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Synthesis and structural insight into ESX‐1 Substrate Protein C, an immunodominant Mycobacterium tuberculosis‐ secreted antigen
Author(s) -
Son Soo Jung,
Harris Paul W. R.,
Squire Chris J.,
Baker Edward N.,
Brimble Margaret A.
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22838
Subject(s) - mycobacterium tuberculosis , antigen , tuberculosis , chemistry , microbiology and biotechnology , mycobacterium , virology , biology , immunology , medicine , pathology
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.
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