Disease relevance of Neisseriaceae

• Pathogenic members of the Neisseriaceae and Pasteurellaceae express outer-membrane receptor proteins involved in the direct assimilation of iron from the host glycoproteins transferrin and lactoferrin [1].
• Strains of gonococci that were transformed into maltose utilizers by DNA from Neisseria lactamica and Neisseria meningitidis showed no change in the isoenzymes so that they could still be differentiated from meningococci and other Neisseriaceae by isoenzyme electrophoresis [2].
• The microflora was dominated by Neisseriaceae, Enterobacteriaceae, and lactic acid bacteria during production [3].
• Pseudomonas, Neisseriaceae, Enterobactericeae, Coryneform, Acinetobacter and lactic acid bacteria dominated the microflora of cold-smoked salmon plants, whereas the microflora in a plant processing semi-preserved herring consisted of Pseudomonas, Alcaligenes and Enterobactericeae [4].

High impact information on Neisseriaceae

• Beta-lactamase production in commensal Neisseriaceae [5].
• The Neisseriaceae can acquire iron (Fe) from lactoferrin (Lf) using host-Lf receptors on the bacterial surface [6].
• Many pathogens of the Pasteurellaceae and Neisseriaceae possess a surface receptor that binds transferrin (Tf) as an initial step in an iron acquisition process [7].
• In contrast, bacterial lactoferrin receptors have only been described for human pathogens in the family Neisseriaceae, and were believed to consist of a single protein, Lbp1, which is highly homologous to Tbp1 [8].
• Two monoclonal antibodies (G6 and 7B), generated against a 63-kDa stress protein (GSP63) from Neisseria gonorrhoeae strain VP1, were used to investigate the antigenic heterogeneity of GSP63 among the Neisseriaceae and its antigenic relationship with the Hsp60 heat-shock protein family [9].

Chemical compound and disease context of Neisseriaceae

• Neisseriaceae, a group of bacteria with dihydrofolate reductases, moderately susceptible to trimethoprim [10].
• Dihydrofolate reductases of five species of the family Neisseriaceae were compared by means of inhibition profiles, using several structurally different inhibitors, including trimethoprim (TMP) and pyrimethamine [10].
• A number of bacterial species in the Neisseriaceae have developed a mechanism for acquiring iron directly from this host glycoprotein which involves surface receptors capable of specifically binding lactoferrin [11].

Gene context of Neisseriaceae

• Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae [12].
• Biochemical analysis of lactoferrin receptors in the Neisseriaceae: identification of a second bacterial lactoferrin receptor protein [8].

References