Bioinformatics of the TULIP domain superfamily

Proteins of the BPI (bactericidal/permeability-increasing protein)-like family contain either one or two tandem copies of a fold that usually provides a tubular cavity for the binding of lipids. Bioinformatic analyses show that, in addition to its known members, which include BPI, LBP [LPS (lipopolysaccharide)-binding protein)], CETP (cholesteryl ester-transfer protein), PLTP (phospholipid-transfer protein) and PLUNC (palate, lung and nasal epithelium clone) protein, this family also includes other, more divergent groups containing hypothetical proteins from fungi, nematodes and deep-branching unicellular eukaryotes. More distantly, BPI-like proteins are related to a family of arthropod proteins that includes hormone-binding proteins (Takeout-like; previously described to adopt a BPI-like fold), allergens and several groups of uncharacterized proteins. At even greater evolutionary distance, BPI-like proteins are homologous with the SMP (synaptotagmin-like, mitochondrial and lipid-binding protein) domains, which are found in proteins associated with eukaryotic membrane processes. In particular, SMP domain-containing proteins of yeast form the ERMES [ER (endoplasmic reticulum)-mitochondria encounter structure], required for efficient phospholipid exchange between these organelles. This suggests that SMP domains themselves bind lipids and mediate their exchange between heterologous membranes. The most distant group of homologues we detected consists of uncharacterized animal proteins annotated as TM (transmembrane) 24. We propose to group these families together into one superfamily that we term as the TULIP (tubular lipid-binding) domain superfamily.

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Similar Organization of the Lipopolysaccharide-Binding Protein (LBP) and Phospholipid Transfer Protein (PLTP) Genes Suggests a Common Gene Family of Lipid-Binding Proteins

Genomics ◽

10.1006/geno.1997.5030 ◽

1997 ◽

Vol 46 (3) ◽

pp. 416-425 ◽

Cited By ~ 51

Author(s):

Carsten J. Kirschning ◽

Janice Au-Young ◽

Norbert Lamping ◽

Dirk Reuter ◽

Dagmar Pfeil ◽

...

Keyword(s):

Gene Family ◽

Binding Proteins ◽

Lipid Binding ◽

Phospholipid Transfer Protein ◽

Lipopolysaccharide Binding Protein ◽

Transfer Protein ◽

Phospholipid Transfer ◽

Lipid Binding Proteins ◽

Similar Organization ◽

Lipopolysaccharide Binding

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The roles of the human lipid-binding proteins ORP9S and ORP10S in vesicular transport

Biochemistry and Cell Biology ◽

10.1139/o05-064 ◽

2005 ◽

Vol 83 (5) ◽

pp. 631-636 ◽

Cited By ~ 17

Author(s):

Gregory D Fairn ◽

Christopher R McMaster

Keyword(s):

Binding Protein ◽

Vesicular Transport ◽

Lipid Binding ◽

Yeast Cells ◽

Phospholipid Transfer Protein ◽

Related Protein ◽

Oxysterol Binding Protein ◽

Transfer Protein ◽

Phospholipid Transfer ◽

Lipid Binding Proteins

Inactivation of the yeast oxysterol binding protein related protein (ORP) family member Kes1p allows yeast cells to survive in the absence of Sec14p, a phospholipid transfer protein required for cell viability because of the role it plays in transporting vesicles from the Golgi. We expressed human ORP9S and ORP10S in yeast lacking Sec14p and Kes1p function, and found that ORP9S completely complemented Kes1p function, whereas ORP10S possessed only a weak ability to replace Kes1p function. Purified ORP9S protein bound several phosphoinositides, whereas ORP10 bound specifically to phosphatidylinositol 3-phosphate. The combined evidence demonstrates that only a subset of human ORP proteins can function as negative regulators of Golgi-derived vesicular transport.Key words: phospholipid, Saccharomyces cerevisiae, Golgi, vesicular transport, oxysterol binding protein related protein.

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Lipopolysaccharide Is Transferred from High-Density to Low-Density Lipoproteins by Lipopolysaccharide-Binding Protein and Phospholipid Transfer Protein

Infection and Immunity ◽

10.1128/iai.73.4.2321-2326.2005 ◽

2005 ◽

Vol 73 (4) ◽

pp. 2321-2326 ◽

Cited By ~ 74

Author(s):

J. H. M. Levels ◽

J. A. Marquart ◽

P. R. Abraham ◽

A. E. van den Ende ◽

H. O. F. Molhuizen ◽

...

Keyword(s):

Acute Phase ◽

Binding Protein ◽

Low Density Lipoproteins ◽

High Density ◽

Phospholipid Transfer Protein ◽

Low Density ◽

Lipoprotein Subclasses ◽

Transfer Protein ◽

Phospholipid Transfer ◽

Dose Dependent

ABSTRACT Lipopolysaccharide (LPS), the major outer membrane component of gram-negative bacteria, is a potent endotoxin that triggers cytokine-mediated systemic inflammatory responses in the host. Plasma lipoproteins are capable of LPS sequestration, thereby attenuating the host response to infection, but ensuing dyslipidemia severely compromises this host defense mechanism. We have recently reported that Escherichia coli J5 and Re595 LPS chemotypes that contain relatively short O-antigen polysaccharide side chains are efficiently redistributed from high-density lipoproteins (HDL) to other lipoprotein subclasses in normal human whole blood (ex vivo). In this study, we examined the role of the acute-phase proteins LPS-binding protein (LBP) and phospholipid transfer protein (PLTP) in this process. By the use of isolated HDL containing fluorescent J5 LPS, the redistribution of endotoxin among the major lipoprotein subclasses in a model system was determined by gel permeation chromatography. The kinetics of LPS and lipid particle interactions were determined by using Biacore analysis. LBP and PLTP were found to transfer LPS from HDL predominantly to low-density lipoproteins (LDL), in a time- and dose-dependent manner, to induce remodeling of HDL into two subpopulations as a consequence of the LPS transfer and to enhance the steady-state association of LDL with HDL in a dose-dependent fashion. The presence of LPS on HDL further enhanced LBP-dependent interactions of LDL with HDL and increased the stability of the HDL-LDL complexes. We postulate that HDL remodeling induced by LBP- and PLTP-mediated LPS transfer may contribute to the plasma lipoprotein dyslipidemia characteristic of the acute-phase response to infection.

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Lipopolysaccharide-Binding Protein and Phospholipid Transfer Protein Release Lipopolysaccharides from Gram-Negative Bacterial Membranes

Infection and Immunity ◽

10.1128/iai.68.5.2410-2417.2000 ◽

2000 ◽

Vol 68 (5) ◽

pp. 2410-2417 ◽

Cited By ~ 98

Author(s):

C. J. Vesy ◽

R. L. Kitchens ◽

G. Wolfbauer ◽

J. J. Albers ◽

R. S. Munford

Keyword(s):

Human Serum ◽

Binding Protein ◽

Normal Human Serum ◽

High Density Lipoproteins ◽

Phospholipid Transfer Protein ◽

Gram Negative ◽

Bacterial Membranes ◽

Transfer Protein ◽

Phospholipid Transfer ◽

Normal Human

ABSTRACT Although animals mobilize their innate defenses against gram-negative bacteria when they sense the lipid A moiety of bacterial lipopolysaccharide (LPS), excessive responses to this conserved bacterial molecule can be harmful. Of the known ways for decreasing the stimulatory potency of LPS in blood, the binding and neutralization of LPS by plasma lipoproteins is most prominent. The mechanisms by which host lipoproteins take up the native LPS that is found in bacterial membranes are poorly understood, however, since almost all studies of host-LPS interactions have used purified LPS aggregates. Using nativeSalmonella enterica serovar Typhimurium outer membrane fragments (blebs) that contained 3H-labeled lipopolysaccharide (LPS) and 35S-labeled protein, we found that two human plasma proteins, LPS-binding protein (LBP) and phospholipid transfer protein (PLTP), can extract [3H]LPS from bacterial membranes and transfer it to human high-density lipoproteins (HDL). Soluble CD14 (sCD14) did not release LPS from blebs yet could facilitate LBP-mediated LPS transfer to HDL. LBP, but not PLTP, also promoted the activation of human monocytes by bleb-derived LPS. Whereas depleting or neutralizing LBP significantly reduced LPS transfer from blebs to lipoproteins in normal human serum, neutralizing serum PLTP had no demonstrable effect. Of the known lipid transfer proteins, LBP is thus most able to transfer LPS from bacterial membranes to the lipoproteins in normal human serum.

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Purification and properties of a phospholipid transfer protein from Rhodopseudomonas sphaeroides.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(20)71336-0 ◽

1984 ◽

Vol 259 (19) ◽

pp. 12178-12183

Author(s):

S P Tai ◽

S Kaplan

Keyword(s):

Phospholipid Transfer Protein ◽

Rhodopseudomonas Sphaeroides ◽

Transfer Protein ◽

Purification And Properties ◽

Phospholipid Transfer

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Molecular cloning of cDNA for lipopolysaccharide-binding protein from the hemolymph of the American cockroach, Periplaneta americana. Similarity of the protein with animal lectins and its acute phase expression

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)98841-1 ◽

1991 ◽

Vol 266 (20) ◽

pp. 13318-13323

Author(s):

T. Jomori ◽

S. Natori

Keyword(s):

Molecular Cloning ◽

Acute Phase ◽

Periplaneta Americana ◽

Binding Protein ◽

American Cockroach ◽

Lipopolysaccharide Binding Protein ◽

Lipopolysaccharide Binding

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Higher Lipopolysaccharide Binding Protein and Chemerin Concentrations Were Associated with Metabolic Syndrome Features in Pediatric Subjects with Abdominal Obesity during a Lifestyle Intervention

Nutrients ◽

10.3390/nu13020289 ◽

2021 ◽

Vol 13 (2) ◽

pp. 289

Author(s):

Amelia Marti ◽

Isabel Martínez ◽

Ana Ojeda-Rodríguez ◽

María Cristina Azcona-Sanjulian

Keyword(s):

Metabolic Syndrome ◽

Children And Adolescents ◽

Lifestyle Intervention ◽

Abdominal Obesity ◽

Plasma Levels ◽

Intervention Program ◽

Binding Protein ◽

Controlled Trial ◽

Lipopolysaccharide Binding Protein ◽

Lipopolysaccharide Binding

Background: Elevated circulating plasma levels of both lipopolysaccharide-binding protein (LBP) and chemerin are reported in patients with obesity, but few studies are available on lifestyle intervention programs. We investigated the association of both LBP and chemerin plasma levels with metabolic syndrome (MetS) outcomes in a lifestyle intervention in children and adolescents with abdominal obesity Methods: Twenty-nine patients enrolled in a randomized controlled trial were selected. The lifestyle intervention with a 2-month intensive phase and a subsequent 10-month follow-up consisted of a moderate calorie-restricted diet, recommendations to increase physical activity levels, and nutritional education. Results: Weight loss was accompanied by a significant reduction in MetS prevalence (−43%; p = 0.009). Chemerin (p = 0.029) and LBP (p = 0.033) plasma levels were significantly reduced at 2 months and 12 months, respectively. At the end of intervention, MetS components were associated with both LBP (p = 0.017) and chemerin (p < 0.001) plasma levels. Conclusions: We describe for the first time a reduction in both LBP and chemerin plasma levels and its association with MetS risk factors after a lifestyle intervention program in children and adolescents with abdominal obesity. Therefore, LBP and chemerin plasma levels could be used as biomarkers for the progression of cardiovascular risk in pediatric populations.

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