Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples

Wasniewski, Christopher M.; Parkanzky, Paul; Bodner, Michele L.; Weliky, David P.

doi:10.1016/j.chemphyslip.2004.09.008

Cited by 45 publications

(50 citation statements)

References 63 publications

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“…For the HFP3-8 FLG and HFP2-14 AAG samples associated with PC:PG, there were shoulders at ~178 and 179 ppm, respectively, which correlated with helical conformation of Ala, Leu, and Phe residues. These results were consistent with previous studies of the conformation of membrane-associated HFP with peptide:lipid ~ 0.04 and with previous observations of greater preference for β strand conformation in cholesterol-containing membranes (27,28,35,55,56,59,70). The data demonstrated that samples containing HFP2-14 AAG have qualitatively larger (ΔS/ S 0 ) exp than do samples containing HFP labeled at other residues.…”

Section: Nih-pa Author Manuscriptsupporting

confidence: 92%

“…The membrane pellet with associated bound HFP was transferred to a 4 mm diameter magic angle spinning (MAS) NMR rotor. The majority of the HFP binds to membranes under these conditions and the membranes remain bilayers for HFP:lipid ~ 0.04 (27,56,59,64).A sample was also prepared for calibration of the NMR experiments and contained HFP4 (0.8 µmol) and DPPC-13 C (20 µmol). The 13 CO signal of this sample was dominated by DPPC-13 C.…”

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confidence: 99%

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Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of β Strand Peptide with Membranes and the Proximity of the Ala-14−Gly-16 Region with Lipid Headgroups

2007

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Human immunodeficiency virus (HIV) infection begins with fusion between viral and host cell membranes and is catalyzed by the HIV gp41 fusion protein. The ~20 N-terminal apolar residues of gp41 are called the HIV fusion peptide (HFP), interact with the host cell membrane, and play a key role in fusion. In this study, the membrane location of peptides which contained the HFP sequence AVGIGALFLGFLGAAGSTMGARS was probed in samples containing either only phospholipids or phospholipids and cholesterol. Four HFPs were examined which each contained 13 CO labeling at three sequential residues between G5 and G16. The 13 CO chemical shifts indicated that HFP had predominant β strand conformation over the labeled residues in the samples. The internuclear distances between the HFP 13 COs and the lipid 31 Ps were measured using solid-state nuclear magnetic resonance rotational-echo double resonance experiments. The closest 13 CO-31 P distances of 5-6 Å were observed for HFP labeled between A14 and G16 and correlated with intimate association of β strand HFP and membranes. These results were confirmed with measurements using HFPs singly 13 CO labeled at A6 or A14. To our knowledge, these data are the first measurements of distances between HIV fusion peptide nuclei and lipid P and qualitative models of membrane location of oligomeric β strand HFP are presented which are consistent with the experimental data. Observation of intimate contact between β strand HFP and membranes provides rationale for further investigation of the relationship between structure and fusion activity for this conformation. KeywordsHIV; fusion peptide; membrane; carbonyl; phosphorus; REDOR; NMR The infection of enveloped viruses such as human immunodeficiency virus (HIV) begins with fusion between the viral and host cell membranes (1-4). Fusion may be catalyzed by fusion proteins and several models of fusion protein catalysis have been proposed (2,(5)(6)(7). For HIV, fusion is catalyzed by a "gp160" glycoprotein complex which is incorporated in the virus membrane and is composed of two non-covalently associated subunits "gp120" and "gp41". The gp120 subunit lies outside the virus and binds to receptors in the target cell membrane and the gp41 subunit contains a region inside HIV as well as a single-pass transmembrane domain *To whom correspondence should be addressed. Telephone: 517-355-9715. Fax: 517-353-1793. Email: weliky@chemistry.msu.edu. † This work was supported by NIH award AI47153 to D. P. W. NIH Public Access Author ManuscriptBiochemistry. Author manuscript; available in PMC 2009 January 27. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript (8,9). The ~170-residue ectodomain of gp41 lies outside HIV and is subdivided into a more C-terminal "soluble ectodomain" and a ~20-residue N-terminal fusion peptide (HFP) which is apolar and fairly conserved. The HFP is believed to interact with the target cell membrane after gp120 binds to cellular receptors and fusion is greatly disrupted by mutation or deletion of the H...

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Section: Nih-pa Author Manuscriptsupporting

confidence: 92%

mentioning

confidence: 99%

Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of β Strand Peptide with Membranes and the Proximity of the Ala-14−Gly-16 Region with Lipid Headgroups

2007

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“…13,18,20,[22][23][24][25][27][28][29][30]32,35,37,40,47 According to these studies, the peptide is either helical, 13,25,41,42 extended, 16,18,32,37,40,43,47 or even a combination of both structures. 19,26,33,44,45 This leads to the conclusion that the gp41 FP present some structural flexibility and is able to adopt various structures depending on its environment.…”

Section: And Abmentioning

confidence: 95%

“…13,18,20,[22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] Resulting data are confusing and somehow paradoxical. The FP structure can be predominantly a-helix, 13,25,26,41,42 b-structures 16,18,31,32,37,40,43 or both.…”

Section: Introductionmentioning

confidence: 91%

The N-terminal 12 Residue Long Peptide of HIV gp41 is the Minimal Peptide Sufficient to Induce Significant T-cell-like Membrane Destabilization in Vitro

Charloteaux

Lorin

Crowet

et al. 2006

Journal of Molecular Biology

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“…Rather than exploiting sample orientation, MAS experiments average orientation-dependent interactions as an alternative approach to achieve narrow resonances, thereby increasing resolution and sensitivity in the spectrum. Several groups are currently investigating selectively labeled membrane peptides and proteins by high-resolution MAS SSNMR [83][84][85][86][87][88][89][90][91][92][93][94][95][96], or investigate on general features of these proteins [97][98][99][100][101]. The ability of SSNMR to report on structural features of fully labeled ligands interacting with integral membrane proteins was demonstrated for several systems.…”

Section: Membrane Systemsmentioning

confidence: 99%

Structural and dynamic studies of proteins by high-resolution solid-state NMR

Böckmann

2005

Comptes Rendus. Chimie

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Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples

Cited by 45 publications

References 63 publications

Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of β Strand Peptide with Membranes and the Proximity of the Ala-14−Gly-16 Region with Lipid Headgroups

Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of β Strand Peptide with Membranes and the Proximity of the Ala-14−Gly-16 Region with Lipid Headgroups

The N-terminal 12 Residue Long Peptide of HIV gp41 is the Minimal Peptide Sufficient to Induce Significant T-cell-like Membrane Destabilization in Vitro

Structural and dynamic studies of proteins by high-resolution solid-state NMR

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