Specific interaction between mycobacterium tuberculosis lipoprotein-derived peptides and target cells inhibits Mycobacterial entry in vitro Academic Article


  • © 2014 John Wiley & Sons A/S.Tuberculosis (TB) continues being one of the diseases having the greatest mortality rates around the world, 8.7 million cases having been reported in 2011. An efficient vaccine against TB having a great impact on public health is an urgent need. Usually, selecting antigens for vaccines has been based on proteins having immunogenic properties for patients suffering TB and having had promising results in mice and non-human primates. Our approach has been based on a functional approach involving the pathogen-host interaction in the search for antigens to be included in designing an efficient, minimal, subunit-based anti-TB vaccine. This means that Mycobacterium tuberculosis has mainly been involved in studies and that lipoproteins represent an important kind of protein on the cell envelope which can also contribute towards this pathogen's virulence. This study has assessed the expression of four lipoproteins from M. tuberculosis H37Rv, that is, Rv1411c (LprG), Rv1911c (LppC), Rv2270 (LppN) and Rv3763 (LpqH), and the possible biological activity of peptides derived from these. Five peptides were found for these proteins which had high specific binding to both alveolar A549 epithelial cells and U937 monocyte-derived macrophages which were able to significantly inhibit mycobacterial entry to these cells in vitro.

publication date

  • 2014/1/1


  • A549 Cells
  • Alveolar Epithelial Cells
  • Antigens
  • Bioactivity
  • Epithelial Cells
  • Host-Pathogen Interactions
  • In Vitro Techniques
  • Lipoproteins
  • Macrophages
  • Mortality
  • Mycobacterium tuberculosis
  • Nuclear Family
  • Pathogens
  • Peptides
  • Primates
  • Proteins
  • Public Health
  • Public health
  • Tuberculosis
  • Tuberculosis Vaccines
  • Vaccines
  • Virulence

International Standard Serial Number (ISSN)

  • 1747-0277

number of pages

  • 16

start page

  • 626

end page

  • 641