Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes.

Aloia, Roland C.; Tian, Huirou; Jensen, Fred C.

doi:10.1073/pnas.90.11.5181

Cited by 393 publications

(405 citation statements)

References 47 publications

(47 reference statements)

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“…The labeled Phe-8, labeled Val-2, and unlabeled samples all contained the LM-2 lipid mixture, which approximately reflects the lipid headgroup and cholesterol composition of the target T cells of the HIV-1 virus [28]. The labeled Phe-8 and unlabeled samples used the same batch of LM-2 while the labeled Val-2 sample used a different LM-2 batch.…”

Section: Resultsmentioning

confidence: 99%

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Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides

Yang

Parkanzky

Bodner

et al. 2002

Journal of Magnetic Resonance

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Clean MAS observation of 13 C-labeled carbons in membrane-bound HIV-1 and influenza fusion peptides was made by using a rotational-echo double-resonance spectroscopy (REDOR) filter of directly bonded 13 C-15 N pairs. The clean filtering achieved with the REDOR approach is superior to filtering done with sample difference spectroscopy. In one labeling approach, the peptide had labels at a single 13 C carbonyl and its directly bonded 15 N. The resulting chemical shift distribution of the filtered signal is used to assess the distribution of local secondary structures at the labeled carbonyl. For the influenza peptide, the Leu-2 carbonyl chemical shift distribution is shown to vary markedly with lipid and detergent composition, as well as peptide:lipid ratio, suggesting that the local peptide structure also has a strong dependence on these factors. Because most carboxylic-and amino-labeled amino acids are commercially available, this REDOR approach should have broad applicability to chemically synthesized peptides as well as bacterially synthesized proteins. In a second labeling approach, the HIV-1 fusion peptide had U-13 C, 15 N labeling over three sequential residues. When a 1.6 ms REDOR dephasing time is used, only backbone 13 C signals are observed. The resulting spectra are used to determine spectral linewidths and to assess feasibility of assignment of uniformly labeled peptide.

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Section: Resultsmentioning

confidence: 99%

“…The HFP samples contained lipid/cholesterol mixtures reflecting the approximate lipid and cholesterol content of the HIV-1 virus and its target T cells [28]. Two mixtures of similar composition were used.…”

Section: Samplesmentioning

confidence: 99%

Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides

Yang

Parkanzky

Bodner

et al. 2002

Journal of Magnetic Resonance

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“…Samples were prepared using lipid/ cholesterol mixtures reflecting the approximate lipid headgroup and cholesterol content of host cells of the virus (76).…”

Section: Methodsmentioning

confidence: 99%

Solid-State Nuclear Magnetic Resonance Evidence for Parallel and Antiparallel Strand Arrangements in the Membrane-Associated HIV-1 Fusion Peptide

Yang

Weliky

2003

Biochemistry

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The HIV-1 fusion peptide serves as a useful model system for understanding viral/target cell fusion, at least to the lipid-mixing stage. Previous solid-state NMR studies have shown that the membranebound HIV-1 fusion peptide adopts an extended conformation in a lipid mixture close to that of host cells of the virus. In the present study, solid-state NMR REDOR methods were applied for detection of oligomeric strand structure. The samples were prepared under fusogenic conditions and contained equimolar amounts of two peptides, one with selective [ 13 C]carbonyl labeling and the other with selective [ 15 N]amide labeling. In the REDOR measurements, observation of reduced 13 C intensity due to hydrogen-bonded amide 15 N provides strong experimental evidence of oligomer formation by the membrane-associated peptide.Comparison of REDOR spectra on samples that were labeled at different residue positions suggests that there are both parallel and antiparallel arrangements of peptide strands. In the parallel arrangement, interpeptide hydrogen bonding decreases toward the C-terminus, while in the antiparallel arrangement, hydrogen bonds are observed along the entire length of residues which was probed (Gly-5 to Gly-16). For the parallel arrangement, these observations are consistent with the model in which the apolar N-terminal and central regions of the peptides penetrate into the membrane and hydrogen bond with one another while the polar C-terminus of the peptide is outside the membrane and hydrogen bonds with water. These measurements show that, at least at the end state of fusion, the peptide can adopt an oligomeric strand structure.Fusion between the membranes of enveloped viruses such as HIV-1 1 and influenza and the membranes of their target host cells is an essential step in infection (1-4). For these viruses, this process is mediated by integral membrane viral envelope proteins which contain N-terminal ∼20-residue apolar fusion peptide domains. For HIV-1 and influenza, the free fusion peptide has also been shown to be a useful model to understand fusion, at least to the lipid-mixing stage. The free peptide causes fusion of liposomes and erythrocytes, and numerous mutational studies have shown strong correlations between fusion peptide-induced liposome fusion and viral/host cell fusion (5-20). Recent studies suggest that envelope protein regions other than the fusion peptide also interact with membranes and play a role in fusion (21-26).There is a crystal structure of the part of the influenza hemagglutinin envelope protein which lies outside the virus and which contains the fusion peptide (27). This "ectodomain" structure corresponds to a prefusogenic conformation. For both the hemagglutinin and the HIV-1 gp41 envelope proteins, there are also atomic resolution structures of the "soluble ectodomains" which do not contain the fusion peptide (28-34). These structures are believed to correspond to the protein conformations after fusion has occurred and perhaps during fusion as well. In each of these soluble...

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“…This has implications for the properties of the envelope membrane. The envelope of HIV, for example, was found to be more ordered than that of the producer cell on average [16].…”

Section: Glmentioning

confidence: 99%

Lipidomics of host–pathogen interactions

Wenk

2006

FEBS Letters

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The cell biology of intracellular pathogens (viruses, bacteria, eukaryotic parasites) has provided us with molecular information of host-pathogen interactions. As a result it is becoming increasingly evident that lipids play important roles at various stages of host-pathogen interactions. They act in first line recognition and host cell signaling during pathogen docking, invasion and intracellular trafficking. Lipid metabolism is a housekeeping function in energy homeostasis and biomembrane synthesis during pathogen replication and persistence. Lipids of enormous chemical diversity play roles as immunomodulatory factors. Thus, novel biochemical analytics in combination with cell and molecular biology are a promising recipe for dissecting the roles of lipids in host-pathogen interactions.

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Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes.

Cited by 393 publications

References 47 publications

Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides

Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides

Solid-State Nuclear Magnetic Resonance Evidence for Parallel and Antiparallel Strand Arrangements in the Membrane-Associated HIV-1 Fusion Peptide

Lipidomics of host–pathogen interactions

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