MersV1, Main, Exploration, bibRecord, 000A17

Crystal structure of the post‐fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution

Identifieur interne : 000A17 ( Main/Exploration ); précédent : 000A16; suivant : 000A18

Crystal structure of the post‐fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution

Auteurs : Lei Yan ; Bing Meng ; Jiangchao Xiang ; Ian A. Wilson ; Bei Yang

Source :

Acta Crystallographica. Section D, Structural Biology [ 2059-7983 ] ; 2018.

RBID : PMC:6130466

Descripteurs français

KwdFr :
- Alignement de séquences, Conformation des protéines, Coronavirus humain 229E (isolement et purification), Coronavirus humain 229E (physiologie), Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus (), Humains, Infections à coronavirus (virologie), Modèles moléculaires, Protéines de fusion recombinantes (), Séquence d'acides aminés.
MESH :
- isolement et purification : Coronavirus humain 229E.
- physiologie : Coronavirus humain 229E.
- virologie : Infections à coronavirus.
- Alignement de séquences, Conformation des protéines, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Humains, Modèles moléculaires, Protéines de fusion recombinantes, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence, Coronavirus 229E, Human (isolation & purification), Coronavirus 229E, Human (physiology), Coronavirus Infections (virology), Crystallography, X-Ray, Humans, Models, Molecular, Protein Conformation, Recombinant Fusion Proteins (chemistry), Sequence Alignment, Spike Glycoprotein, Coronavirus (chemistry).
MESH :
- chemical , chemistry : Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- isolation & purification : Coronavirus 229E, Human.
- physiology : Coronavirus 229E, Human.
- virology : Coronavirus Infections.
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Models, Molecular, Protein Conformation, Sequence Alignment.

Abstract

Human coronavirus 229E (HCoV‐229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV‐229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six‐helix membrane‐fusion structure termed the fusion core. Here, the complete fusion‐core structure of HCoV‐229E has been determined at 1.86 Å resolution, representing the most complete post‐fusion conformation thus far among published human alphacoronavirus (α‐HCoV) fusion‐core structures. The overall structure of the HCoV‐229E fusion core is similar to those of SARS, MERS and HCoV‐NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side‐by‐side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α‐HCoVs and β‐HCoVs at certain positions and that the HCoV‐229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure‐based design of pan‐coronavirus small molecules or peptides to inhibit viral fusion.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6130466

DOI: 10.1107/S2059798318008318
PubMed: 30198895
PubMed Central: 6130466

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p><italic>Human coronavirus 229E</italic>
 (HCoV‐229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV‐229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six‐helix membrane‐fusion structure termed the fusion core. Here, the complete fusion‐core structure of HCoV‐229E has been determined at 1.86 Å resolution, representing the most complete post‐fusion conformation thus far among published human alphacoronavirus (α‐HCoV) fusion‐core structures. The overall structure of the HCoV‐229E fusion core is similar to those of SARS, MERS and HCoV‐NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side‐by‐side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α‐HCoVs and β‐HCoVs at certain positions and that the HCoV‐229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure‐based design of pan‐coronavirus small molecules or peptides to inhibit viral fusion.</p>
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Serveur d'exploration MERS

Crystal structure of the post‐fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution

Crystal structure of the post‐fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	Serveur d'exploration MERS
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