muramidase and Tuberculosis

Lysozyme level was measured in the fluid and serum of 42 tuberculous (25 pleural, 11 ascites and 6 pericardial) and 29 non-tuberculous (5 malignant, 9 empyema thoracis, 10 transudative ascites and 5 pyopericardium) effusions. The mean fluid lysozyme level was significantly raised in tuberculous pleural, ascites, and pericardial effusions in comparison to malignant pleural (p <0.001), transudative ascites (p < 0.001), and pyopericardium (p < 0.02) cases, respectively. The mean fluid/serum lysozyme ratio did not differ significantly between tuberculous and their corresponding non-tuberculous effusions. The confirmed tuberculous pleural effusion patients had significantly higher mean fluid lysozyme level and fluid/serum lysozyme ratio when compared with clinical cases (p < 0.05). The cut-off fluid lysozyme level of > or = 50/UI(-1) and fluid/serum lysozyme ratio of > or = 1.1 were considered for the diagnosis of tuberculous effusions; the sensitivity and specificity of fluid lysozyme and fluid/serum lysozyme ratios were 100, 100 per cent, and 97.6, 33.3 per cent, respectively, on excluding the patients with purulent effusions. A significant correlation was observed between the fluid and serum lysozyme levels in tuberculous effusions (r = 0.39,p < 0.01). Thus, fluid lysozyme was found to be a better and reliable test than fluid/serum lysozyme ratio for the diagnosis of tuberculous effusions in children.

Topics: Adolescent; Ascitic Fluid; Biomarkers; Child; Child, Preschool; Female; Humans; Infant; Male; Muramidase; Pericardial Effusion; Pleural Effusion; Reference Values; Regression Analysis; Sensitivity and Specificity; Tuberculosis

The increasing incidence of multidrug-resistant

Topics: Animals; Antitubercular Agents; Bacteriocins; Cell Line; Drug Synergism; Ethambutol; Humans; Macrophages; Mice; Microbial Sensitivity Tests; Muramidase; Mycobacterium tuberculosis; RAW 264.7 Cells; Tuberculosis

Virulence factors (VFs) contribute to the emergence of new human Mycobacterium tuberculosis strains, are lineage dependent, and are relevant to the development of M. tuberculosis drugs/vaccines. VFs were sought within M. tuberculosis lineage 3, which has the Central Asian (CAS) spoligotype. Three isolates were selected from clusters previously identified as dominant in London, United Kingdom. Strain-associated virulence was studied in guinea pig, monocyte-derived macrophage, and lysozyme resistance assays. Whole-genome sequencing, single nucleotide polymorphism (SNP) analysis, and a literature review contributed to the identification of SNPs of interest. The animal model revealed borderline differences in strain-associated pathogenicity. Ex vivo, isolate C72 exhibited statistically significant differences in intracellular growth relative to C6 and C14. SNP candidates inducing lower fitness levels included 123 unique nonsynonymous SNPs, including three located in genes (lysX, caeA, and ponA2) previously identified as VFs in the laboratory-adapted reference strain H37Rv and shown to confer lysozyme resistance. C72 growth was most affected by lysozyme in vitro. A BLAST search revealed that all three SNPs of interest (C35F, P76Q, and P780R) also occurred in Tiruvallur, India, and in Uganda. Unlike C72, however, no single isolate identified through BLAST carried all three SNPs simultaneously. CAS isolates representative of three medium-sized human clusters demonstrated differential outcomes in models commonly used to estimate strain-associated virulence, supporting the idea that virulence varies within, not just across, M. tuberculosis lineages. Three VF SNPs of interest were identified in two additional locations worldwide, which suggested independent selection and supported a role for these SNPs in virulence. The relevance of lysozyme resistance to strain virulence remains to be established.

Topics: Adult; Antitubercular Agents; Asia; Bacterial Proteins; Drug Resistance, Bacterial; Female; Gene Expression Regulation, Bacterial; Humans; Male; Middle Aged; Muramidase; Mycobacterium tuberculosis; Polymorphism, Single Nucleotide; Tuberculosis; Virulence; Virulence Factors; Young Adult

Tuberculosis is a chronic infectious disease caused by Mycobacterium tuberculosis that is responsible for almost 1.5 million deaths per year. Sensing of mycobacteria by the host's immune system relies on different families of receptors present on innate immune cells. Amongst them, several members of the TLR family are involved in the activation of immune cells by mycobacteria, yet the in vivo contribution of individual TLRs to the protective immune response remains controversial. On the contrary, MyD88, the adaptor molecule for most TLRs, plays a non-redundant role in the protection against tuberculosis and mice with a complete germline deletion of MyD88 succumb very early to infection. MyD88 is expressed in both immune and non-immune cells, but it is not clear whether control of mycobacteria requires ubiquitous or cell-type specific MyD88 expression. Therefore, using novel conditional switch-on mouse models, we aimed to investigate the importance of MyD88 signalling in DCs and macrophages for the induction of protective effector mechanisms against mycobacterial infection. We conclude that specific reactivation of MyD88 signalling in CD11c- or lysozyme M-expressing myeloid cells during Mycobacterium bovis Bacille Calmette-Guerin infection is sufficient to restore systemic and local inflammatory cytokine production and to control pathogen burden.

Topics: Animals; CD11c Antigen; Chronic Disease; Cytokines; Dendritic Cells; Disease Models, Animal; Gene Deletion; Humans; Macrophages; Mice; Mice, Knockout; Muramidase; Mycobacterium bovis; Myeloid Differentiation Factor 88; Signal Transduction; Tuberculosis

Serine/threonine protein kinases (STPK) play a major role in the physiology and pathogenesis of Mycobacterium tuberculosis. Here, we have examined the role of pknE, a STPK in the adaptive responses of M. tuberculosis using a deletion mutant ΔpknE. The survival of ΔpknE was assessed in the presence of stress (pH, surfactant and cell wall-damaging agents) and anti-tuberculosis drugs. ΔpknE had a defective growth in pH 7.0 and lysozyme (a cell wall-damaging agent) with better survival in pH 5.5, SDS and kanamycin (a second-line anti-tuberculosis drug). Furthermore, ΔpknE was reduced in cell size during growth in liquid media and exhibited hypervirulence in a guinea pig model of infection. In conclusion, our data suggest that pknE plays a role in adaptive response of M. tuberculosis regulating cellular integrity and survival.

Topics: Animals; Antitubercular Agents; Drug Resistance, Bacterial; Guinea Pigs; Hydrogen-Ion Concentration; Muramidase; Mycobacterium tuberculosis; Polymorphism, Restriction Fragment Length; Protein Serine-Threonine Kinases; Sequence Deletion; Sodium Dodecyl Sulfate; Stress, Physiological; Tuberculosis

Mycobacterium tuberculosis, the etiologic agent of tuberculosis (TB) possesses at least five genes predicted to encode proteins with NlpC/P60 hydrolase domains, including the relatively uncharacterized Rv2190c. As NlpC/P60 domain-containing proteins are associated with diverse roles in bacterial physiology, our objective was to characterize Rv2190c in M. tuberculosis growth and virulence. Our data indicate that lack of Rv2190c is associated with impaired growth, both in vitro and during an in vivo mouse model of TB. These growth defects are associated with altered colony morphology and phthiocerol dimycocerosate levels, indicating that Rv2190c is involved in cell wall maintenance and composition. In addition, we have demonstrated that Rv2190c is expressed during active growth phase and that its protein product is immunogenic during infection. Our findings have significant implications, both for better understanding the role of Rv2190c in M. tuberculosis biology and also for translational developments.

Topics: Animals; Bacterial Proteins; Female; Gene Expression Regulation, Bacterial; Genetic Complementation Test; Lipids; Mice; Mice, Inbred BALB C; Microscopy, Electron, Transmission; Muramidase; Mutation; Mycobacterium tuberculosis; Phenotype; Protein Biosynthesis; Tuberculosis; Virulence; Virulence Factors

Manipulating Mycobacterium tuberculosis clinical specimens and cultures represents a risk factor for laboratory personnel. One of the processes that requires high concentrations of microorganisms is DNA extraction for molecular procedures. Pulmonary tuberculosis cases have occurred among professionals in charge of molecular procedures that require manipulation of massive quantities of microorganisms. This has prompted research studies on biosafety aspects of extraction protocols; however, as yet, no consensus has been reached regarding risks associated with the process.. The biosafety was evaluated for the DNA extraction protocol of van Soolingen, et al. 2002 by determining M. tuberculosis viability at each process stage.. Eight hundred eighty cultures were grown from 220 M. tuberculosis clinical isolates that had been processed through the first three DNA extraction stages. Molecular identifications of positive cultures used a PCR isolation of a fragment of the heat shock protein PRA-hsp65 and examination of its restriction enzyme profile (spoligotyping).. Growth was seen in one culture with one of the procedures used. The molecular characterization did not correspond to the initially analyzed isolate, and therefore was deduced to be the product of a cross-contamination.. The DNA extraction protocol, as described by van Soolingen, et al. 2002 and as implemented at the Instituto Nacional de Salud, was established to be safe for laboratory personnel as well as for the environment.

Topics: Academies and Institutes; Bacteriological Techniques; Cell Fractionation; Chemical Fractionation; Clinical Laboratory Techniques; Colombia; Containment of Biohazards; DNA, Bacterial; Endopeptidase K; Hot Temperature; Humans; Medical Laboratory Personnel; Muramidase; Mycobacterium tuberculosis; Occupational Exposure; Safety Management; Specimen Handling; Tuberculosis

Tuberculosis remains a major global health problem that kills up to 2 million people annually. Central to the success of Mycobacterium tuberculosis (Mtb) as a pathogen is its ability to evade host immunity and to establish a chronic infection. Although its primary intracellular niche is within macrophages, the underlying molecular mechanisms are poorly understood. Here we show that Rv2224c, a cell envelope-associated predicted protease, is critical for Mtb virulence. Disruption of Rv2224c led to prolonged survival of infected mice and highly reduced lung pathology. Absence of Rv2224c enhanced host innate immune responses, compromised the intracellular survival of Mtb in macrophages, and increased its susceptibility to lysozyme. We provide insights into the molecular basis for Rv2224c function by showing that Rv2224c activity promotes processing and extracellular release of the Mtb protein, GroEL2. Inhibition of Rv2224c and its targets offers opportunities for therapeutic interventions and immune-modulatory strategies.

Topics: Amino Acid Sequence; Animals; Cell Membrane; Cell Survival; Humans; Immune System; Macrophages; Mice; Mice, Inbred C57BL; Mice, Transgenic; Models, Genetic; Molecular Sequence Data; Muramidase; Mycobacterium bovis; Mycobacterium tuberculosis; Plasmids; Time Factors; Tuberculosis

CD4(+) T cells are central in mediating granuloma formation and limiting growth and dissemination of mycobacterial infections. To determine whether T cells responding to influenza infection can interact with T cells responding to Mycobacterium bovis bacille Calmette-Guérin (BCG) infection and disrupt granuloma formation, we infected mice containing two monoclonal T cell populations specific for the model Ags pigeon cytochrome c (PCC) and hen egg lysozyme (HEL). These mice were chronically infected with PCC epitope-tagged BCG (PCC-BCG) and acutely infected with HEL epitope-tagged influenza virus (HEL-flu). In these mice, PCC-BCG infection is much more abundant in the liver than the lung, whereas HEL-flu infection is localized to the lung. We observe that both T cells have access to both inflammatory sites, but that PCC-specific T cells dominate the PCC-BCG inflammatory site in the liver, whereas HEL-specific T cells dominate the HEL-flu inflammatory site in the lung. Influenza infection, in the absence of an influenza-specific T cell response, is able to increase the activation state and IFN-gamma secretion of PCC-BCG-specific T cells in the granuloma. Activation of HEL-specific T cells allows them to secrete IFN-gamma and contribute to protection in the granuloma. Ultimately, infection with influenza has little effect on bacterial load, and bacteria do not disseminate. In summary, these data illustrate complex interactions between T cell responses to infectious agents that can affect effector responses to pathogens.

Topics: Animals; Antigens; Cell Communication; Chickens; Clone Cells; Columbidae; Cytochromes c; Granuloma; Humans; Immunity; Influenza, Human; Mice; Mice, Knockout; Muramidase; Mycobacterium bovis; T-Lymphocytes; Tuberculosis

Live mycobacteria secrete a number of unique proteins early in their multiplication which are important for both the pathogenesis and the stimulation of specific host responses. We have investigated the mechanisms by which the host mounts immune response against tuberculosis after vaccination with secretory proteins (SP) of a vaccine candidate Mycobacterium habana TMC 5135. Mice vaccinated with SP of 10th day growth of M. habana, either alone or emulsified in Freund's incomplete adjuvant (FIA) possessed antituberculous resistance and cellular immune responses against M. tuberculosis H37Rv. These proteins induced a significant cutaneous delayed type hypersensitivity response in guinea pigs vaccinated with heat killed M. tuberculosis H37Rv, which was equivalent to that observed with a standard purified protein derivative (PPD). The splenocytes of these guinea pigs have shown higher proliferative response after stimulation with SP than with PPD. The SP + FIA immunization has been found to exert maximum prophylactic effect by potentiating both the oxygen dependent arms and enzymatic activities of macrophages. Macrophages from mice vaccinated with SP of M. habana produced enhanced levels of interleukin(IL)-2, interleukin-12 and interferon(IFN)-gamma. The protective as well as cell mediated immune responses were upregulated in SP immunized animals when compared to whole cell (M. habana) vaccinated animals. SDS-PAGE of SP from M. habana showed the prominent bands of 60, 32, 31 and 30 kDa. Furthermore, the western analysis of SP with pulmonary tuberculosis patient's serum has revealed the presence of immunoreactive antigens of 36, 35, 33/32 kDa. Overall study demonstrated that the secretory antigens released by actively growing M. habana bacilli could activate different arms of effective immune response.

Topics: Acid Phosphatase; Animals; Bacterial Proteins; Blotting, Western; Disease Models, Animal; Electrophoresis, Polyacrylamide Gel; Glucuronidase; Interferon-gamma; Interleukin-12; Interleukin-2; Mice; Mice, Inbred AKR; Muramidase; Mycobacterium; Reactive Oxygen Species; Tuberculosis

Serum adenosine deaminase (ADA) activity and lysozyme levels were measured in 51 patients with tuberculosis (21 pulmonary, 15 miliary, 11 neurotuberculoma and four abdominal plus osteoarticular) and 20 healthy controls. The mean serum ADA activity and lysozyme levels were significantly raised in children with different forms of tuberculosis in comparison with controls (p < 0.001). The neurotuberculoma cases had the lowest mean enzyme levels and the differences were significant when compared with other forms of tuberculosis. The cut-off serum ADA activity of > or = 42 IU/l and lysozyme level of > or = 20 U/l were diagnostic of tuberculosis with 100 per cent sensitivity. A significant correlation was observed between the two parameters (r = 0.66; p < 0.001). Thus, with compatible clinical presentation, the raised serum level of either ADA or lysozyme can be used as a supportive diagnostic test.

Topics: Adenosine Deaminase; Adolescent; Case-Control Studies; Child; Child, Preschool; Female; Humans; Infant; Male; Muramidase; Predictive Value of Tests; Tuberculosis

The catalytic concentration of pleural adenosine deaminase (ADA) and the ratio of pleural lysozyme (PL) to serum lysozyme (SL) were measured in consecutive patients (49 tuberculous and 179 nontuberculous) with two automated procedures in a Hitachi 717 analyzer. Using sensitivity and specificity curves, we established cutoff values at 33 U/L for ADA and 1.7 for the PL/SL ratio. The sensitivity of ADA activities for tuberculous effusion was 90%, specificity 85%. Combining ADA with the PL/SL ratio enhanced specificity to 99%. However, high values for ADA and lysozyme ratios are not, alone or in combination, sensitive or specific enough to replace pleural biopsy or culture of pleural fluid for the diagnosis of tuberculous empyema.

Topics: Adenosine Deaminase; Autoanalysis; Clinical Enzyme Tests; Diagnosis, Differential; Empyema, Tuberculous; HIV Infections; Humans; Muramidase; Pleural Effusion; Prospective Studies; Reference Values; Tuberculosis

Topics: Antibodies, Bacterial; Antigens, Bacterial; Humans; Lipopolysaccharides; Muramidase; Mycobacterium; Serologic Tests; Tuberculosis

Active tuberculosis (TB) and leprosy are difficult to diagnose early because there are few organisms to detect and the specific immune response does not distinguish between active and inactive disease. We developed an immunoassay for lysozyme to see whether serum lysozyme levels could be used to identify individuals with clinical leprosy or TB. The immunoassay for lysozyme proved superior to standard enzyme assays that were less sensitive and reliable. The lysozyme assay was compared with assays for antibodies to Mycobacterium tuberculosis lipoarabinomannan (LAM) and M. leprae phenolic glycolipid-1. The sera tested were from Ethiopian leprosy (paucibacillary and multibacillary) and TB patients and from healthy Ethiopian and U.S. controls. The lysozyme assay was able to detect more of the individuals with TB (sensitivity, 100% for 19 patients) or leprosy (sensitivity, 86% for 36 patients) than either antibody assay. In particular, lysozyme levels were raised in a higher proportion of the paucibacillary leprosy patients (83% of 17), for whom the antibody assays were less sensitive; the LAM IgG and the phenolic glycolipid-1 IgM levels were raised in only 62 and 44% of 16 patients, respectively. The data suggest that lysozyme measurements may be useful in the diagnosis of mycobacterial infections and other chronic infectious granulomatoses.

Topics: Antibodies, Bacterial; Antigens, Bacterial; Glycolipids; HIV Infections; Humans; Immunoassay; Leprosy; Lipopolysaccharides; Muramidase; Tuberculosis

Topics: Adenosine Deaminase; Aged; Clinical Enzyme Tests; Humans; Male; Muramidase; Pleural Effusion; Tuberculosis

This study is an attempt to understand the mechanism of macrophage activation and its effect on the microbicidal properties of the macrophage. Alveolar macrophages (AM) from normal and BCG-vaccinated guinea pigs were harvested at intervals of 1, 7, 14, 21, and 28 days. Half of the guinea pigs from each group were challenged intratracheally with Mycobacterium tuberculosis H37Rv. In AM, the levels of three lysosomal enzymes, beta-galactosidase (beta-gal), N-acetylglucosaminidase (N-ac), and lysozyme (lyso), were measured histochemically. The percentage of AM staining positively for these enzymes and the intensity of this staining were estimated as parameters of AM activation, along with the number of intracellular bacilli in these cells. Histochemical methods are preferred to biochemical methods as only the former indicate activation in individual cells. The enzymatic responses of AM depend on the type of vaccination and infection. Thus, beta-gal activity was significantly enhanced in immune animals whereas no such enhancement of activity was observed in the case of N-ac and lyso. The N-ac content was higher in infected animals and in the immune group, whereas lyso fluctuated at different time intervals after infection.

Topics: Acetylglucosaminidase; Animals; beta-Galactosidase; Female; Guinea Pigs; Macrophage Activation; Macrophages; Male; Muramidase; Mycobacterium tuberculosis; Pulmonary Alveoli; Time Factors; Tuberculosis

Seven patients with Hodgkin's disease were studied for the presence of lysozyme and alpha-1-antitrypsin activity by immunoelectron microscopy. As a result, Reed-Sternberg cells, Hodgkin's cells, and atypical cells were distinctly positive for lysozyme in four cases and weakly positive in the remaining three cases. These cells were also positive for alpha-1-antitrypsin in all cases. Because the cells of the monocyte-macrophage lineage also bore lysozyme and alpha-1-antitrypsin, it is suggested that Reed-Sternberg cells, Hodgkin's cells, and the atypical cells are derived from the monocyte-macrophage lineage.

Topics: alpha 1-Antitrypsin; Histocytochemistry; Hodgkin Disease; Humans; Immunoenzyme Techniques; Leukemia, Myeloid; Lymph Nodes; Lymphatic Diseases; Macrophages; Microscopy, Electron; Monocytes; Muramidase; Sarcoidosis; Tuberculosis

Topics: Animals; Guinea Pigs; Humans; Lysosomes; Macrophages; Muramidase; Mycobacterium tuberculosis; Phagocytosis; Rabbits; Tuberculosis

Topics: Humans; Hypokalemia; Leukemia, Myeloid, Acute; Muramidase; Sarcoidosis; Tuberculosis

The muramidase content of reactive cells in the lesions of human foreign body reactions, lepromatous and tuberculoid leprosy, sarcoidosis, tuberculosis, and granulomatous hepatitis, was assessed using specific anti-human muramidase antiserum and a peroxidase-anti-peroxidase marker system. Epithelioid and giant cells in sarcoidosis, tuberculosis, granulomatous hepatitis, and tuberculoid leprosy all showed the presence of muramidase in their cytoplasm. The muramidase content of macrophages in foreign body reactions and lepromatous leprosy varied and most multinucleate cells in these lesions gave a negative reaction. Possibly varying rates of muramidase secretion may account for these differences.

Topics: Cytoplasm; Foreign-Body Reaction; Hepatitis; Humans; Leprosy; Lung; Lymph Nodes; Muramidase; Sarcoidosis; Tuberculosis

Lysozyme activity of macrophages and giant cells in various human granulomas were examined with immunoperoxidase bridge method in tissue sections. Various numbers of epithelioid cells and giant cells of epithelioid cell granulomas of tuberculosis, sarcoidosis and Crohn's disease exhibited intense granular cytoplasmic lysozyme activity. Foreign body granulomas induced with various substances showed negative or faintly positive lysozyme stain. Macrophages and giant cells of aspergillus granuloma associated with thymus hypoplasia and T-cell depression contained no lysozyme. The results suggest that cell-mediated immunology plays an important role for the lysozyme synthesis of macrophages in granuloma.

Topics: Aspergillosis; Child, Preschool; Crohn Disease; Foreign-Body Reaction; Granuloma; Humans; Macrophages; Muramidase; Sarcoidosis; T-Lymphocytes; Thymus Gland; Tuberculosis

The distribution of muramidase (lysozyme) in normal and pathological human tissues has been studied, using an immunohistological technique. The enzyme was demonstrated in a variety of healthy tissues, including serous salivary acinar cells, lactating mammary tissue, Paneth cells, renal tubular cells, myeloid cells (including eosinophils), and histiocytic cells. In pathological tissues the most striking positivity was encountered in reactive histiocytic cells in granulomatous conditions such as tuberculosis and Crohn's disease. The finding of this study are related to previous reports of the distribution of human and animal muramidase and the implications of patterns of muramidase staining in pathological histiocytes are briefly discussed.

Topics: Bone Marrow; Bone Marrow Cells; Breast; Crohn Disease; Eosinophils; Histological Techniques; Humans; Immune Sera; Immunologic Techniques; Intestinal Mucosa; Kidney Tubules, Distal; Kidney Tubules, Proximal; Kupffer Cells; Lacrimal Apparatus; Lymph Nodes; Muramidase; Salivary Glands; Tuberculosis

Topics: Egg White; Humans; Leukemia; Leukemia, Lymphoid; Leukemia, Myeloid; Leukocytes; Mass Screening; Muramidase; Pyelonephritis; Sarcoidosis; Tears; Tuberculosis

Topics: Acid Phosphatase; Animals; Cell Count; Deoxyribonucleases; Esterases; Female; Glucuronidase; Lipase; Macrophages; Male; Muramidase; Pulmonary Alveoli; Rabbits; Radiation Injuries, Experimental; Ribonucleases; Tuberculosis; Tuberculosis, Pulmonary

Topics: Animals; Biological Assay; Exudates and Transudates; Genetics; Glycogen; Leukocytes; Macrophages; Mineral Oil; Muramidase; Rabbits; Research; Sarcina; Toxicology; Tuberculosis

Topics: Aging; Blood Cell Count; Blood Chemical Analysis; Clinical Enzyme Tests; Diabetes Mellitus; Geriatrics; Humans; Japan; Leukocyte Count; Leukocytes; Muramidase; Nuclear Warfare; Radiation Injuries; Respiratory Tract Diseases; Sex; Syphilis; Tuberculosis

Topics: Animals; Bacteriological Techniques; BCG Vaccine; Body Fluids; Cell Biology; Chromatography; Cricetinae; Histocytochemistry; Lung; Macrophages; Muramidase; Mycobacterium; Mycobacterium bovis; Rabbits; Rats; Research; Tissue Culture Techniques; Tissue Extracts; Tuberculin; Tuberculosis; Vaccination

Topics: Acid Phosphatase; Alkaline Phosphatase; Exudates and Transudates; Glucosidases; Leukocytes; Muramidase; Peritoneal Cavity; Tuberculosis

Topics: Blood Chemical Analysis; Clinical Enzyme Tests; Guinea Pigs; Muramidase; Rabbits; Research; Tuberculosis

Topics: Animals; Hypersensitivity, Delayed; In Vitro Techniques; Mice; Muramidase; Tuberculin; Tuberculin Test; Tuberculosis

Topics: Humans; Lung; Muramidase; Pneumonia; Tuberculosis

Topics: Animals; Anti-Infective Agents, Local; Guinea Pigs; Muramidase; Mycobacterium tuberculosis; Tuberculosis

Topics: Animals; Anti-Infective Agents, Local; Antitubercular Agents; Lung; Muramidase; Rabbits; Tuberculosis; Tuberculosis, Pulmonary

Topics: Anti-Infective Agents, Local; Humans; Muramidase; Serum; Tuberculosis

Topics: Humans; Muramidase; Saliva; Tuberculosis; Tuberculosis, Pulmonary

Topics: Anti-Infective Agents, Local; Blood; Dermatologic Agents; Humans; Isoniazid; Muramidase; Niacin; Nicotinic Acids; Tuberculosis

Topics: Humans; Leukocytes; Muramidase; Patient Discharge; Plasma; Tuberculin; Tuberculosis

Topics: Aminosalicylic Acid; Glycoside Hydrolases; Lipase; Muramidase; Tuberculosis; Tuberculosis, Osteoarticular

Topics: Humans; Lung; Muramidase; Neoplasms; Tuberculoma; Tuberculosis; Tuberculosis, Pulmonary