Investigation of autoantibody profiles for cerebrospinal fluid biomarker discovery in patients with relapsing-remitting multiple sclerosis.

Using the UNIarray® marker technology platform, cerebrospinal fluid immunoglobulin G reactivities of 15 controls and 17 RRMS patients against human recombinant proteins were investigated. Patient cerebrospinal fluids were oligoclonal band positive and reactivities were compared to that of sex- and age-matched controls. We hereby aimed at the characterization of autoreactivity in patients with RRMS.

Optimization of antibody immobilization for on-line or off-line immunoaffinity chromatography.

The covalent immobilization of antibodies to solid supports for immunoaffinity (IA) purification is widely used in the biological sciences. However, relative immobilization yields, immobilization stability, and antigen-binding capacity vary significantly with the antibody and protocol used. A systematic study was conducted to determine the most versatile antibody immobilization method for use in on-line and off-line IA chromatography applications using commonly accessible immobilization methods.

A mouse model for ricin poisoning and for evaluating protective effects of antiricin antibodies.

Unlabelled: BACKGROUND. Ricin is a potential bioterrorism agent and no specific antidote or treatment exists for ricin poisoning. For this reason, we developed ricin-specific antibodies that were tested in a murine model of ricin poisoning for use as antidotes against symptoms of ricin poisoning.

Extraction and identification of electroimmunoprecipitated proteins from agarose gels.

A method for the identification of protein antigens captured in electroimmunoprecipitates was developed. Different antigen-antibody precipitates were generated by agarose gel immunoelectrophoresis. The immunoprecipitates were excised and various methods for extracting and dissociating the precipitates were systematically studied by analyzing for protein components of the extracts using peptide mass fingerprinting after sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Effect of different hapten-carrier conjugation ratios and molecular orientations on antibody affinity against a peptide antigen.

Hapten-carrier conjugate immunization is an important tool in the generation of hapten-specific antibodies for analytical purposes and in the uncovering of basic vaccine-immunological mechanisms. The affinity of antibodies is known to play an important role for the resulting sensitivity of antibody-based assay systems and in deciding whether a vaccine-induced antibody response will be protective. With ovalbumin as a carrier protein and a peptide (7.

[Botulinum and ricin toxins].

Due to their acute toxicity, accessibility and history of use, ricin and botulinum toxins are at the present time the most relevant bioterror toxins. We give a brief review of their toxicity and possible uses in bioterror attacks and describe two cases in Denmark in which immunochemical, PCR and mass spectrometric assays developed in-house were used to confirm a foodborne botulinum toxin E case and to identify bovine serum albumin as the powder enclosed in a letter sent to the U.S.

Rapid decay of Salmonella flagella antibodies during human gastroenteritis: a follow up study.

An indirect enzyme-linked immunosorbent assay (ELISA) based on Salmonella re-polymerized flagella was employed to measure levels of immunoglobulin (Ig) G, IgM and IgA antibodies in sera from 303 Danish patients diagnosed with either Salmonella enteritidis or Salmonella typhimurium. The antibody-levels were assessed at one, three and six months after onset of salmonellosis, and sera from a control-group of 170 healthy blood donors were additionally analysed in order to establish cut-off values for the analysis. Cross-reactions to other Salmonella serotypes, as well as to Escherichia coli, Yersinia enterocolitica, Campylobacter jejuni, Campylobacter coli and Helicobacter pylori were observed.

Comparison of native and recombinant chlorite dismutase from Ideonella dechloratans.

A detailed comparison between native chlorite dismutase from Ideonella dechloratans, and the recombinant version of the protein produced in Escherichia coli, suggests the presence of a covalent modification in the native enzyme. Although the native and recombinant N- and C-terminal sequences are identical, the enzymes display different electrophoretic mobilities, and produce different peptide maps upon digestion with trypsin and separation of fragments using capillary electrophoresis. Comparison of MALDI mass spectra of tryptic peptides from the native and recombinant enzymes suggests two locations for modification in the native protein.

Proteome analysis of the purine stimulon from Lactococcus lactis.

A comparative expression proteome analysis was carried out by analyzing differential expression patterns of pulse-labelled proteins on two-dimensional gels under standard conditions and during purine nucleotide starvation, followed by mass spectrometric identification of regulated proteins. Based upon the expression patterns, three stimulons could be identified in Lactococcus lactis subsp. cremoris.