PittsburghV1, Main, Exploration, bibRecord, 000100

Dynamic Nuclear Polarization enhanced MAS NMR spectroscopy for structural analysis of HIV-1 protein assemblies

Identifieur interne : 000100 ( Main/Exploration ); précédent : 000099; suivant : 000101

Dynamic Nuclear Polarization enhanced MAS NMR spectroscopy for structural analysis of HIV-1 protein assemblies

Auteurs : Rupal Gupta [États-Unis] ; Manman Lu [États-Unis] ; Guangjin Hou [États-Unis] ; Marc A. Caporini [États-Unis] ; Mélanie Rosay [États-Unis] ; Werner E. Maas [États-Unis] ; Jochem Struppe [États-Unis] ; Christopher Suiter [États-Unis] ; Jinwoo Ahn [États-Unis] ; In-Ja L. Byeon [États-Unis] ; Trent W. Franks [Allemagne] ; Marcella Orwick-Rydmark [Allemagne] ; Andrea Bertarello [France] ; Hartmut Oschkinat [Allemagne] ; Anne Lesage [France] ; Guido Pintacuda [France] ; Angela M. Gronenborn [États-Unis] ; Tatyana Polenova [États-Unis]

Source :

Journal of Physical Chemistry B [ 1520-6106 ] ; 2016-01.

RBID : Hal:hal-01363595

English descriptors

mix :
- Dynamic nuclear polarization, Intermolecular correlations, Magnetic field strengths, Molecular structure, Nuclear magnetic resonance spectroscopy, Peptides, Proteins, Proteolytic cleavage, Sensitivity enhancements, Structure determination, Temperature dependence, Temperature distribution, Tubular steel structures Cryogenic temperatures, Amino acids.

Abstract

Mature infectious HIV-1 virions contain conical capsids composed of CA protein, generated by the proteolytic cleavage cascade of the Gag polyprotein, termed maturation. The mechanism of capsid core formation through the maturation process remains poorly understood. We present DNP-enhanced MAS NMR studies of tubular assemblies of CA and Gag CA-SP1 maturation intermediate and report 20-64-fold sensitivity enhancements due to DNP at 14.1 T. These sensitivity enhancements enabled direct observation of spacer peptide 1 (SP1) resonances in CA-SP1 by dipolar-based correlation experiments, unequivocally indicating that the SP1 peptide is unstructured in assembled CA-SP1 at cryogenic temperatures, corroborating our earlier results. Furthermore, the dependence of DNP enhancements and spectral resolution on magnetic field strength (9.4-18.8 T) and temperature (109-180 K) was investigated. Our results suggest that DNP-based measurements could potentially provide residue-specific dynamics information by allowing for the extraction of the temperature dependence of the anisotropic tensorial or relaxation parameters. With DNP, we were able to detect multiple well-resolved isoleucine side-chain conformers; unique intermolecular correlations across two CA molecules; and functionally relevant conformationally disordered states such as the 14-residue SP1 peptide, none of which are visible at ambient temperatures. The detection of isolated conformers and intermolecular correlations can provide crucial constraints for structure determination of these assemblies. Overall, our results establish DNP-based MAS NMR spectroscopy as an excellent tool for the characterization of HIV-1 assemblies.

Url:

https://hal.archives-ouvertes.fr/hal-01363595

DOI: 10.1021/acs.jpcb.5b12134

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<placeName><settlement type="city">Lyon</settlement>
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<author><name sortKey="Gronenborn, Angela M" sort="Gronenborn, Angela M" uniqKey="Gronenborn A" first="Angela M" last="Gronenborn">Angela M. Gronenborn</name>
<affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-465998" status="INCOMING">          <orgName>Pittsburgh Center for HIV Protein Interactions  </orgName>
          <desc>            <address>              <addrLine>University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15260, United States</addrLine>
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          </desc>
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<country>États-Unis</country>
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<author><name sortKey="Polenova, Tatyana" sort="Polenova, Tatyana" uniqKey="Polenova T" first="Tatyana" last="Polenova">Tatyana Polenova</name>
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          <desc>            <address>              <addrLine>University of Delaware, Newark, Delaware 19716, United States</addrLine>
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<idno type="DOI">10.1021/acs.jpcb.5b12134</idno>
<series><title level="j">Journal of Physical Chemistry B</title>
<idno type="ISSN">1520-6106</idno>
<imprint><date type="datePub">2016-01</date>
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<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term> Dynamic nuclear polarization</term>
<term> Intermolecular correlations</term>
<term> Magnetic field strengths</term>
<term> Molecular structure</term>
<term> Nuclear magnetic resonance spectroscopy</term>
<term> Peptides</term>
<term> Proteins</term>
<term> Proteolytic cleavage</term>
<term> Sensitivity enhancements</term>
<term> Structure determination</term>
<term> Temperature dependence</term>
<term> Temperature distribution</term>
<term> Tubular steel structures  Cryogenic temperatures</term>
<term>Amino acids</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Mature infectious HIV-1 virions contain conical capsids composed of CA protein, generated by the proteolytic cleavage cascade of the Gag polyprotein, termed maturation. The mechanism of capsid core formation through the maturation process remains poorly understood. We present DNP-enhanced MAS NMR studies of tubular assemblies of CA and Gag CA-SP1 maturation intermediate and report 20-64-fold sensitivity enhancements due to DNP at 14.1 T. These sensitivity enhancements enabled direct observation of spacer peptide 1 (SP1) resonances in CA-SP1 by dipolar-based correlation experiments, unequivocally indicating that the SP1 peptide is unstructured in assembled CA-SP1 at cryogenic temperatures, corroborating our earlier results. Furthermore, the dependence of DNP enhancements and spectral resolution on magnetic field strength (9.4-18.8 T) and temperature (109-180 K) was investigated. Our results suggest that DNP-based measurements could potentially provide residue-specific dynamics information by allowing for the extraction of the temperature dependence of the anisotropic tensorial or relaxation parameters. With DNP, we were able to detect multiple well-resolved isoleucine side-chain conformers; unique intermolecular correlations across two CA molecules; and functionally relevant conformationally disordered states such as the 14-residue SP1 peptide, none of which are visible at ambient temperatures. The detection of isolated conformers and intermolecular correlations can provide crucial constraints for structure determination of these assemblies. Overall, our results establish DNP-based MAS NMR spectroscopy as an excellent tool for the characterization of HIV-1 assemblies.</div>
</front>
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<name sortKey="Oschkinat, Hartmut" sort="Oschkinat, Hartmut" uniqKey="Oschkinat H" first="Hartmut" last="Oschkinat">Hartmut Oschkinat</name>
</country>
<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Bertarello, Andrea" sort="Bertarello, Andrea" uniqKey="Bertarello A" first="Andrea" last="Bertarello">Andrea Bertarello</name>
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Dynamic Nuclear Polarization enhanced MAS NMR spectroscopy for structural analysis of HIV-1 protein assemblies

Dynamic Nuclear Polarization enhanced MAS NMR spectroscopy for structural analysis of HIV-1 protein assemblies

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