A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics

Protein Sci. 2018 Feb;27(2):369-380. doi: 10.1002/pro.3346. Epub 2017 Dec 27.

Abstract

Adherence, colonization, and survival of mycobacteria in host cells require surface adhesins, which are attractive pharmacotherapeutic targets. A large arsenal of pilus and non-pilus adhesins have been identified in mycobacteria. These adhesins are capable of interacting with host cells, including macrophages and epithelial cells and are essential to microbial pathogenesis. In the last decade, several structures of mycobacterial adhesins responsible for adhesion to either macrophages or extra cellular matrix proteins have been elucidated. In addition, key structural and functional information have emerged for the process of mycobacterial adhesion to epithelial cells, mediated by the Heparin-binding hemagglutinin (HBHA). In this review, we provide an overview of the structural and functional features of mycobacterial adhesins and discuss their role as important biomarkers for diagnostics and therapeutics. Based on the reported data, it appears clear that adhesins are endowed with a variety of different structures and functions. Most adhesins play important roles in the cell life of mycobacteria and are key virulence factors. However, they have adapted to an extracellular life to exert a role in host-pathogen interaction. The type of interactions they form with the host and the adhesin regions involved in binding is partly known and is described in this review.

Keywords: adhesion; biomarker; host-pathogen; protein structure.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / classification
  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / metabolism
  • Bacterial Adhesion
  • Binding Sites
  • Biomarkers / chemistry
  • Biomarkers / metabolism
  • Host-Pathogen Interactions*
  • Humans
  • Lectins / chemistry*
  • Lectins / genetics
  • Lectins / metabolism
  • Lung / metabolism
  • Lung / microbiology
  • Lung / pathology
  • Macrophages, Alveolar / metabolism
  • Macrophages, Alveolar / microbiology*
  • Macrophages, Alveolar / pathology
  • Models, Molecular
  • Mycobacterium tuberculosis / chemistry*
  • Mycobacterium tuberculosis / genetics
  • Mycobacterium tuberculosis / metabolism
  • Mycobacterium tuberculosis / pathogenicity
  • Protein Binding
  • Protein Structure, Secondary
  • Respiratory Mucosa / metabolism
  • Respiratory Mucosa / microbiology
  • Respiratory Mucosa / pathology
  • Tuberculosis, Pulmonary / metabolism
  • Tuberculosis, Pulmonary / microbiology
  • Tuberculosis, Pulmonary / pathology
  • Virulence Factors / chemistry*
  • Virulence Factors / classification
  • Virulence Factors / genetics
  • Virulence Factors / metabolism

Substances

  • Adhesins, Bacterial
  • Biomarkers
  • Lectins
  • Virulence Factors
  • heparin-binding hemagglutinin