PubMed Health⌕ Search

Biomedical subjects

J Gabay

Publications and source records attributed to J Gabay.

10 recordsLinked to original sources
PubMed1992

Treatment of patients with chronic granulomatous disease with recombinant human interferon-gamma does not improve neutrophil oxidative metabolism, cytochrome b558 content or levels of four anti-microbial proteins.

Recombinant interferon-gamma (rIFN-gamma) has been described to enhance phagocyte functions in vitro and in vivo in several patients with chronic granulomatous disease (CGD). To demonstrate the clinical usefulness of this treatment, 128 patients were treated in a randomized, double-blind multi-centre study with a placebo preparation or with rIFN-gamma. We analysed parameters of neutrophil oxidative and non-oxidative metabolism in 16 patients enrolled in this study. No enhanced superoxide-release was observed in patients treated with rIFN-gamma compared to placebo-treated patients. Phagocyte cytochrome b558 content also remained unchanged. Levels of four non-oxidative antimicrobial proteins (cathepsin G, azurocidine, p29b, lactoferrin) rose, fell, or remained unchanged, irrespective of treatment with rIFN-gamma or placebo.

Blood Proteins↗
PubMed1988

Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein.

A 14-kD protein was purified from human PMNs and its NH2-terminal sequence was determined. Comparison of a portion of the NH2-terminal sequence of this protein to the recently reported NH2-terminal sequence of eosinophil major basic protein (MBP) showed them to be identical. To aid further characterization of the structural and functional properties of this molecule, we isolated from an HL-60 cDNA library a single class of cDNA clones whose sequence matched exactly the NH2-terminal amino acid sequence of the 14-kD polypeptide. Northern analysis of HL-60 cells suggests that MBP is constitutively expressed in HL-60 cells and is highly transcribed from a single copy gene. The sequence of the full-length cDNA clones predicts that MBP is synthesized as a 23-kD precursor form (pro-MBP) which is subsequently cleaved to release the mature 14-kD MBP. The putative pro-MBP has a predicted pI of 6.0, but both the charged and the hydrophobic residues are asymmetrically distributed, creating a bipolar molecule. The NH2-terminal half has a predicted pI of 3.7 and is hydrophilic, while the COOH-terminal half (corresponding to mature MBP) has a predicted pI of 11.1 and is hydrophobic.

Base Sequence↗
PubMed1983

Genetic mapping of antigenic determinants on a membrane protein.

The antigenic determinants recognized by two monoclonal antibodies were mapped on LamB, an outer membrane protein of Escherichia coli. The procedure consisted of performing immunoprecipitation experiments with extracts of strains which produced truncated fragments of LamB, either in a free form (deletion and nonsense mutants) or fused to another polypeptide (malK-lamB and lamB-lacZ fusion strains). The conclusion is that the two antigenic determinants are located within 70 residues from the COOH-terminal end of LamB, which contains a total of 421 amino acids. Since these two antigenic sites were previously demonstrated to be exposed at the cell surface, it follows that a COOH-terminal portion of LamB must be located on the outer surface of the outer membrane.

ATP-Binding Cassette Transporters↗
PubMed1983

Evidence for a coupling of synthesis and export of an outer membrane protein in Escherichia coli.

We describe a lesion, lamB701-708, affecting the hydrophilic portion of the lambda receptor signal sequence. The C to A transversion of the sixth codon of the signal sequence changes a positively charged arginine to a neutral serine. The phenotype conferred by this alteration is unique among previously described signal sequence mutations. The results suggest an essential role for the charged amino acids of the hydrophilic segment in the initial interaction between a nascent secreted protein and a membrane export site. The results further suggest that synthesis of lambda receptor is coupled to its export.

Artificial Gene Fusion↗
PubMed1982

Monoclonal antibody as a probe for structure and function of an Escherichia coli outer membrane protein.

Eight independently derived monoclonal antibodies directed against the LamB protein were produced and characterized. By using these antibodies as probes, we identified four distinct topological and functional regions in the LamB molecule. Four monoclonal antibodies recognize antigenic determinants of the protein exposed on the outer side of the membrane. Two of these have their binding sites located in a region involved in maltose transport. One monoclonal antibody presumably binds to a determinant which is normally hidden in the membrane and three monoclonal antibodies recognize determinants facing the periplasmic space.

Animals↗
PubMed1982

Monoclonal antibodies against the LamB protein.

Eight independently derived monoclonal antibodies directed against the LamB protein were produced and characterized. These antibodies allowed the identification of 4 distinct topological and functional regions in the LamB molecule. Four monoclonal antibodies recognize determinants present at the cell surface. Two of these have their binding sites located in a region involved in maltose transport. One monoclonal antibody presumably binds to a determinant which is normally hidden in the membrane, and three monoclonal antibodies recognize a region of the protein which is in close association with the peptidoglycan sacculus.

Antibodies, Monoclonal↗
PubMed1980

Interaction of the lamB protein with the peptidoglycan layer in Escherichia coli K12.

In Escherichia coli K12 the product of gene lamB is an outer membrane protein involved in the transport of maltose and maltodextrins and serving as a receptor for several bacteriophages including lambda. About 30 to 40% of this protein can be recovered associated to peptidoglycan when the cells are dissolved in sodium dodecyl sulfate in the presence of 2 mM Mg2+ ions. The bound protein can then be quantitatively eluted from peptidoglycan by incubating the complex in Triton X-100 and EDTA, or sodium dodecyl sulfate and NaCl. The protein eluted in such ways is still totally active in its phage-neutralizing activity. Two other membrane proteins known to behave similarly to the lamB protein are proteins Ia and Ib. However the binding of these proteins to peptidoglycan appears tighter, in several respects, than that of the lamB protein. The lamB protein may span the outer membrane since it appears to interact with the peptidoglycan on the inner side of this membrane while it is known to be accessible to both phages and antibodies at the cell surface.

Bacterial Outer Membrane Proteins↗
PubMed1976

[Study of a specific polyoside and a group antigen extracted from Leptospira biflexa patoc, patoc I strain].

We extracted from L. biflexa patoc a fraction F, reacting in hemagglutination and ring tests with sera prepared against more than ten different serogroups. This fraction contains mainly a polysaccharide (65 per cent), the role of which was clearly demonstrated in the precipitation reaction with homologous antisera, through periodic oxidation; it also contains lipids (20 per cent) and proteins (10 per cent). We isolated from this fraction F, by Biogel column chromatography, 2 distinct antigens, one, F2, carrying the patoc-type specificity, the other, F 1B, a group specificity shared by many leptospira. These antigens differ not only immunogically, but also in their chemical composition. The type-specific antigen F2 contains mainly a polysaccharide composed of arabinose and glucosamine (possibly an immunodominant sugar). As for the group-specific fraction F 1B, its composition is more complex since lipids and proteins are also found with the polysaccharide. This antigen could therefore be a lipoglycoprotein.

Animals↗