The goal of this project was to find and collect high concentrations of endotoxin-specific antibodies for therapeutic IgG- or IgM-enriched preparations. Various enzyme-linked immunosorbent assays (ELISAs) were developed to perform longitudinal studies of the serological response to a large panel of smooth and rough purified lipopolysaccharide (LPS) extracts in a population of healthy blood donors. To accomplish this, 1612 human serum samples from volunteer blood donors collected by seven different blood banks in Belgium were screened and specific IgM and IgG activities were measured.
View Article and Find Full Text PDFObjective: This study follows the sequential changes in anti-lipopolysaccharide antibodies in infected patients with and without septic shock.
Summary Background Data: A relation between high endogenous levels of anti-LPS antibodies and protection against bacteremia and septic shock in at-risk patient groups has been observed. However, information on the daily follow-up and kinetics of apparition or disappearance of anti-LPS antibody activities and their relations with the protective properties of the different immunoglobulin classes has not been clearly investigated.
Mice were passively immunized with sera from blood donors active for rough lipopolysaccharides (LPS), the J5 (Rc chemotype) mutant of Escherichia coli O111:B4, and the Re595 (Re chemotype) mutant of Salmonella minnesota. All protected the mice against lethal challenge with smooth E. coli WF96 LPS, E.
View Article and Find Full Text PDFComparison of both mesophilic (35 degrees C) and thermophilic (55 degrees C) anaerobic digestions of the organic fraction of municipal refuses in pilot digesters designed to process in a semisolid phase at total solids concentrations of ca. 25% shows that the average gas production is 20-25% higher in thermophilic conditions than in mesophilic conditions even for a retention time of 10 days. These results and the data recorded during long periods of experimentation indicate that the process allows to increase the net energy production and to improve the economical balance of an industrial plant.
View Article and Find Full Text PDFAn enzyme-linked immunosorbent assay using monoclonal antibodies was developed to study the subclass distribution of immunoglobulin G (IgG) to cytomegalovirus (CMV) in individuals from a number of clinical groups. Most CMV-seropositive individuals had IgG1 and IgG3. IgG2 and IgG4 were detected less frequently at very low levels of activity, mostly among mothers at delivery and renal patients.
View Article and Find Full Text PDFAn enzyme-linked immunosorbent assay was developed to study the subclass distribution of immunoglobulin G (IgG) specific to the core glycolipid (CGL) of the Re mutant of Salmonella minnesota R595 in serum samples from individuals with an IgG response toward these antigens. In a group of healthy blood donors, we detected predominantly the IgG2 and IgG1 subclasses. In a group of patients in an intensive care unit who developed infectious complications due to gram-negative bacteria, the anti-CGL IgG activity was due mainly to the IgG2 and IgG3 subclasses.
View Article and Find Full Text PDFWe have developed an ELISA for IgM and IgG antibodies to the core glycolipid (CGL) of the Re mutant Salmonella minnesota R 595, and to lipid A. Anti-CGL antibodies have been detected in sera from 37% of healthy blood donors, whereas anti-lipid A activities were found in 13% of individuals only. The anti-CGL and anti-lipid A activities were examined in patients in a surgical intensive care unit, selected on the basis of a definite risk of infectious complications due to Gram-negative bacteria.
View Article and Find Full Text PDFVarious data obtained with activable hydrophobic probes, proteolytic treatments and anti M-protein polyclonal antibodies strongly suggest that M-protein of influenza A is an integral part of the lipid bilayer of native virions and somehow spans at the surface of the virions. Therefore we have looked for the presence of M-protein epitopes on the surface of influenza A virion by using four type A M-protein monoclonal antibodies. We developed a specific and sensitive competition ELISA where intact virions, dodecyl-sulfate disrupted virions and spikeless particles obtained after proteolytic treatment with caseinase C were used to test their ability to inhibit the reaction between these monoclonal antibodies and pure M-protein.
View Article and Find Full Text PDFDirect enzyme-linked immunosorbent assay methods offer several advantages in assessing past or recent exposure to cytomegalovirus (CMV) infection, but there persist many pitfalls in the use of these methods for determining specific immunoglobulin M (IgM). The efficiency of absorption of sera by IgG-coated latex beads, aggregated human IgG, or Staphylococcus aureus, i.e.
View Article and Find Full Text PDFAnti M-protein antibody response has been looked for in sera from individuals with serological evidence of A or B influenza infection using pure M-protein (M) in complement fixation tests (CF), in IgG and in IgA specific enzyme linked immunosorbent assays (ELISA). Mp ELISA (IgG specific) antibodies are not restricted to people with history of recent respiratory infection. Individuals under 15 years are less prone than those older to display M ELISA activity.
View Article and Find Full Text PDFArch Int Physiol Biochim
December 1979
Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated concentrated suspensions of these virions and fixed complement in their presence. Antibodies to M-protein were readily absorbed by intact virions or by spikeless particles obtained after proteolytic treatment, giving clear evidence that M-protein is exposed at the surface of the virus envelope.
View Article and Find Full Text PDFComp Biochem Physiol B
September 1989
1. The amino acid sequence of the major parvalbumin of the Whiting has been determined; the polypeptide chain is made of 108 residues, the terminal amino acid group is acetylated, there is no disulfide bridges, the structure of the two calcium binding sites is preserved and the distribution along the polypeptide chain of the hydrophobic residues implicated in the compact hydrophobic core of the protein is also maintained. 2.
View Article and Find Full Text PDFArch Int Physiol Biochim
October 1971