Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Extracellular and surface-exposed polysaccharides of non-tuberculous mycobacteria

Article Abstract:

Comparison of the extracellular materials (ECMs) and the surface-exposed materials (SXMs) of five pathogenic and non-pathogenic mycobacterial species reveals that the glycosyl composition of the ECMs and SXMs in a given species are similar. However, the SXMs of M. avium and M. phlei lack arabinose and their polysaccharides lack arabinomannans. Anion-exchange and gel-filtration chromatography indicate that the polysaccharides in the materials are neutral. The polysaccharides of ECMs consist of glycogen-like glucans, mannans and arabinomannans of high molecular mass.

Author: Lemassu, Anne, Daffe, Mamadou, Ortalo-Magne, Annick, Bardou, Fabienne, Silve, Gaby, Laneelle, Marie-Antoinette
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
Analysis, Polysaccharides

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


The outermost capsular arabinomannans and other mannoconjugates of virulent and avirulent tubercle bacilli

Article Abstract:

The occurrence and structure of the outermost mannoconjugates of the capsule of five strains of the tubercle bacillus differing in their degrees of virulence were studied. The extracellular and surface-exposed arabinomannan-containing polysaccharides were found to be made mostly of neutral fatty-acyl-free arabinomannans with a reducing end made of mannose. Findings indicated that mannosylated molecules are not involved in the selective phagocytosis of virulent tubercle bacilli.

Author: Daffe, Mamadou, Ortalo-Magne, Annick, Andersen, Ase B.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
Tuberculosis

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Mechanisms of pyrazinamide resistance in mycobacteria: importance of lack of uptake in addition to lack of pyrazinamidase activity

Article Abstract:

A study was conducted to analyze the uptake mechanism of the antituberculosis drug, pyrazinamide, in Mycobacterium tuberculosis. Results indicated that one of the mechanisms of resistance to pyrazinamide resides in the failure of strains to take up the drug. Findings also showed that susceptibility to the drug in mycobacteria requires the presence of a functional PZase and a PZA transport system.

Author: Laneelle, Gilbert, Daffe, Mamadou, Raynaud, Catherine, Laneelle, Marie-Antoinette, Draper, Philip, Senaratne, Ryan H.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
Antitubercular agents, Pyrazinamide

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Mycobacteria, Mycobacterium, Mycobacterium tuberculosis
Similar abstracts:
  • Abstracts: Evaluation of a wipe surface sample method for collection of Bacillus spores from nonporous surfaces. Monochloramine inactivation of bacterial select agents
  • Abstracts: Expression of Aureobasidium pullulans xynA in, and secretion of the xylanase from, Saccharomyces cerevisiae. Monocentric and polycentric anaerobic fungi produce structurally related cellulases and xylanases
  • Abstracts: Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarinus. The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase
  • Abstracts: Purification and characterization of L-methionine gamma-lyase from Brevibacterium linens BL2. Nucleotide sequence and taxonomical distribution of the bacteriocin gene lin cloned from Brevibacterium linens M18
  • Abstracts: Enzymes involved in anaerobic polyethylene glycol degradation by Pelobacter venetianus and Bacteroides strain PG1
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.