Missense mutations that alter the DNA-binding domain of the MtrR protein occur frequently in rectal isolates of Neisseria gonorrhoeae that are resistant to faecal lipids
Article Abstract:
Analysis of the structure of Neisseria gonorrhoeae shows that mutations in the multiple transferable resistance Regulator may be responsible for the bacteria's resistance to antibiotics. The analysis was initially determined for clinical isolates, but was found to also apply to rectal isolates. Fecal lipids were examined for resistance because they are able to cause the emergence of such variants. The most common missense mutation noticed was in codon 45.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
The phase-variable pilus-associated protein PilC is commonly expressed in clinical isolates of Neisseria gonorrhoeae, and shows sequence variability among strains
Article Abstract:
Several strains of Neisseria gonorrhoeae with identified epidemiological data were analyzed for production of the PilC protein. PilC is related to the pilus-mediated adherence of pathogenic Neisseria to target cells. Results show differences in the amino acid sequence of the tested strains. This indicates that PilC sequences differ among gonococcal strains despite the common expression of the phase-variable protein.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
User Contributions:
Comment about this article or add new information about this topic:
Identification of an EF-Tu protein that is periplasm-associated and processed in Neisseria gonorrhoeae
Article Abstract:
The peptide sequence derived from a cyanogen-bromide-cleaved fragment of a 44 kDa protein which is a dominant component of periplasmic extracts of Neisseria gonorrhoeae, was found to be homologous with elongation factor Tu (EF-Tu). A synthetic peptide antiserum specific for a component of the C terminus of EF-Tu confirmed that the 37 kDa protein in whole-cell lysates of N. gonorrhoeae was a processed form of EF-Tu.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Suppressing posttranslational gluconoylation of heterologous proteins by metabolic engineering of Escherichia coli
- Abstracts: The bHLH protein PTF1-p48 is essential for the formation of the exocrine and the correct spatial organization of the endocrine pancreas
- Abstracts: Expression of the actin gene family in embryos of the sea urchin Lytechinus pictus. Integrin alpha(sub v) subunit is expressed on mesodermal cell surfaces during amphibian gastrulation
- Abstracts: Developmental regulation of Fos-protein during proliferative growth of the otic vesicle and its relation to differentiation induced by retinoic acid
- Abstracts: A ten-year study of the stopover patterns of migratory passerines during fall migration on Appledore Island, Maine