Novel Mutations in MPT64 Secretory Protein of Mycobacterium tuberculosis Complex

Noor Muhammad, Muhammad Tahir Khan, Sajid Ali, Taj Ali Khan, Anwar Sheed Khan, Nadeem Ullah, Hassan Higazi (), Sara Ali, Salma Mohamed and Muhammad Qasim ()
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Noor Muhammad: Department of Microbiology, Kohat University of Science and Technology, Kohat 26000, Pakistan
Muhammad Tahir Khan: Zhongjing Research and Industrialization Institute of Chinese Medicine, Zhongguancun Scientific Park, Meixi, Nanyang 473006, China
Sajid Ali: Department of Microbiology & Biotechnology, Bacha Khan University, Charsadda 24550, Pakistan
Taj Ali Khan: Institute of Basic Medical Sciences, Khyber Medical University, Peshawar 25100, Pakistan
Anwar Sheed Khan: Department of Microbiology, Kohat University of Science and Technology, Kohat 26000, Pakistan
Nadeem Ullah: Department of Clinical Microbiology, Umeå University, 90185 Umeå, Sweden
Hassan Higazi: Department of Medical Laboratory Sciences, College of Health Sciences, Gulf Medical University, Ajman P.O. Box 4184, United Arab Emirates
Sara Ali: Department of Medical Laboratory Sciences, College of Health Sciences, Gulf Medical University, Ajman P.O. Box 4184, United Arab Emirates
Salma Mohamed: Department of Medical Laboratory Sciences, College of Health Sciences, Gulf Medical University, Ajman P.O. Box 4184, United Arab Emirates
Muhammad Qasim: Department of Microbiology, Kohat University of Science and Technology, Kohat 26000, Pakistan

IJERPH, 2023, vol. 20, issue 3, 1-11

Abstract: Tuberculosis (TB) is a global health problem caused by the Mycobacterium tuberculosis complex (MTBC). These bacteria secrete various proteins involved in the pathogenesis and persistence of MTBC. Among the secretory proteins, MPT64 (Rv1980C) is highly conserved and is also known as a major culture filtrate that is used in rapid diagnosis of MTBC. In the current study, we aimed to find the mutation in this highly conserved protein in isolates from the Pashtun-dominant province of Pakistan. We analyzed 470 M. tuberculosis whole-genome sequences of Khyber Pakhtunkhwa Province. Mutations in the MPT64 gene were screened through TB-Profiler and BioEdit software tools. The DynaMut web server was used to analyze the impact of the mutation on protein dynamics and stability. Among 470 MTB genomes, three non-synonymous mutations were detected in nine isolates, and one synonymous mutation (G208A) was found in four isolates. Mutation G211T (F159L), which was detected at the C-terminal domain of the protein in six isolates, was the most prominent. The second novel mutation, T480C (I70V), was detected in two isolates at the C-terminal side of the protein structure. The third novel mutation, A491C (L66R), was detected in a single isolate at the N-terminal side of the MPT64 protein. The effect of these three mutations was destabilizing on the protein structure. The molecular flexibility of the first two mutations increased, and the last one decreased. MPT64 is a highly conserved secretory protein, harboring only a few mutations. This study provides useful information for better managing the diagnosis of MTB isolates in high TB-burden countries.

Keywords: MPT64; mutations; diagnosis; genomes; mycobacterium; tuberculosis (search for similar items in EconPapers)
JEL-codes: I I1 I3 Q Q5 (search for similar items in EconPapers)
Date: 2023
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