The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation

Lombana, Laura; Ortega-Atienza, Sara; Gómez-Gutiérrez, Julián; Yelamos, Belèn; Gavilanes, Francisco

doi:10.1016/j.virusres.2016.02.009

Cited by 7 publications

(6 citation statements)

References 53 publications

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“…Furthermore, several studies have identified a hydrophobic region in E1 (CSALYVGDLC) that may represent a putative fusion peptide [104][105][106]. An E1 deletion mutant (lacking residues 268-292) was defective in its ability to form fusion pores and thus rendered HCV pseudoparticles non-infectious [107]. Another recent study identified a central hydrophobic region in E1 that controls requirements for low pH-dependent fusion [108].…”

Section: Viral Determinants Of Fusion: E1 and E2 Glycoproteinsmentioning

confidence: 99%

Hepatitis C Virus Entry: An Intriguingly Complex and Highly Regulated Process

Colpitts

Tsai

Zeisel

2020

IJMS

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Hepatitis C virus (HCV) is a major cause of chronic hepatitis and liver disease worldwide. Its tissue and species tropism are largely defined by the viral entry process that is required for subsequent productive viral infection and establishment of chronic infection. This review provides an overview of the viral and host factors involved in HCV entry into hepatocytes, summarizes our understanding of the molecular mechanisms governing this process and highlights the therapeutic potential of host-targeting entry inhibitors.

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Section: Viral Determinants Of Fusion: E1 and E2 Glycoproteinsmentioning

confidence: 99%

Hepatitis C Virus Entry: An Intriguingly Complex and Highly Regulated Process

Colpitts

Tsai

Zeisel

2020

IJMS

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“…It is currently believed that the E1 of both BVDV and hepatitis C virus is a fusion protein. Although conserved hydrophobic sequence in E1 (CSALYVGDLC, residues 272–281) is essential for HCV fusion [ 35 , 36 , 37 , 38 , 39 , 40 ], the similar hydrophobic sequence in BVDV E1 has not been determined yet. Thus, the role of E1 in the entry of BVDV into cells is unclear and requires further study.…”

Section: Viral Proteins That Mediate Bvdv Entry: E Rns ...mentioning

confidence: 99%

Host Cell Receptors Implicated in the Cellular Tropism of BVDV

Sun

et al. 2022

Viruses

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Bovine viral diarrhea virus (BVDV) is one of the most hazardous viruses, which causes huge economic losses in the cattle industry around the world. In recent years, there has been a continuous increase in the diversity of pestivirus worldwide. As a member of the genus Pestivirus in the Flaviviridae family, BVDV has a wide range of host animals including cattle, goat, sheep, pig, camel and other cloven-hoofed animals, and it has multi-tissue tropism as well. The recognition of their permissive cells by viruses via interaction with the cellular receptors is a prerequisite for successful infection. So far, little is known about the cellular receptors essential for BVDV entry and their detailed functions during BVDV infection. Thus, discovery of the cellular receptors involved in the entry of BVDV and other pestiviruses is significant for development of the novel intervention. The viral envelope glycoprotein Erns and E2 are crucial determinants of the cellular tropism of BVDV. The cellular proteins bound with Erns and E2 potentially participate in BVDV entry, and their abundance might determine the cellular tropism of BVDV. Here, we summarize current knowledge regarding the cellular molecules have been described for BVDV entry, such as, complement regulatory protein 46 (CD46), heparan sulfate (HS), the low-density lipoprotein (LDL) receptor, and a disintegrin and metalloproteinase 17 (ADAM17). Furthermore, we focus on their implications of the recently identified cellular receptors for pestiviruses in BVDV life cycle. This knowledge provides a theoretical basis for BVDV prevention and treatment by targeting the cellular receptors essential for BVDV infection.

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“…The putative region was studied by the synthesis of a truncated chimeric protein, as described by both Lombana et al and Tong et al ( Lombana et al, 2016 ; Tong et al, 2017 ). The protein is lacking the residues (268–292), which did not modify the overall structure.…”

Section: Case Study: Hepatitis C Virusmentioning

confidence: 99%

“…The protein is lacking the residues (268–292), which did not modify the overall structure. Both the native and chimeric proteins showed destabilization of the membrane, but in the case of the chimeric protein, a 15-fold higher concentration was needed for the membrane leakage test ( Lombana et al, 2016 ). In both studies, a decrease of infectivity was observed when comparing the protein lacking the putative region and the native protein.…”

Section: Case Study: Hepatitis C Virusmentioning

confidence: 99%

Identification and Characteristics of Fusion Peptides Derived From Enveloped Viruses

et al. 2021

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Membrane fusion events allow enveloped viruses to enter and infect cells. The study of these processes has led to the identification of a number of proteins that mediate this process. These proteins are classified according to their structure, which vary according to the viral genealogy. To date, three classes of fusion proteins have been defined, but current evidence points to the existence of additional classes. Despite their structural differences, viral fusion processes follow a common mechanism through which they exert their actions. Additional studies of the viral fusion proteins have demonstrated the key role of specific proteinogenic subsequences within these proteins, termed fusion peptides. Such peptides are able to interact and insert into membranes for which they hold interest from a pharmacological or therapeutic viewpoint. Here, the different characteristics of fusion peptides derived from viral fusion proteins are described. These criteria are useful to identify new fusion peptides. Moreover, this review describes the requirements of synthetic fusion peptides derived from fusion proteins to induce fusion by themselves. Several sequences of the viral glycoproteins E1 and E2 of HCV were, for example, identified to be able to induce fusion, which are reviewed here.

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The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation

Cited by 7 publications

References 53 publications

Hepatitis C Virus Entry: An Intriguingly Complex and Highly Regulated Process

Hepatitis C Virus Entry: An Intriguingly Complex and Highly Regulated Process

Host Cell Receptors Implicated in the Cellular Tropism of BVDV

Identification and Characteristics of Fusion Peptides Derived From Enveloped Viruses

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