A novel peptide interferes with Mycobacterium tuberculosis virulence and survival

被引:2
|
作者
Samuchiwal, Sachin Kumar [1 ]
Tousif, Sultan [2 ,3 ,5 ]
Singh, Dhiraj Kumar [2 ]
Kumar, Arun [2 ]
Ghosh, Anamika [1 ]
Bhalla, Kuhulika [1 ]
Prakash, Prem [1 ]
Kumar, Sushil [1 ]
Trivedi, Ashish Chandra [4 ]
Bhattacharyya, Maitree [3 ]
Das, Gobardhan [5 ]
Ranganathan, Anand [1 ]
机构
[1] ICGEB, Recombinant Gene Prod Grp, Int Ctr Genet Engn & Biotechnol, New Delhi 110067, India
[2] ICGEB, Immunol Grp, Int Ctr Genet Engn & Biotechnol, New Delhi 110067, India
[3] Univ Calcutta, Dept Biochem, Kolkata 700019, India
[4] IMT Manesar, Innovat Life Discoveries Pvt Ltd, Manesar, Haryana, India
[5] Univ Kwazulu Natal, Sch Lab Med, Coll Hlth Sci, Durban, South Africa
来源
FEBS OPEN BIO | 2014年 / 4卷
关键词
Antimycobacterial peptides; ESAT6; Mycobacterium tuberculosis; Protein-protein interaction; ESAT-6-CFP-10; COMPLEX; ESAT-6; PROTEINS; PATHOGENESIS; GROWTH; CFP-10; BIND; BCG;
D O I
10.1016/j.fob.2014.08.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Tuberculosis (TB) is a huge global burden, with new and resistant strains emerging at an alarming rate, necessitating an urgent need for a new class of drug candidates. Here, we report that SL3, a novel 33-amino acid peptide, causes debilitating effects on mycobacterial morphology. Treatment with SL3 drastically inhibits the growth of Mycobacterium tuberculosis in vitro as well as in a pre-clinical mouse model for M.tb infection. Microarray analysis of SL3-expressing strain demonstrates wide-scale transcriptional disruption in M.tb. We therefore believe that SL3 and similar peptides may herald a new approach towards discovering new molecules for TB therapy. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:735 / 740
页数:6
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