Monospecific polyclonal anti-anti-idiotypic antibodies to the carboxyterminal undecapeptide of the SV40 large tumour antigen.

The murine monoclonal antibody PAb1605 defines an epitope, peptide Lys(698)-Thr(708) (KT), on the carboxyterminus of the tumour(T)antigen of SV40-transformed cells. In vivo and in vitro experiments had shown that this sequence represents an epitope for both humoral and cellular immune responses. When injected into rabbits PAb1605 induces anti-idiotypic antibodies (Ab-2).

Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene.

The superoxide dismutase (SOD) of Helicobacter pylori, a pathogenic bacterium which colonizes the gastric mucosa, evoking a marked inflammatory response, was purified and characterized, and the N-terminal amino acid sequence was determined. The enzyme consists of two identical subunits each with an apparent molecular weight of 24,000. Analysis of the primary structure and inhibition studies revealed that H.

Evaluation of an antigen-capture enzyme immunoassay for rapid diagnosis of Mycoplasma pneumoniae infection.

A new enzyme immunoassay (EIA; Enzygost) for rapid detection of Mycoplasma pneumoniae antigen was evaluated in 51 young adults with acute respiratory infection. The EIA results using sputa and nasopharyngeal aspirates were compared with those of serological antibody tests, culture and a DNA probe. In sputum the sensitivity of the EIA ranged from 40% to 81% and the specificity from 64% to 100%, depending on the reference method.

In situ localization of the 60 k protein of Helicobacter pylori, which belongs to the family of heat shock proteins, by immuno-electron microscopy.

The groEl homologue of Helicobacter pylori was isolated and characterized by means of immunoelectron microscopy, after cryosectioning. The 60 k protein was isolated from Helicobacter pylori by treatment of the cells with 2-butanol and purified by anion exchange chromatography. The native molecular weight of the 60 k protein was estimated to be 420 k by size exclusion chromatography.

Serodiagnosis of Helicobacter pylori infections with an enzyme immunoassay using the chromatographically purified 120 kilodalton protein.

A membrane-associated 120 kDa protein of Helicobacter pylori with known species-specificity was isolated and used in an enzyme immunoassay (EIA) for the detection of Helicobacter pylori-specific IgG antibodies in patient sera. The EIA was compared with two other methods used for serodiagnosis of Helicobacter pylori infections: an EIA using sonicated whole Helicobacter pylori cell antigen and Western immunoblot. In a prospective study 127 unselected patients (76 patients with antrum gastritis, 51 patients without gastritis) who underwent gastroscopy were studied histologically and serologically.

Immunodominant epitopes of the adhesin of Mycoplasma pneumoniae.

Overlapping octapeptides from the amino acid sequence of the adherence protein of Mycoplasma pneumoniae were synthesized and used as the antigen in an enzyme-linked immunosorbent assay with serum samples from M. pneumoniae-infected patients. Of a sequence of 338 amino acids positioned between leucine 801 and leucine 1139, only two regions with immunodominant continuous epitopes were detected.

Topological mapping of the P1-adhesin of Mycoplasma pneumoniae with adherence-inhibiting monoclonal antibodies.

Five adherence-inhibiting monoclonal antibodies (mAbs) were used for topological mapping of the binding sites of the 169 kDa membrane-integrated adhesin of Mycoplasma pneumoniae. Antibody binding sites were characterized using overlapping synthetic octapeptides. Three regions of the protein seem to be involved in adherence: the N-terminal region [N-reg, epitopes beginning at amino acid (aa) 1 to aa 14 and aa 231 to aa 238, respectively]; a domain (D1) approximately in the middle of the molecule (beginning at aa 851 to aa 858 and aa 921 to aa 928); and a domain (D2) closer to the C-terminus (beginning at aa 1303 to aa 1310, aa 1391 to aa 1398 and aa 1407 to aa 1414).

Binding sites of attachment-inhibiting monoclonal antibodies and antibodies from patients on peptide fragments of the Mycoplasma pneumoniae adhesin.

The adherence protein (P1 protein) of Mycoplasma pneumoniae was purified by electroelution and cleaved with cyanogen bromide. The resulting peptides were separated by two-dimensional electrophoresis. Spots reacting in Western immunoblots with two attachment-inhibiting monoclonal antibodies were isolated, and the amino-terminal ends of these peptides were microsequenced.