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Characterization of differential pore‐forming activities of ESAT‐6 proteins from Mycobacterium tuberculosis and Mycobacterium smegmatis
Author(s) -
Peng Xiuli,
Jiang Guozhong,
Liu Wei,
Zhang Qi,
Qian Wei,
Sun Jianjun
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12072
Subject(s) - mycobacterium smegmatis , mycobacterium tuberculosis , esat 6 , microbiology and biotechnology , mycobacterium , chemistry , bacterial protein , tuberculosis , bacteria , biology , biochemistry , medicine , gene , genetics , pathology
Mycobacterium tuberculosis ESAT‐6 (MtbESAT‐6) plays essential roles in pathogenesis. MtbESAT‐6 exhibits a unique pore‐forming activity (PFA) that is not found in its ortholog from non‐pathogenic Mycobacterium smegmatis (MsESAT‐6). Here, we characterized the differential PFAs and found that exchange of I25‐H26/T25‐A26 between two proteins reciprocally affected their PFAs. MtbESAT‐6(IH/TA) had ~ 40% reduction, while MsESAT‐6(TA/IH) fully acquired its activity similar to MtbESAT‐6. Mutations of A17E, K38T, N67L or R74Q on MtbESAT‐6(IH/TA) further reduced the activity, with MtbESAT‐6(IH/TA‐17) being the lowest. This study suggests I25‐H26 as the pH‐sensor essential for MsESAT‐6 to fully acquire the activity, while multiple residues contributed to MtbESAT‐6 PFA.