Related ArticlesNMR investigation of domain III of Dengue virus E protein: antibody binding modulates conformational exchange in the antigen.
J Virol. 2015 Dec 4;
Authors: Moraes AH, Simonelli L, Pedotti M, Almeida FC, Varani L, Valente AP
Abstract
Domain III of Dengue virus E protein (DIII) participates in recognition of cell receptors and in structural rearrangements required for membrane fusion and ultimately viral infection; furthermore, it contains epitopes for neutralizing antibodies and has been considered a potential vaccination agent. In this work we addressed various structural aspects of DIII and their relevance for both the Dengue virus infection mechanism and antibody recognition. We provided a dynamic description of DIII at physiological and endosomal pH and in complex with the neutralizing human antibody DV32.6. We observed conformational exchange in the isolated DIII, in regions important for the packing of E protein dimers on the viral surface. This conformational diversity is likely to facilitate the partial detachment of DIII from the other E protein domains, which is required to achieve fusion to the host cellular membranes and to expose the epitopes of many anti-DIII antibodies. A comparison of DIII from two Dengue serotypes revealed many common features but also some possibly unexpected differences. Antibody binding to DIII of Dengue serotype 4 attenuated the conformational exchange in the epitope region but, somehow surprisingly, generated exchange in other parts of DIII through allosteric effects.
IMPORTANCE: Many studies have provided extensive structural information on E protein and particularly on DIII, also in complex with antibodies. However, there is very scarce information regarding the molecular dynamics of DIII and almost nothing is available on the dynamics effect of antibody binding, especially at the quantitative level. This work provides one of the very rare descriptions of the effect of antibody binding on antigen dynamics.
PMID: 26637461 [PubMed - as supplied by publisher]
[NMR paper] Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy.
Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy.
Biochem Biophys Res Commun. 2015 Jun 12;461(4):677-80
Authors: Zhu L, Yang J, Li H, Sun H, Liu J, Wang J
Abstract
The dengue virus NS2B-NS3 protease (NS2B-NS3p), an important antiviral target for drug development,...
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Determinants of Dengue Virus NS4A Protein Oligomerization - Journal of Virology
Determinants of Dengue Virus NS4A Protein Oligomerization - Journal of Virology
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Determinants of Dengue Virus NS4A Protein Oligomerization
Journal of Virology
Nuclear magnetic resonance (NMR) analysis of NS4A amino acids 17 to 80 suggests that residues L31, L52, E53, G66, and G67 could participate in oligomerization. Ala substitution for 15 flavivirus conserved NS4A residues revealed that these amino acids ...
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NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain
NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain
Abstract
Lymphocyte function-associated antigen-1 (LFA-1) is an integrin protein that transmits information across the plasma membrane through the so-called inside-out and outside-in signaling mechanisms. To investigate these mechanisms, we carried out an NMR analysis of the dynamics of the LFA-1 I-domain, which has enabled us to characterize the motions of this domain on a broad range of timescales. We studied first the internal motions on the nanosecond timescale by...
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09-05-2014 03:03 PM
[NMR paper] NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 i domain.
NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 i domain.
Related Articles NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 i domain.
Protein Sci. 2014 Aug 21;
Authors: Leung HT, Kukic P, Camilloni C, Bemporad F, DeSimone A, Aprile FA, Kumita J, Vendruscolo M
Abstract
Lymphocyte function-associated antigen-1 (LFA-1) is an integrin protein that transmits information across the plasma membrane through the...
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08-26-2014 01:25 PM
NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 i domain
NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 i domain
Abstract
Lymphocyte function-associated antigen-1 (LFA-1) is an integrin protein that transmits information across the plasma membrane through the so-called ‘inside-out’ and ‘outside-in’ signalling mechanism. To investigate this mechanism, we carried out an NMR analysis of the dynamics of the LFA-1 I-domain, which has enabled us to characterise the motions of this domain on a broad range of timescales. We studied first the internal motions on the nanosecond timescale...
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08-21-2014 06:43 PM
[NMR paper] Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
J Biochem. 2013 Oct 4;
Authors: Yuasa N, Koyama T, Subedi GP, Yamaguchi Y, Matsushita M, Fujita-Yamaguchi Y
Abstract
T-antigen (Gal?1-3GalNAc?-1-Ser/Thr), also known as...
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[NMR paper] Effect of antibody binding on protein motions studied by hydrogen-exchange labeling a
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
Related Articles Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
Biochemistry. 1992 Nov 10;31(44):10678-85
Authors: Mayne L, Paterson Y, Cerasoli D, Englander SW
We have used hydrogen-exchange labeling detected by 2D NMR to study antibody-protein interactions for two monoclonal antibodies raised against horse cytochrome c. The data show that these antibodies bind mainly to the...
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[NMR paper] An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensi
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.
Related Articles An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.
Science. 1990 Aug 17;249(4970):755-9
Authors: Paterson Y, Englander SW, Roder H
The interaction of a protein antigen, horse cytochrome c (cyt c), with a monoclonal antibody has been studied by hydrogen-deuterium (H-D) exchange labeling and two-dimensional nuclear magnetic resonance (2D NMR) methods. The H-exchange rate of residues in three...
NMR investigation of domain III of Dengue virus E protein: antibody binding modulates conformational exchange in the antigen.
Linear Mode
