Inhibition of Viral Membrane Fusion by Peptides and Approaches to Peptide Design

Düzgüneş, Nejat; Fernández-Fuentes, Narcís; Konopka, Krystyna

doi:10.3390/pathogens10121599

Cited by 18 publications

(12 citation statements)

References 188 publications

(227 reference statements)

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“…Costin et al ( 2010 ) designed a peptide AVP1056 (DN57opt), which interacts with the Dengue Virus E protein and inhibits viral infection in culture. The peptide AVP1056 inhibits virus binding to cells through binding directly to the E protein (Düzgüneş et al 2021 ). In our molecular docking study, AVP1056 is ranked first (docking score of -305.87) and interacts with ARG107, PHE104, SER108, TYR63, SER60, and SER110 residues of the modeled RBD of omicron (Fig.…”

Section: Resultsmentioning

confidence: 99%

Identification of antiviral peptide inhibitors for receptor binding domain of SARS-CoV-2 omicron and its sub-variants: an in-silico approach

et al. 2022

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Omicron, a variant of concern (VOC) of SARS-CoV-2, emerged in South Africa in November 2021. Omicron has been continuously acquiring a series of new mutations, especially in the spike (S) protein that led to high infectivity and transmissibility. Peptides targeting the receptor-binding domain (RBD) of the spike protein by which omicron and its variants attach to the host receptor, angiotensin-converting enzyme (ACE2) can block the viral infection at the first step. This study aims to identify antiviral peptides from the Antiviral peptide database (AVPdb) and HIV-inhibitory peptide database (HIPdb) against the RBD of omicron by using a molecular docking approach. The lead RBD binder peptides obtained through molecular docking were screened for allergenicity and physicochemical criteria (isoelectric point (pI) and net charge) required for peptide-based drugs. The binding affinity of the best five peptide inhibitors with the RBD of omicron was validated further by molecular dynamics (MD) simulation. Our result introduces five antiviral peptides, including AVP1056, AVP1059, AVP1225, AVP1801, and HIP755, that may effectively hinder omicron-host interactions. It is worth mentioning that all the three major sub-variants of omicron, BA.1 (B.1.1.529.1), BA.2 (B.1.1.529.2), and BA.3 (B.1.1.529.3), exhibits conserved ACE-2 interacting residues. Hence, the screened antiviral peptides with similar affinity can also interrupt the RBD-mediated invasion of different major sub-variants of omicron. Altogether, these peptides can be considered in the peptide-based therapeutics development for omicron treatment after further experimentation. Supplementary Information The online version contains supplementary material available at 10.1007/s13205-022-03258-4.

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Section: Resultsmentioning

confidence: 99%

Identification of antiviral peptide inhibitors for receptor binding domain of SARS-CoV-2 omicron and its sub-variants: an in-silico approach

et al. 2022

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“…Inhibitors able to prevent this structural refolding offer a great deal of therapeutic and commercial potential since they block the infection prior to the virus’ entry into the host cells. FP inhibitors have not been largely used for interfering with the fusion/entry process with respect to HR-derived inhibitors [ 44 , 54 , 55 , 56 , 57 , 58 ]. To date, only a few studies have reported FP-targeted peptides as anti-HIV agents [ 59 , 60 , 61 ].…”

Section: Discussionmentioning

confidence: 99%

SARS-CoV-2 Fusion Peptide Conjugated to a Tetravalent Dendrimer Selectively Inhibits Viral Infection

Zannella,

Chianese,

Monti

et al. 2023

Pharmaceutics

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Fusion is a key event for enveloped viruses, through which viral and cell membranes come into close contact. This event is mediated by viral fusion proteins, which are divided into three structural and functional classes. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein belongs to class I fusion proteins, characterized by a trimer of helical hairpins and an internal fusion peptide (FP), which is exposed once fusion occurs. Many efforts have been directed at finding antivirals capable of interfering with the fusion mechanism, mainly by designing peptides on the two heptad-repeat regions present in class I viral fusion proteins. Here, we aimed to evaluate the anti-SARS-CoV-2 activity of the FP sequence conjugated to a tetravalent dendrimer through a classical organic nucleophilic substitution reaction (SN2) using a synthetic bromoacetylated peptide mimicking the FP and a branched scaffold of poly-L-Lysine functionalized with cysteine residues. We found that the FP peptide conjugated to the dendrimer, unlike the monomeric FP sequence, has virucidal activity by impairing the attachment of SARS-CoV-2 to cells. Furthermore, we found that the peptide dendrimer does not have the same effects on other coronaviruses, demonstrating that it is selective against SARS-CoV-2.

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“…Viral S protein interacts with receptor and then virus particles are wrapped in endosomes to enter host cells [ 72 ]. In endosomes, the viral envelope and membrane structure of endosomes are fused in the environment of cathepsin L (CTSL) and low pH to release the viral genome into the host cytoplasm [ 73 ]. The other is membrane fusion, through which exogenous proteases or host proteases activate the S protein upon the binding of the virus to the receptor, and that virus then enters the cytoplasm through membrane fusion.…”

Section: Secov Infection and The Involvement Of Host Factorsmentioning

confidence: 99%

Swine Enteric Coronavirus: Diverse Pathogen–Host Interactions

Yan

Sun

Zeng

et al. 2022

IJMS

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Swine enteric coronavirus (SeCoV) causes acute gastroenteritis and high mortality in newborn piglets. Since the last century, porcine transmissible gastroenteritis virus (TGEV) and porcine epidemic diarrhea virus (PEDV) have swept farms all over the world and caused substantial economic losses. In recent years, porcine delta coronavirus (PDCoV) and swine acute diarrhea syndrome coronavirus (SADS-CoV) have been emerging SeCoVs. Some of them even spread across species, which made the epidemic situation of SeCoV more complex and changeable. Recent studies have begun to reveal the complex SeCoV–host interaction mechanism in detail. This review summarizes the current advances in autophagy, apoptosis, and innate immunity induced by SeCoV infection. These complex interactions may be directly involved in viral replication or the alteration of some signal pathways.

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Inhibition of Viral Membrane Fusion by Peptides and Approaches to Peptide Design

Cited by 18 publications

References 188 publications

Identification of antiviral peptide inhibitors for receptor binding domain of SARS-CoV-2 omicron and its sub-variants: an in-silico approach

Identification of antiviral peptide inhibitors for receptor binding domain of SARS-CoV-2 omicron and its sub-variants: an in-silico approach

SARS-CoV-2 Fusion Peptide Conjugated to a Tetravalent Dendrimer Selectively Inhibits Viral Infection

Swine Enteric Coronavirus: Diverse Pathogen–Host Interactions

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