Bacterial Urease and its Role in Long-Lasting Human Diseases

Author(s): Iwona Konieczna, Paulina Zarnowiec, Marek Kwinkowski, Beata Kolesinska, Justyna Fraczyk, Zbigniew Kaminski, Wieslaw Kaca

Journal Name: Current Protein & Peptide Science

Volume 13 , Issue 8 , 2012

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Urease is a virulence factor found in various pathogenic bacteria. It is essential in colonization of a host organism and in maintenance of bacterial cells in tissues. Due to its enzymatic activity, urease has a toxic effect on human cells. The presence of ureolytic activity is an important marker of a number of bacterial infections. Urease is also an immunogenic protein and is recognized by antibodies present in human sera. The presence of such antibodies is connected with progress of several long-lasting diseases, like rheumatoid arthritis, atherosclerosis or urinary tract infections. In bacterial ureases, motives with a sequence and/or structure similar to human proteins may occur. This phenomenon, known as molecular mimicry, leads to the appearance of autoantibodies, which take part in host molecules destruction. Detection of antibodies- binding motives (epitopes) in bacterial proteins is a complex process. However, organic chemistry tools, such as synthetic peptide libraries, are helpful in both, epitope mapping as well as in serologic investigations.

In this review, we present a synthetic report on a molecular organization of bacterial ureases - genetic as well as structural. We characterize methods used in detecting urease and ureolytic activity, including techniques applied in disease diagnostic processes and in chemical synthesis of urease epitopes. The review also provides a summary of knowledge about a toxic effect of bacterial ureases on human body and about occurrence of anti-urease antibodies in long-lasting diseases.

Keywords: Antibodies, long-lasting diseases, synthetic peptides, urease, UREASE PRODUCING ORGANISMS, Ureolytic activity, Proteus mirabilis, Ureapasma urealyticum, Klebsiella spp, Corynebacterium sp. D2

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Article Details

Year: 2012
Page: [789 - 806]
Pages: 18
DOI: 10.2174/1389203711213080008

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