About: HIV-1 Fusion Is Blocked through Binding of GB Virus C E2D Peptides to the HIV-1 gp41 Disulfide Loop

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About: HIV-1 Fusion Is Blocked through Binding of GB Virus C E2D Peptides to the HIV-1 gp41 Disulfide Loop Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	HIV-1 Fusion Is Blocked through Binding of GB Virus C E2D Peptides to the HIV-1 gp41 Disulfide Loop
Creator	Jiang, Shibo Zou, Peng Eichler, Jutta Sticht, Heinrich Eissmann, Kristin Fleckenstein, Bernhard Gross, Andrea Jung, Susan Mueller, Sebastian Reil, Heide
Source	PMC
abstract	A strategy for antiviral drug discovery is the elucidation and imitation of viral interference mechanisms. HIV-1 patients benefit from a coinfection with GB Virus C (GBV-C), since HIV-positive individuals with long-term GBV-C viraemia show better survival rates than HIV-1 patients without persisting GBV-C. A direct influence of GBV-C on HIV-1 replication has been shown in coinfection experiments. GBV-C is a human non-pathogenic member of the flaviviridae family that can replicate in T and B cells. Therefore, GBV-C shares partly the same ecological niche with HIV-1. In earlier work we have demonstrated that recombinant glycoprotein E2 of GBV-C and peptides derived from the E2 N-terminus interfere with HIV entry. In this study we investigated the underlying mechanism. Performing a virus-cell fusion assay and temperature-arrested HIV-infection kinetics, we provide evidence that the HIV-inhibitory E2 peptides interfere with late HIV-1 entry steps after the engagement of gp120 with CD4 receptor and coreceptor. Binding and competition experiments revealed that the N-terminal E2 peptides bind to the disulfide loop region of HIV-1 transmembrane protein gp41. In conjunction with computational analyses, we identified sequence similarities between the N-termini of GBV-C E2 and the HIV-1 glycoprotein gp120. This similarity appears to enable the GBV-C E2 N-terminus to interact with the HIV-1 gp41 disulfide loop, a crucial domain involved in the gp120-gp41 interface. Furthermore, the results of the present study provide initial proof of concept that peptides targeted to the gp41 disulfide loop are able to inhibit HIV fusion and should inspire the development of this new class of HIV-1 entry inhibitors.
has issue date	2013-01-22(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0054452
bibo:pmid	23349893
has license	cc-by
sha1sum (hex)	54cbbaf44335fdc1995cb19e5a08779929fd0966
schema:url	https://doi.org/10.1371/journal.pone.0054452
resource representing a document's title	HIV-1 Fusion Is Blocked through Binding of GB Virus C E2D Peptides to the HIV-1 gp41 Disulfide Loop
has PubMed Central identifier	PMC3551756
has PubMed identifier	23349893
schema:publication	PLoS One
resource representing a document's body	covid:54cbbaf44335fdc1995cb19e5a08779929fd0966#body_text
is schema:about of	named entity 'BLOCKED' named entity 'GP41' named entity 'BINDING' named entity 'DEVELOPMENT' named entity 'PERFORMING' named entity 'INTERFERE' named entity 'INHIBITORY' named entity 'GB VIRUS C' named entity 'VIRAEMIA' named entity 'PATHOGENIC' named entity 'DISULFIDE' named entity 'EVIDENCE' named entity 'EXPERIMENTS' named entity 'DEMONSTRATED' named entity 'HUMAN' named entity 'DIRECT' named entity 'REPLICATE' named entity 'INFLUENCE' named entity 'BENEFIT' named entity 'ENGAGEMENT' named entity 'BINDING' named entity 'DOMAIN' named entity 'REVEALED' named entity 'ENTRY INHIBITORS' named entity 'FAMILY' named entity 'VIRUS' named entity 'BIND' named entity 'B CELLS' named entity 'FLAVIVIRIDAE' named entity 'CLASS' named entity 'GBV-C' named entity 'TRANSMEMBRANE PROTEIN' named entity 'PROOF OF CONCEPT' named entity 'HAVE' named entity 'CORECEPTOR' named entity 'LONG-TERM' named entity 'TEMPERATURE' named entity 'STUDY' named entity 'ASSAY' named entity 'PROVIDE' named entity 'TARGETED' named entity 'EARLIER' named entity 'DRUG DISCOVERY' named entity 'GLYCOPROTEIN' named entity 'DERIVED' named entity 'INDIVIDUALS' named entity 'PEPTIDES' named entity 'ANTIVIRAL DRUG' named entity 'IDENTIFIED' named entity 'PRESENT' named entity 'PATIENTS' named entity 'TO INHIBIT' named entity 'CONJUNCTION' named entity 'SURVIVAL RATES' named entity 'NON-' named entity 'FUSION' named entity 'LOOP' named entity 'PEPTIDES' named entity 'DISULFIDE' named entity 'INITIAL' named entity 'STRATEGY' named entity 'BETTER' named entity 'CD4 RECEPTOR' named entity 'CELL FUSION' named entity 'GP120' named entity 'COMPUTATIONAL' covid:arg/54cbbaf44335fdc1995cb19e5a08779929fd0966 named entity 'IS A' named entity 'ENTRY' named entity 'TO INTERACT WITH' named entity 'NICHE' named entity 'GB VIRUS C'

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