Synthesis and structural insight into ESX-1 Substrate Protein C, an immunodominant Mycobacterium tuberculosis-secreted antigen

Biopolymers. 2016 May;106(3):267-74. doi: 10.1002/bip.22838.


Tuberculosis, the second leading cause of death from a single infectious agent, is recognized as a major threat to human health due to a lack of practicable vaccines against the disease and the widespread occurrence of drug resistance. With a pressing need for a novel protein target as a platform for new vaccine development, ESX-1 Substrate Protein C (EspC) was recently identified as a novel Mycobacterium tuberculosis-secreted antigen that is as immunodominant as the two specific immunodiagnostic T-cell antigens, CFP-10 and ESAT-6. Here, we present the first chemical total synthesis, folding conditions, and circular dichroism data of EspC. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 267-274, 2016.

Keywords: SPPS; antigen; mycobacterium tuberculosis; native chemical ligation.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Bacterial / chemistry*
  • Antigens, Bacterial / genetics
  • Antigens, Bacterial / immunology
  • Antigens, Differentiation, T-Lymphocyte / chemistry
  • Antigens, Differentiation, T-Lymphocyte / immunology
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / immunology
  • Gene Expression
  • Humans
  • Mycobacterium tuberculosis / chemistry*
  • Mycobacterium tuberculosis / immunology
  • Peptides / chemical synthesis*
  • Peptides / immunology
  • Protein Folding
  • Protein Structure, Secondary
  • Solutions
  • Type VII Secretion Systems / genetics


  • Antigens, Bacterial
  • Antigens, Differentiation, T-Lymphocyte
  • Bacterial Proteins
  • ESAT-6 protein, Mycobacterium tuberculosis
  • Peptides
  • Solutions
  • Type VII Secretion Systems