Utilization of patterns of biotinyl-polypeptides as a promising analytical target for bacterial identification.

Abstract The family of biotin enzymes, which are involved in carboxylation, transcarboxylation, and decarboxylation reactions in cells, is essential and conserved for bacteria. The prosthetic group biotin is stably linked to the biotinyl-polypeptide by an amide bond. Since avidin interacts with biotin in an irreversible manner, the patterns of biotinyl-polypeptides for bacterial cells could be revealed by probing them with an avidin-enzyme complex in Western blots of total cellular proteins. In this way, the family of commonly existing gene products of bacteria could be monitored and compared without the use of specific DNA probes, oligonucleotide primers, or antibodies. In this study, this approach was tested and it was found that different species of bacteria showed different patterns of biotinyl-polypeptides. Our results indicate that patterns of biotinyl-polypeptides can be a promising analytical target for bacterial identification.