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The "cell wall core" consisting of a mycolyl-arabinogalactan-peptidoglycan (mAGP) complex represents the hallmark of the mycobacterial cell envelope. It has been the focus of intense research at both structural and biosynthetic levels during the past few decades. Because it is essential, mAGP is also regarded as a target for several antitubercular drugs. Herein, we demonstrate that exposure of Mycobacterium bovis Bacille Calmette-Guérin or Mycobacterium marinum to thiacetazone, a second line antitubercular drug, is associated with a severe decrease in the level of a major apolar glycolipid. This inhibition requires MmaA4, a methyltransferase reported to participate in the activation process of thiacetazone. Following purification, this glycolipid was subjected to detailed structural analyses, combining gas-liquid chromatography, mass spectrometry, and nuclear magnetic resonance. This allowed to identify it as a 5-O-mycolyl-β-Araf-(1→2)-5-O-mycolyl-α-Araf-(1→1)-Gro, designated dimycolyl diarabinoglycerol (DMAG). The presence of DMAG was subsequently confirmed in other slow growing pathogenic species, including Mycobacterium tuberculosis. DMAG production was stimulated in the presence of exogenous glycerol. Interestingly, DMAG appears structurally identical to the terminal portion of the mycolylated arabinosyl motif of mAGP, and the metabolic relationship between these two components was provided using antitubercular drugs such as ethambutol or isoniazid known to inhibit the biosynthesis of arabinogalactan or mycolic acid, respectively. Finally, DMAG was identified in the cell wall of M. tuberculosis. This opens the possibility of a potent biological function for DMAG that may be important to mycobacterial pathogenesis.

Small membrane proteins emerge as a novel class of regulatory molecules in bacteria. Experiments carried out in Mycobacterium bovis BCG indicate that the ompATb gene (Rv0899), encoding a major outer membrane protein, is organized in operon with Rv0900 and Rv0901, encoding two small proteins with a predicted transmembrane domain. Fractioning experiment confirmed the association of Rv0901 with the membrane fraction. To investigate the role of Rv0900 and Rv0901 in M. bovis BCG, we have constructed a strain deleted for the whole operon as well as complemented strains carrying a deletion of Rv0900 or a frameshift mutation in either Rv0900 or Rv0901. Importantly, mutations in Rv0900 and/or Rv0901 strongly altered OmpATb expression, demonstrating that Rv0900 and Rv0901 play a regulatory role, which appears to occur at a post-transcriptional level., (Copyright © 2011 Elsevier Ltd. All rights reserved.)

Background: New diagnosis tests are urgently needed to address the global tuberculosis (TB) burden and to improve control programs especially in resource-limited settings. An effective in vitro diagnostic of TB based on serological methods would be regarded as an attractive progress because immunoassays are simple, rapid, inexpensive, and may offer the possibility to detect cases missed by standard sputum smear microscopy. However, currently available serology tests for TB are highly variable in sensitivity and specificity. Lipolytic enzymes have recently emerged as key factors in lipid metabolization during dormancy and/or exit of the non-replicating growth phase, a prerequisite step of TB reactivation. The focus of this study was to analyze and compare the potential of four Mycobacterium tuberculosis lipolytic enzymes (LipY, Rv0183, Rv1984c and Rv3452) as new markers in the serodiagnosis of active TB., Methods: Recombinant proteins were produced and used in optimized ELISA aimed to detect IgG and IgM serum antibodies against the four lipolytic enzymes. The capacity of the assays to identify infection was evaluated in patients with either active TB or latent TB and compared with two distinct control groups consisting of BCG-vaccinated blood donors and hospitalized non-TB individuals., Results: A robust humoral response was detected in patients with active TB whereas antibodies against lipolytic enzymes were infrequently detected in either uninfected groups or in subjects with latent infection. High specifity levels, ranging from 93.9% to 97.5%, were obtained for all four antigens with sensitivity values ranging from 73.4% to 90.5%, with Rv3452 displaying the highest performances. Patients with active TB usually exhibited strong IgG responses but poor IgM responses., Conclusion: These results clearly indicate that the lipolytic enzymes tested are strongly immunogenic allowing to distinguish active from latent TB infections. They appear as potent biomarkers providing high sensitivity and specificity levels for the immunodiagnosis of active TB.

Out of 120 patients with chronic liver diseases (45 liver cirrhosis, 38 chronic hepatitis, 15 fatty degeneration of the liver and 22 stasis liver) the osmotic resistance of the erythrocytes after Hennemann and the mechanic resistance after Schubothe was determined. 24% of the patients had a decreased osmotic resistance of the erythrocytes, even 55% a decreased incubation resistance. 16% of the patients with liver diseases had a decreased mechanic resistance of the erythrocytes. The comparison of the groups of disease and the stages of the diseases resulted in an increased mechanical resistance of the erythrocytes only for the decompensated liver cirrhosis. A positive correlation was the result between the degree of the haemolysis and the spherical index of the erythrocytes.

Jablon, James M. (National Children's Cardiac Hospital, Miami, Fla.), Betty Brust, and Milton S. Saslaw. beta-Hemolytic streptococci with group A and type II carbohydrate antigens. J. Bacteriol. 89:529-534. 1965.-Ten strains of beta-hemolytic streptococci with unusual somatic antigens were isolated from excised tonsils or throat cultures or both. Acid extracts of these strains reacted with commercial group A and group F antisera, but gave no reaction when tested with 35 type-specific group A antisera. Serum cross-absorption and agar-gel diffusion studies established the identity of the reactive antigens as the specific carbohydrates of group A and of type II. The latter antigen has been found in many strains of group F streptococci. The organisms do not possess the group-specific carbohydrate of group F, and the reaction with the commercial group F antiserum is due to the presence of type II antibody in the antiserum. The organisms give a stronger reaction to fluorescein-conjugated type II antiserum than to group A. However, the organisms have only one group-specific carbohydrate, that of group A, and, tentatively, should be classified as such.