coronavirus fusion peptide (FP), the segment of the fusion protein that inserts to a target lipid bilayer during membrane fusion, has revealed its particular attributes which imparts some of the unusual properties of the S protein, such as Ca2+-dependency. These unusual characteristics can explain at least in part the biphasic nature of coronavirus entry. In this review, using severe acute respiratory syndrome coronavirus (SARS-CoV) as model virus, we give an overview of advances in research on the coronavirus fusion peptide with an emphasis on its role and properties within the biological context of host cell entry.
Url:
DOI: 10.1016/j.virol.2017.12.015
PubMed: 29275820
PubMed Central: 7112017
Affiliations:
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Whittaker</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Membrane (physiology)</term><term>Humans</term><term>Membrane Fusion</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Viral Envelope Proteins</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Humains</term><term>Membrane cellulaire (physiologie)</term><term>Protéines de l'enveloppe virale</term><term>Pénétration virale</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Membrane cellulaire</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Membrane</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Membrane Fusion</term><term>Viral Envelope Proteins</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Protéines de l'enveloppe virale</term><term>Pénétration virale</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>During viral entry, enveloped viruses require the fusion of their lipid envelope with host cell membranes. For coronaviruses, this critical step is governed by the virally-encoded spike (S) protein, a class I viral fusion protein that has several unique features. Coronavirus entry is unusual in that it is often biphasic in nature, and can occur at or near the cell surface or in late endosomes. Recent advances in structural, biochemical and molecular biology of the coronavirus S protein has shed light on the intricacies of coronavirus entry, in particular the molecular triggers of coronavirus S-mediated membrane fusion. Furthermore, characterization of the coronavirus fusion peptide (FP), the segment of the fusion protein that inserts to a target lipid bilayer during membrane fusion, has revealed its particular attributes which imparts some of the unusual properties of the S protein, such as Ca<sup>2+</sup>-dependency. These unusual characteristics can explain at least in part the biphasic nature of coronavirus entry. In this review, using severe acute respiratory syndrome coronavirus (SARS-CoV) as model virus, we give an overview of advances in research on the coronavirus fusion peptide with an emphasis on its role and properties within the biological context of host cell entry.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Apellaniz, B" uniqKey="Apellaniz B">B. Apellaniz</name></author><author><name sortKey="Huarte, N" uniqKey="Huarte N">N. Huarte</name></author><author><name sortKey="Largo, E" uniqKey="Largo E">E. Largo</name></author><author><name sortKey="Nieva, J L" uniqKey="Nieva J">J.L. Nieva</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Basso, L G" uniqKey="Basso L">L.G. Basso</name></author><author><name sortKey="Vicente, E F" uniqKey="Vicente E">E.F. Vicente</name></author><author><name sortKey="Crusca, E" uniqKey="Crusca E">E. 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|area= SrasV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= PMC:7112017
|texte= Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:29275820" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |