SARS-CoV-2 envelope protein topology in eukaryotic membranes

Duart, Gerard; García-Murria, Ma Jesús; Grau, Brayan; Acosta-Cáceres, José M.; Martínez-Gil, Luis; Mingarro, Ismael

doi:10.1101/2020.05.27.118752

Cited by 5 publications

(4 citation statements)

References 35 publications

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“…The exact function of the N‐terminus of the E protein has not been clearly identified. This region is located inside the Golgi/ER membrane, and Asn15 in the domain forms an H‐bond, which maintains the stability of the N‐terminus 57,58 . Studies have shown that homotypic interactions mediated by the N‐terminus of alternating E protein molecules may interact with each other through the luminal loops between the TMD of the proteins to initiate the rearrangement of ER membranes and induce membrane curvature.…”

Section: Differences In Amino Acid Sequence and Structure Between The Sars‐cov And Sars‐cov‐2 E Proteinsmentioning

confidence: 99%

Characterization of the SARS‐CoV‐2 E Protein: Sequence, Structure, Viroporin, and Inhibitors

et al. 2021

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The COVID-19 epidemic is one of the most influential epidemics in history. Understanding the impact of coronaviruses (CoVs) on host cells is very important for disease treatment. The SARS-CoV-2 envelope (E) protein is a small structural protein involved in many aspects of the viral life cycle. The E protein promotes the packaging and reproduction of the virus, and deletion of this protein weakens or even abolishes the virulence. This review aims to establish new knowledge by combining recent advances in the study of the SARS-CoV-2 E protein and by comparing it with the SARS-CoV E protein. The E protein amino acid sequence, structure, self-assembly characteristics, viroporin mechanisms and inhibitors are summarized and analyzed herein. Although the mechanisms of the SARS-CoV-2 and SARS-CoV E proteins are similar in many respects, specific studies on the SARS-CoV-2 E protein, for both monomers and oligomers, are still lacking. A comprehensive understanding of this protein should prompt further studies on the design and characterization of effective targeted therapeutic measures.

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Section: Differences In Amino Acid Sequence and Structure Between The Sars‐cov And Sars‐cov‐2 E Proteinsmentioning

confidence: 99%

Characterization of the SARS‐CoV‐2 E Protein: Sequence, Structure, Viroporin, and Inhibitors

et al. 2021

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“…An even-net charge distribution was discovered on both sides of the E-protein membrane. Only eight charged residues have been discovered in the protein sequence: two negatively charged residues preceding the transmembrane section, five charged residues, and one negatively charged residue in the C-terminal domain [ 17 ]. Interestingly during the replication cycle, only a few portions are assimilated into the virion envelope, and on the contrary, the protein is mostly expressed inside the infected cell [ 15 ].…”

Section: Resultsmentioning

confidence: 99%

An integrated computational approach towards the screening of active plant metabolites as potential inhibitors of SARS-CoV-2: an overview

Kushari¹,

Hazarika²,

Laloo³

et al. 2022

Struct Chem

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COVID-19 and its causative organism SARS-CoV-2 paralyzed the world and was designated a pandemic by the World Health Organization in March 2020. The worldwide health system is trying to discover an effective therapeutic measure since no clinically authorized medications are present. Screening of plant-derived pharmaceuticals may be a viable technique to fight COVID-19 in this vital situation. This review discusses the potential application of in silico approaches in developing new therapeutic molecules related to preventing SARS-CoV-2 infection. Also, it describes the binding affinity of various phytoconstituents with distinct SARS-CoV-2 target sites. In this perspective, an extensive literature survey was carried out to find the potential phytoconstituents to develop new therapeutic entities to treat COVID-19 in different online academic databases and books. Data retrieved from databases were analyzed and interpreted to conclude that many phytochemicals will bind with the 3-chymotrypsin-like (3CLpro) and papain-like proteases (PL pro ), spike glycoprotein, ACE-2, NSP15-endoribonuclease, and E protein targets of SARS-CoV-2 main protease using in silico molecular docking approach. The present investigations reveal that phytoconstituents such as curcumin, apigenin, chrysophanol, and gingerol are significantly binding with spike glycoprotein; laurolistine, acetoside, etc. are bound with M pro for anti-SARS-CoV-2 therapies. Using virtual applications of in silico studies, the current study constitutes a progressive data analysis on the mechanism of binding efficiency of distinct classes of plant metabolites against the active sites of SARS-CoV-2. Furthermore, the current review also demonstrates the fundamental necessity of the alternative and complementary medicine for future therapeutic uses of phytoconstituents by phytochemists in the fight against COVID-19.

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“…After a short centrifugation (1000 rpm for 5 min on a table-top centrifuge) cells were lysed by adding 100 μL of lysis buffer (30 mM Tris-HCl, 150 mM NaCl, 0.5% Nonidet P-40) were sonicated in an ice bath in a bioruptor (Diagenode) during 10min and centrifuged. After protein quantification, equal amounts of protein were submitted to Endo H treatment or mock-treated followed by SDS-PAGE analysis and transferred into a PVDF transfer membrane (ThermoFisher Scientific) as previously described [40]. Protein glycosylation status was analysed by Western Blot using an anti-c-myc antibody (Sigma), anti-rabbit IgG-peroxidase conjugated (Sigma), and with ECL developing reagent (GE Healthcare).…”

Section: Methodsmentioning

confidence: 99%

Intra-helical salt bridge contribution to membrane protein insertion

Duart

Lamb

Elofsson

et al. 2021

Preprint

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Salt bridges between negatively (D, E) and positively charged (K, R, H) amino acids play an important role in protein stabilization. This has a more prevalent effect in membrane proteins where polar amino acids are exposed to a very hydrophobic environment. In transmembrane (TM) helices the presence of charged residues can hinder the insertion of the helices into the membrane. This can sometimes be avoided by TM region rearrangements after insertion, but it is also possible that the formation of salt bridges could decrease the cost of membrane integration. However, the presence of intra-helical salt bridges in TM domains and their effect on insertion has not been properly studied yet. In this work, we use an analytical pipeline to study the prevalence of charged pairs of amino acid residues in TM α-helices, which shows that potentially salt-bridge forming pairs are statistically over-represented. We then selected some candidates to experimentally determine the contribution of these electrostatic interactions to the translocon-assisted membrane insertion process. Using both in vitro and in vivo systems, we confirm the presence of intra-helical salt bridges in TM segments during biogenesis and determined that they contribute between 0.5-0.7 kcal/mol to the apparent free energy of membrane insertion (ΔGapp). Our observations suggest that salt bridge interactions can be stabilized during translocon-mediated insertion and thus could be relevant to consider for the future development of membrane protein prediction software.

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SARS-CoV-2 envelope protein topology in eukaryotic membranes

Cited by 5 publications

References 35 publications

Characterization of the SARS‐CoV‐2 E Protein: Sequence, Structure, Viroporin, and Inhibitors

Characterization of the SARS‐CoV‐2 E Protein: Sequence, Structure, Viroporin, and Inhibitors

An integrated computational approach towards the screening of active plant metabolites as potential inhibitors of SARS-CoV-2: an overview

Intra-helical salt bridge contribution to membrane protein insertion

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