What is it about?
Leucine aminopeptidases are proteases that cleave a broad spectrum of amino acids off the N-termini of proteins. Here we show that in addition to protease activity, leucine aminopeptidase from Mycoplasma hyopneumoniea, an economically significant pig pathogen, acts as a DNA-binding protein, and as an adhesin by binding to heparin and plasminogen.
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Why is it important?
When a protein has two or more distinct biological activities it is referred to as a moonlighting protein. Identifying adhesins in Mycoplasma hyopneumoniae is important as they facilitate attachment to respiratory cilia and establish infection. Surface-exposed DNA-binding proteins play roles in preventing adaptive immune responses and in biofilm formation. By demonstrating that this leucine aminopeptidase has three distinct biological activities on the surface of a pathogen that is prevalent in pig farms worldwide, we introduce an attractive therapeutic target.
Perspectives
This was the first paper I published during my PhD candidature. I found it fascinating that proteins, which are generally defined as having a single function, have the potential of having additional, completely unrelated functions. It adds complexity to pathogenesis.
Dr Veronica M Jarocki
University of Technology Sydney
Read the Original
This page is a summary of: MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae, Open Biology, January 2015, Royal Society Publishing,
DOI: 10.1098/rsob.140175.
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