About: Interaction of the Dengue Virus Fusion Peptide with Membranes Assessed by NMR: The Essential Role of the Envelope Protein Trp101 for Membrane Fusion

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About: Interaction of the Dengue Virus Fusion Peptide with Membranes Assessed by NMR: The Essential Role of the Envelope Protein Trp101 for Membrane Fusion 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	Interaction of the Dengue Virus Fusion Peptide with Membranes Assessed by NMR: The Essential Role of the Envelope Protein Trp101 for Membrane Fusion
Creator	Castanho, Miguel Almeida, Fabio Carneiro, Fabiana Da Poian, Andrea Melo, Manuel Mohana-Borges, Ronaldo Sousa, Francisco Valente, Ana
Source	Elsevier; Medline; PMC
abstract	Summary Dengue virus (DV) infection depends on a step of membrane fusion, which occurs in the acidic environment of the endosome. This process is mediated by virus surface envelope glycoprotein, in which the loop between residues D98–G112 is considered to be crucial, acting as a fusion peptide. Here, we have characterized functionally and structurally the interaction between the DV fusion peptide and different model membranes by fluorescence and NMR. Its interaction was strongest in dodecylphosphocholine (DPC) micelles and anionic phosphatidylcholine/phosphatidylglycerol vesicles, the only vesicle that was fused by DV fusion peptide. The three-dimensional structure of DV fusion peptide bound to DPC micelles was solved by solution homonuclear NMR with an r.m.s.d. of 0.98 Å. The most striking result obtained from the solution structure was the hydrophobic triad formed by residues W101, L107, and F108, pointing toward the same direction, keeping the segment between G102 and G106 in a loop conformation. The interaction of DV fusion peptide with phosphatidylcholine/phosphatidylglycerol vesicles was also mapped by transfer-nuclear Overhauser enhancement (NOE) experiments, in which the majority of the NOE cross-peaks were from the hydrophobic triad, corroborating the DPC-bound structure. Substitution of the residue W101 by an alanine residue completely abolished membrane binding and, thus, fusion by the peptide and its NOE cross-peaks. In conclusion, the 15-residue DV fusion peptide has intrinsic ability to promote membrane fusion, most likely due to the hydrophobic interaction among the residues W101, L107, and F108, which maintains its loop in the correct spatial conformation.
has issue date	2009-09-25(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2009.07.035
bibo:pmid	19619560
has license	els-covid
sha1sum (hex)	dece55ca4326ff6107a8b0fffc67afdccfeb9d51
schema:url	https://doi.org/10.1016/j.jmb.2009.07.035
resource representing a document's title	Interaction of the Dengue Virus Fusion Peptide with Membranes Assessed by NMR: The Essential Role of the Envelope Protein Trp101 for Membrane Fusion
has PubMed Central identifier	PMC7094664
has PubMed identifier	19619560
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:dece55ca4326ff6107a8b0fffc67afdccfeb9d51#body_text
is schema:about of	named entity 'COMPLETELY' named entity 'SPATIAL' named entity 'MEMBRANE FUSION' named entity 'PEPTIDE' named entity 'FUSED' named entity 'EXPERIMENTS' named entity 'FUSION' named entity 'INTERACTION' named entity 'RESULT' named entity 'DENGUE VIRUS' named entity 'SOLUTION' named entity 'BOUND' named entity 'TRIAD' named entity 'TRANSFER' named entity 'VESICLES' named entity 'PROCESS' named entity 'DODECYLPHOSPHOCHOLINE' named entity 'HAVE' named entity 'ENVELOPE GLYCOPROTEIN' named entity 'VIRUS' named entity 'SUBSTITUTION' named entity 'DIRECTION' named entity 'MEDIATED' named entity 'PHOSPHATIDYLCHOLINE' named entity 'SURFACE' named entity 'MEMBRANE BINDING' named entity 'RESIDUE' named entity 'ASSESSED' named entity 'ENVELOPE PROTEIN' named entity 'DENGUE VIRUS' named entity 'MAJORITY' named entity 'MICELLES' named entity 'ITS' named entity 'MEMBRANES' named entity 'POINTING' named entity 'SEGMENT' named entity 'HERE' named entity 'D98' named entity 'ALANINE RESIDUE' named entity 'FLUORESCENCE' named entity 'ABOLISHED' named entity 'CROSS' named entity 'CONCLUSION' named entity 'MOST LIKELY' named entity 'MEMBRANE FUSION' named entity 'ENDOSOME' named entity 'STRIKING' named entity 'DIFFERENT' named entity 'STEP' named entity 'NUCLEAR OVERHAUSER ENHANCEMENT' named entity 'NMR' named entity 'ESSENTIAL' named entity 'NMR' named entity 'INTERACTION' named entity 'FUSION PEPTIDE' named entity 'ROLE' named entity 'DPC' named entity 'MAPPED' named entity 'HYDROPHOBIC INTERACTION' named entity 'MODEL' named entity 'G112' named entity 'CORRECT' named entity 'DUE TO' named entity 'CHARACTERIZED' named entity 'CONFORMATION' named entity 'OBTAINED' named entity 'M.S.' named entity 'INTRINSIC' named entity 'STRUCTURE' named entity 'FUSION PEPTIDE' named entity 'FORMED' named entity 'THREE-DIMENSIONAL' named entity 'PEAKS' named entity 'INFECTION'

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