Identification of an Onchocerca volvulus cDNA encoding a low-molecular-weight antigen uniquely recognized by onchocerciasis patient sera

Lobos, Edgar; Altmann, Michael; Mengod, Guadalupe; Weiss, N.; Rudin, W.; Karam, M

doi:10.1016/0166-6851(90)90016-f

Cited by 67 publications

(39 citation statements)

References 22 publications

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“…PEBP homologues have been identified in other mammals including rat (26), mouse (27), and monkey (28). Other members of the PEBP family include the putative odorant-binding protein in Drosophila (29), the putative PEBP of the malaria parasite Plasmodium falciparum (30), and the Ov-16 antigen of Onchocera volvulus (31) and the toxocara excretory-secretory antigen 26 of Toxocara canis (32), two parasitic nematodes. A dosage-dependent suppressor of CDC25 mutations in Saccharomyces cerevisiae, TFS1 (33), and several proteins in flowering plants (Arabidopsis thaliana (Refs.…”

Section: Discussionmentioning

confidence: 99%

The Phosphatidylethanolamine-binding Protein Is the Prototype of a Novel Family of Serine Protease Inhibitors

Hengst

Albrecht

Heß

et al. 2001

Journal of Biological Chemistry

172

145

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Serine proteases are involved in many processes in the nervous system and specific inhibitors tightly control their proteolytic activity. Thrombin is thought to play a role in tissue development and homeostasis. To date, protease nexin-1 is the only known endogenous protease inhibitor that specifically interferes with thrombotic activity and is expressed in the brain. In this study, we report the detection of a novel thrombin inhibitory activity in the brain of protease nexin-1 (؊/؊) mice. Purification and subsequent analysis by tandem mass spectrometry identified this protein as the phosphatidylethanolamine-binding protein (PEBP). We demonstrate that PEBP exerts inhibitory activity against several serine proteases including thrombin, neuropsin, and chymotrypsin, whereas trypsin, tissue type plasminogen activator, and elastase are not affected. Since PEBP does not share significant homology with other serine protease inhibitors, our results define it as the prototype of a novel class of serine protease inhibitors. PEBP immunoreactivity is found on the surface of Rat-1 fibroblast cells and although its sequence contains no secretion signal, PEBP-H 6 can be purified from the conditioned medium upon recombinant expression.

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Section: Discussionmentioning

confidence: 99%

The Phosphatidylethanolamine-binding Protein Is the Prototype of a Novel Family of Serine Protease Inhibitors

Hengst

Albrecht

Heß

et al. 2001

Journal of Biological Chemistry

172

145

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“…Ag16 was localized in the hypodermis, the cuticle and the uterine epithelium of the filarial parasite 0. voZvuZus. It seems to be presented to the host immune system through excretory-secretory mechanisms; however, its biological function is unknown [23]. TFS 1 was identified as a dosage-dependent suppressor of CDC25 mutations.…”

Section: -Kda Protein Affinity Towards Nucleotides and Small Gtp-bimentioning

confidence: 99%

“…5). Recently, Schoentgen et al [17], showed a significant similarity between the three mammalian 21-kDa proteins, TFSl from S. cerevisiae [22] and an antigen (Ag16) from Onchocerca volvulus [23]. More particularly, residues 60-126 of the 21-kDa proteins presented 79% sequence identity with residues 91-155 of Ag16 and 55% sequence identity with residues 88-120 and 139-170 of yeast TFS1, the sequence similarity being raised to 98% and 72%, respectively, when conserved amino acids are taken into account (Fig.…”

Section: -Kda Protein Affinity Towards Nucleotides and Small Gtp-bimentioning

confidence: 99%

Relationships Between Molecular Interactions (Nucleotides, Lipids and Proteins) and Structural Features of the Bovine Brain 21‐kDa Protein

Bucquoy

Jollès

Schoentgen

1994

European Journal of Biochemistry

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A cytosolic 21-kDa protein isolated from bovine brain was demonstrated to bind hydrophobic ligands, particularly phosphatidylethanolamine. It was encountered in several tissues and species ; however, its accurate function remained partially unknown. In order to obtain information from its structural features, we built a molecular model which revealed it to possess a nucleotide-binding site. In the present research, we describe the affinity of the bovine brain 21-kDa protein for nucleotides, and its association with cytosolic proteins, small GTP-binding proteins and lipid droplets. Our results suggest that, through its association with small GTP-binding proteins, the 21 -kDa protein is implicated in signal mechanisms during cell growth and maturation.From bovine brain, Bernier and Jolli% purified, in 1984, a soluble basic 23-kDa protein which showed a significant affinity for organic anions [l]. The protein was further characterized as a phosphatidylethanolamine-binding protein, suggesting its involvement in lipid metabolism [2]. The determination of its complete amino acid sequence 131 revealed the correct molecular mass to be 21-kDa. The comparison of the primary structure of the 21-kDa protein with sequence protein data banks showed very few significant sequence similarities; it was concluded that, from a structural point of view, the 21-kDa protein might represent a new type of protein [3]. Immunochemical studies using a rabbit antiserum demonstrated the presence of the 21-kDa protein in the entire cytoplasm, along the plasma membrane and the membranes of rough endoplasmic reticulum in rat brain oligodendrocytes Independent of these experiments, Bollengier and Mahler purified, in 1980, a cytosolic protein from human brain, identified as h3 [5]. In SDSPAGE, the human h3 behaved as a protein of molecular mass approximately 23 kDa. Further physicochemical studies showed that the human brain protein h3 possessed two free sulphydryl groups responsible for doublet (21 kDa and 23 kDa) and polymer formation by disulphide bonding [6]. Immunoblotting revealed the presence of protein h3 in different tissues from human, bovine, rat and chicken species 171. Recently, the human protein h3 primary structure was established both by deduction from the corresponding cDNA sequence and by direct microsequencing of the purified protein [8]; it was shown to be constituted by 186 amino acids corresponding to a calculated molecular mass of 21 kDa and present 95% sequence identity with the bovine 21-kDa protein. Furthermore, by morphine affinity chromatography, Grandy et al. 191 isolated a 23-kDa protein from rat brain membranes; although not an opioid receptor itself, the rat brain 23-kDa protein may be associated with such a receptor. The authors screened a rat brain cDNA library and established the sequence of a cDNA coding for the 23-kDa rat brain protein. The deduced 23-kDa protein shared 85% identity with the bovine 21-kDa protein and 85.5% identity with the human protein h3, revealing that the three mammalian proteins are mem...

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“…l). The Agl6 was localized in the hypodermis, the cuticle and the uterine epithelium of the parasite; however, its biological function remains unknown [24]. Between the yeast TFS1 gene product and the bovine brain 21-23 kDa protein 29% of the amino acids are identical and the similarity increased to 53% when conservative changes were included [27].…”

Section: ~V----gt--~izv~sdy~s~t~lmentioning

confidence: 99%

From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site

Schoentgen

Jollès

1995

FEBS Letters

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Identification of an Onchocerca volvulus cDNA encoding a low-molecular-weight antigen uniquely recognized by onchocerciasis patient sera

Cited by 67 publications

References 22 publications

The Phosphatidylethanolamine-binding Protein Is the Prototype of a Novel Family of Serine Protease Inhibitors

The Phosphatidylethanolamine-binding Protein Is the Prototype of a Novel Family of Serine Protease Inhibitors

Relationships Between Molecular Interactions (Nucleotides, Lipids and Proteins) and Structural Features of the Bovine Brain 21‐kDa Protein

From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site

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