Exploring the Potential Role of Moonlighting Function of the Surface-Associated Proteins From Mycobacterium bovis BCG Moreau and Pasteur by Comparative Proteomic

In this study, the proteomic profile of the surface-associated proteins from M. bovis BCG Moreau was compared to the BCG Pasteur reference strain. The methodology used was 2DE gel electrophoresis combined with mass spectrometry techniques (MALDI-TOF/TOF), leading to the identification of 115 proteins. Of these, 24 proteins showed differential expression between the two BCG strains. Furthermore, 27 proteins previously described as displaying moonlighting function were identified, 8 of these proteins showed variation in abundance comparing BCG Moreau to Pasteur and 2 of them presented two different domain hits. Moonlighting proteins are multifunctional proteins in which two or more biological functions are fulfilled by a single polypeptide chain. Therefore, the identification of such proteins with moonlighting predicted functions can contribute to a better understanding of the molecular mechanisms unleashed by live BCG Moreau RDJ vaccine components. Introduction Tuberculosis (TB) is one of the 10 major causes of death worldwide. According to the World Health Organization (WHO), TB killed 1.7 million people in 2016 with 10.4 million new cases estimated worldwide ratifying the need for more effective treatment and prevention (1). To date, Bacillus Calmette-Guérin (BCG) is the only widely used prophylactic measure against TB (1). BCG is an attenuated Mycobacterium bovis strain obtained at the beginning of the Twentieth century at the Pasteur Institute, in Lille. It wa...
Source: Frontiers in Immunology - Category: Allergy & Immunology Source Type: research

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