Optimizing and accelerating the assignation of lineages in Mycobacterium tuberculosis using novel alternative single-tube assays.

The assignation of lineages in Mycobacterium tuberculosis (MTB) provides valuable information for evolutionary and phylogeographic studies and makes for more accurate knowledge of the distribution of this pathogen worldwide. Differences in virulence have also been found for certain lineages. MTB isolates were initially assigned to lineages based on data obtained from genotyping techniques, such as spoligotyping or MIRU-VNTR analysis, some of which are more suitable for molecular epidemiology studies.

The use of monoclonal antibodies anti-lectin from freshwater prawn Macrobrachium rosenbergii (DeMan, 1879) in the recognition of protein with lectin activity in Decapod's hemolymph.

We determined the cross-reactivity of a monoclonal antibody against the Macrobrachium rosenbergii lectin with proteins in the hemolymph from Procambarus clarkii (Pc), Procambarus americanus (Pa), Litopenaeus setiferus (Ls), and Pseudothelphusa americana (Psa). Crustaceans' hemolymph agglutinated erythrocytes from rat, mouse, guinea pig, and rabbit. Decapods' hemolymph hemagglutinating activity was inhibited by N-acetylated carbohydrates as well as by antibodies.

Characterization of lectin aggregates in the hemolymph of freshwater prawn Macrobrachium rosenbergii.

In invertebrates, lectins play relevant roles in innate immunity; however, their regulatory mechanisms have not been identified yet. In this work, we purified, by gel filtration and affinity chromatography, lectin aggregates circulating in the hemolymph of the freshwater prawn Macrobrachium rosenbergii and compared their physicochemical properties with a previously described lectin (MrL). High-molecular weight MrL aggregates (MrL-I) lack hemagglutinating activity and showed bands of 62.

Isolation of a 19-kDa mycobacterium, bovis-specific antigen, different from MPB70/80, by chromatofocusing.

Two antigens, 19-kDa each, were purified from Mycobacterium bovis culture filtrate protein extract by chromatofocusing. Antigen I had a 4.5 pI, and its amino terminal (DPVDAVINTTCNYGQVVAALNATDP) showed a 100% homology with the hypothetical protein Rv1174c.