Abstract
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
Current Protein & Peptide Science
Title:Bacterial Urease and its Role in Long-Lasting Human Diseases
Volume: 13 Issue: 8
Author(s): Iwona Konieczna, Paulina Zarnowiec, Marek Kwinkowski, Beata Kolesinska, Justyna Fraczyk, Zbigniew Kaminski and Wieslaw Kaca
Affiliation:
Keywords: Antibodies, long-lasting diseases, synthetic peptides, urease, UREASE PRODUCING ORGANISMS, Ureolytic activity, Proteus mirabilis, Ureapasma urealyticum, Klebsiella spp, Corynebacterium sp. D2
Abstract: 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.
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Cite this article as:
Konieczna Iwona, Zarnowiec Paulina, Kwinkowski Marek, Kolesinska Beata, Fraczyk Justyna, Kaminski Zbigniew and Kaca Wieslaw, Bacterial Urease and its Role in Long-Lasting Human Diseases, Current Protein & Peptide Science 2012; 13 (8) . https://dx.doi.org/10.2174/138920312804871094
DOI https://dx.doi.org/10.2174/138920312804871094 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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