Structure of a novel glycopeptidolipid antigen containing a O-methylated serine isolated from Mycobacterium xenopi. Complete 1H-NMR and 13C-NMR assignment.

GPL X-1, a novel glycopeptidolipid (GPL) isolated from Mycobacterium xenopi (CIPT 140 35004), has recently been found to typify a new class of mycobacterial glycopeptidolipids devoid of C-mycoside core structure, the so-called serine-containing glycopeptidolipid [Rivière, M. & Puzo, G. (1991) J.

[Use of the immunoblotting method in serodiagnosis of M. kansasii mycobacteriosis].

The indirect enzyme test ELISA with soluble complex antigen of M. kansasii, used for assessment of the titre of IgG serum antibodies in a group of patients suffering from mycobacteriosis M. kansasii and in a control group of patients suffering from tuberculosis did not reveal statistically significant differences between serological responses of these two groups.

Preparation and properties of monoclonal antibodies against Mycobacterium tuberculosis.

The above mentioned monoclonal antibodies of idiotype IgG 3/Kappa against TMC 120 and TMC 107 strains of M. tuberculosis were prepared by fusion of mouse myeloma line FO cells with splenocytes BALB/c of mice immunized with complex antigens. These were prepared from the bacterial mass previously inactivated with gamma-rays radiation, and applied without mycobacterial adjuvant agent.

Screening of serum antibodies against Mycobacterium tuberculosis by enzyme-linked immunosorbent assay (ELISA) in healthy population.

Serum samples of venous blood of healthy individuals, chosen at random from two areas of the People's Democratic republic of Yemen, were examined for the presence of IgG antibodies against mycobacterial antigen by ELISA. From the district of Aden, the capital (A), there were 214 samples (72% vaccinated by BCG, 108 men and 106 women), other 235 ones originated from mountain area Laudar Muhairas (H) (66% vaccinated, 115 men and 120 women). The overall average of acquired titres was 1:81.

Characterization of a monoclonal antibody to Mycobacterium kansasii.

The characterization of an IgG2/Kappa monoclonal antibody against a protein antigen obtained by gel chromatography of the complex sonicate of M. kansasii biomass is described. It recognized specifically epitope molecules in complex and fractionated M.