Fusogenic activity of SIV (Simian Immunodeficiency Virus) peptides located in the GP32 NH2 terminal domain

Martin, Isabelle; Defrise-Quertain, Fabienne; Mandieau, Valérie; Nielsen, Nete Munk; Særmark, T.; Burny, Arsène; Brasseur, Robert; Ruysschaert, Jean‐Marie; Vandenbranden, Michel

doi:10.1016/0006-291x(91)91646-t

Cited by 87 publications

(83 citation statements)

References 16 publications

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“…Similar effects have been reported also for viral peptides (Lear and DeGrado, 1987;Martin et al 1991), signal peptides (Gierasch, 1989;Goormaghtigh et al, 1989) and synthetic amphipathic a-helical peptides (McLean et al, 1991). In the latter cases, however, the peptides are predominantly disordered in the absence of lipids and aquire a helical conformation upon membrane interaction, while SP-C is highly helical also in the absence of lipids.…”

Section: Protein-lipid Interactions In Surfactantsupporting

confidence: 74%

Molecular Structures and Interactions of Pulmonary Surfactant Components

Johansson

Curstedt

1997

European Journal of Biochemistry

272

217

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The dominating functional property of pulmonary surfactant is to reduce the surface tension at the alveolar aidliquid interface, and thereby prevent the lungs from collapsing at the end of expiration. In addition, the system exhibits host-defense properties. Insufficient amounts of pulmonary surfactant in premature infants causes respiratory distress syndrome, a serious threat which nowadays can be effectively treated by airway instillation of surfactant preparations. Surfactant is a mixture of many molecular species, mainly phospholipids and specific proteins, surfactant protein A (SP-A), SP-B, SP-C and SP-D. SP-A and SP-D are water-soluble and belong to the collectins, a family of large multimeric proteins which structurally exhibit collagenousAectin hybrid properties and functionally are Caz+-dependent carbohydrate binding proteins involved in innate host-defence functions. SP-A and SP-D also bind lipids and SP-A is involved in organization of alveolar surfactant phospholipids. SP-B belongs to another family of proteins, which includes also lipid-interacting polypeptides with antibacterial and lytic properties. SP-B is a 17.4-kDa homodimer and each subunit contains three intrachain disulphides and has been proposed to contain four amphipathic helices oriented pairwise in an antiparallel fashion. SP-A, SP-B and SP-D all have been detected also in the gastrointestinal tract. SP-C, in contrast, appears to be a unique protein with extreme structural and stability properties and to exist exclusively in the lungs. SP-C is a lipopeptide containing covalently linked palmitoyl chains and is folded into a 3.7-nm a-helix with a central 2.3-nm all-aliphatic part, making it perfectly suited to interact in a transmembranous way with a fluid bilayer composed of dipalmitoylglycerophosphocholine, the main component of surfactant. Homozygous genetic deficiency of proSP-B causes lethal respiratory distress soon after birth and is associated with aberrant processing of the precursor of SP-C. This review focuses on the chemical composition, structures and interactions of the pulmonary surfactant, in particular the associated proteins.

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Section: Protein-lipid Interactions In Surfactantsupporting

confidence: 74%

Molecular Structures and Interactions of Pulmonary Surfactant Components

Johansson

Curstedt

1997

European Journal of Biochemistry

272

217

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“…Using this same approach, it has been shown that the 25 amino acid peptide corresponding to the amino terminus of the vesicular stomatitis virus envelope glycoprotein (G) causes haemolysis of sheep erythrocytes over a pH range similar to that observed for the virus on induction of cell~cell fusion, haemolytic activities and virus-cell fusion (Schlegel & Wade, 1984). There have been several reports on interactions with lipid of peptides corresponding to the amino-terminal sequence of human immunodeficiency virus (HIV) gp41 emphasizing its importance during the initial infective steps (Martin et al, 1991(Martin et al, , 1993.…”

Section: Introductionmentioning

confidence: 99%

Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein

Rodrı́guez-Crespo

Núñez

Gómez-Gutiérrez

et al. 1995

Journal of General Virology

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One of the first steps in the infective cycle of an enveloped virus consists of the fusion of the viral and cellular membranes. This process is usually achieved as a result of membrane destabilization brought about by a viral fusion peptide located at the amino terminus of one of the viral envelope glycoproteins. Previous sequence similarity studies by Rodrlguez-Crespo et al. (Journal of General Virology 75, 637-639, 1994) have shown that a hydrophobic stretch in the amino-terminal sequence of the S protein of hepatitis B virus shares several characteristics with fusion peptides of retroviruses and paramyxoviruses. A 16 residue peptide with this sequence was synthesized and its interaction with liposomes characterized. This peptide was able to mediate vesicle aggregation, lipid mixing and liposome leakage in a pH dependent manner at concentrations ranging from 3"5 to 52.0 pM. These effects were specific for negatively charged phospholipid vesicles. The peptide was also able to haemolyse erythrocytes. This study supports the notion that the sequence might be important in the initial infective steps of this virus, interacting with the target membranes and bringing about their subsequent destabilization.

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“…This method is based on an analysis of the shape and position of hydrophobic clusters in a given protein sequence (13). The 25 to 35 fragment (AIGLAWIPYFG) shows a hydrophobicity profile similar to that of the SIV tilted peptide, well known for its fusogenic properties (22,26), although, as shown on Fig. 1, the two stretches have no sequence identity.…”

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confidence: 99%

Distribution of Hydrophobic Residues Is Crucial for the Fusogenic Properties of the Ebola Virus GP2 Fusion Peptide

Adam

Lins

Stroobant

et al. 2004

J Virol

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The lipid-destabilizing properties of the N-terminal domain of the GP2 of Ebola virus were investigated. Our results suggest that the domain of Ebola virus needed for fusion is shorter than that previously reported. The fusogenic properties of this domain are related to its oblique orientation at the lipid/water interface owing to an asymmetric distribution of the hydrophobic residues when helical.The Ebola virus, known for its deadly outbreaks, causes hemorrhagic fevers in humans, yet there is still no effective vaccine or antiviral treatment available.The virion consists of a central ribonucleoprotein core linked by two matrix proteins to a glycoprotein (GP) carrying a lipid bilayer derived from the host cell.The GPs form trimeric spikes on the virion surface and are responsible for receptor binding and fusion of the virus to the host membrane. The GP is cleaved into two parts: GP1 and GP2. The GP2 seems to fold spontaneously into a trimeric, highly ␣-helical, rod-shaped structure, similar to HA2 in influenza virus and to gp41 in human immunodeficiency virus (25). Glycoprotein 2 (GP2) contains a fusion peptide at its N-terminal implicated in virus cell entry. It has previously been demonstrated that the Ebola virus fusion peptide predicted by Gallaher (14), from residues 23 to 38, induces fusion with liposomes and that mutations in this peptide inhibit Ebola virus infectivity (19,32).We have shown that the fusion peptides of simian immunodeficiency virus (SIV) and bovine leukemia virus have an asymmetric distribution of their hydrophobicity residues, the net hydrophobicity increasing from one end of the helix to the other (18,35). This particular distribution is characteristic of the so-called tilted peptides (3,4,5). Recently the orientation of the SIV tilted peptide was determined in planar lipid bilayers by neutron lamellar diffraction. The peptide was shown to form an angle of 55°with the membrane surface when helical, confirming our computational predictions (2). We have previously suggested that the Ebola virus fusion peptide also has such a distribution of hydrophobic residues (34).The present study examines the fusogenic properties of the Ebola virus fusion peptide 25 to 35 in relation to the hydrophobicity gradient by combining modeling and biophysical approaches.We have analyzed the Ebola virus fusion peptide sequence with respect to its hydrophobicity with the hydrophobic cluster analysis. This method is based on an analysis of the shape and position of hydrophobic clusters in a given protein sequence (13). The 25 to 35 fragment (AIGLAWIPYFG) shows a hydrophobicity profile similar to that of the SIV tilted peptide, well known for its fusogenic properties (22, 26), although, as shown on Fig. 1, the two stretches have no sequence identity.The three-dimensional structure of the 25 to 35 Ebola virus peptide was calculated as previously described, assuming a helical secondary structure (3,6,7,28). Small peptides can adopt ␣ and ␤ type structures (12,22,33). It was shown that the ability of the Ebola viru...

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Fusogenic activity of SIV (Simian Immunodeficiency Virus) peptides located in the GP32 NH2 terminal domain

Cited by 87 publications

References 16 publications

Molecular Structures and Interactions of Pulmonary Surfactant Components

Molecular Structures and Interactions of Pulmonary Surfactant Components

Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein

Distribution of Hydrophobic Residues Is Crucial for the Fusogenic Properties of the Ebola Virus GP2 Fusion Peptide

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