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.

Genetic regulation, Genetic transcription, Transcription (Genetics), Mutation (Biology), Mutation

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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.

Bacterial proteins, Amino acid sequence, Amino acid sequencing

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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.

Proteins

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