Development of a rapid and sensitive DNA turbidity biosensor test for diagnosis of katG gene in isoniazid resistant Mycobacterium tuberculosis

2017 ◽  
Author(s):  
Jutturong Ckumdee ◽  
Somchai Santiwatanakul ◽  
Thongchai Kaewphinit
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Katg Gene

scholarly journals Direct detection of rpoB and katG gene mutations of Mycobacterium tuberculosis in clinical samples

2017 ◽  
Vol 7 (8) ◽  
pp. 698-701
Author(s):  
Sunil Pandey ◽  
Ashima Lamichhane ◽  
Anu Byanjankar ◽  
Ansuma Kharel ◽  
Chandrakala Rai ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Direct Detection ◽  
Gene Mutations ◽  
Clinical Samples ◽  
Katg Gene

scholarly journals Presence of katG gene in resistant Mycobacterium tuberculosis.

1996 ◽  
Vol 49 (11) ◽  
pp. 945-947 ◽  
Author(s):  
M Jaber ◽  
A Rattan ◽  
R Kumar
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Katg Gene

Novel mutations in katG gene of a clinical isolate of isoniazid-resistant Mycobacterium tuberculosis

Biologia ◽  
2012 ◽  
Vol 67 (1) ◽  
Author(s):  
Purkan ◽  
Ihsanawati ◽  
Yana Syah ◽  
Debbie Retnoningrum ◽  
Achmad Noer ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Clinical Isolate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Intramolecular Interactions ◽  
Wild Type ◽  
Katg Gene ◽  
Gene Encoding ◽  
Oxidation Activity ◽  
Catalase Peroxidase

AbstractMost of isoniazid-resistant Mycobacterium tuberculosis evolved due to mutation in the katG gene encoding catalase-peroxidase. A set of new mutations, namely T1310C, G1388T, G1481A, T1553C, and A1660G, which correspond to amino acid substitutions of L437P, R463L, G494D, I518T, and K554E, in the katG gene of the L10 clinical isolate M. tuberculosis was identified. The wild-type and mutant KatG proteins were expressed in Escherichia coli BL21(DE3) as a protein of 80 kDa based on sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis. The mutant KatG protein exhibited catalase and peroxidase activities of 4.6% and 24.8% toward its wild type, respectively, and retained 19.4% isoniazid oxidation activity. The structure modelling study revealed that these C-terminal mutations might have induced formation of a new turn, perturbing the active site environment and also generated new intramolecular interactions, which could be unfavourable for the enzyme activities.

scholarly journals Lack of Clinical Significance for the Common Arginine‐to‐Leucine Substitution at Codon 463 of the katG Gene in Isoniazid‐Resistant Mycobacterium tuberculosis in Singapore

1997 ◽  
Vol 176 (4) ◽  
pp. 1125-1126 ◽  
Author(s):  
Ann Siew‐Gek Lee ◽  
Lynn Lay‐Hoon Tang ◽  
Irene Hua‐Khim Lim ◽  
Moi‐Lin Ling ◽  
Leng Tay ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Clinical Significance ◽  
Katg Gene ◽  
The Common

scholarly journals DETECTION OF MUTATIONS IN THE KatG GENE RELATED TO ISONIAZID RESISTANCE OF MYCOBACTERIUM TUBERCULOSIS COLLECTED IN CENTRAL AND SOUTH VIETNAM

2018 ◽  
Vol 16 (2) ◽  
pp. 353-360
Author(s):  
Nghiem Minh Ngoc ◽  
Nguyen Thi Hoai Thu
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Multi Drug Resistance ◽  
Katg Gene ◽  
Isoniazid Resistance ◽  
South Vietnam ◽  
Substitution Mutations ◽  
Detection Of Mutations ◽  
And Control ◽  
Common Infections

Infection of Mycobacterium tuberculosis (MTB) is one of the most common infections in humans. However, the detection rate is only 37% of estimated patients. Currently, Tuberculosic bacteria (TB) are becoming more serious with many TB strains developing multi-drug resistance, and particularly, in case of co-infection with TB and HIV/AIDS. The izoniazid resistant TB strains (INH) also resistant to the other anti-TB antibiotics. The molecular biology methods have allowed rapid and accurate diagnosis of patients infected with drug-resistant TB bacteria. In this study, we used primers katG-F and katG-R designed for amplication of a fragment of 684 bp in katG gene in 7 strains of TB bacteria collected in Pham Ngoc Thach - Ho Chi Minh city and Hue Central hospitals. Sequence analysis of the katG gene fragments showed that 5 samples had substitution mutations at codon 315 (point mutation G to C), leading to the change of amino acid from Serine to Threonine (S315T). In the 5th sample there appeared another mutation at codon 324, changing amino acid Aspartic (D) to Glycine (G) (D324G). In the sample DA1, no mutation has been found in any codon in the katG gene fragment studied. The results obtained in this study may have important implications in changing the treatment regimen and control of tuberculosis in a country with high number of TB patients as in Vietnam.

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