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- W2045752435 abstract "Hepatitis C virus (HCV) protein NS4B is a poorly characterized highly hydrophobic integral membrane protein which is associated with membranes of the ER or an ER-derived modified compartment. NS4B induces the formation of intracellular membrane changes that are visible by electron microscopy, the so called membranous web. This membranous web has been postulated to be the HCV RNA replication complex. Since morphogenesis and budding has been suggested to take place in ER modified membranes, a function of NS4B might be to induce a specific ER membrane alteration that serves as a scaffold for the formation of the HCV replication complex. If that were true, NS4B might have a critical role in the HCV cycle. It has been predicted that NS4B possess four / five transmembrane (TM) domains. Two helical elements have been predicted in the C-terminal part of the protein, pointing out to a yet unknown common function of the C-terminal globular part. Additionally, RNA binding properties through a nucleotide-binding motif have recently been reported, as well as a new membrane association segment in the N-terminal portion of the protein. Many questions remain unanswered about the NS4B topology but due to the highly hydrophobic nature of the protein, a detailed structure determination using experimental techniques will not be obtained in the near future. In order to define the membrane topology of NS4B we have analyzed the spatial distribution of the spatial hydrophobicity of thirty-one sequences of protein NS4B pertaining to different strains representing the seven major genotypes of HCV. Our study shows that NS4B has at least five and possibly six TM domains." @default.
- W2045752435 created "2016-06-24" @default.
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- W2045752435 date "2010-01-01" @default.
- W2045752435 modified "2023-09-30" @default.
- W2045752435 title "Membrane Topology of Hepatitis C Virus Protein NS4B" @default.
- W2045752435 doi "https://doi.org/10.1016/j.bpj.2009.12.283" @default.
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