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Novel mutations in MPT64 secretory protein of Mycobacterium tuberculosis complex
Department of Microbiology, Kohat University of Science and Technology, Kohat, Pakistan.
Zhongjing Research and Industrialization, Institute of Chinese Medicine, Zhongguancun Scientific Park, Meixi, Nanyang, China; Institute of Molecular Biology and Biotechnology (IMBB), The University of Lahore, KM Defense Road, Lahore, Pakistan.
Department of Microbiology & Biotechnology, Bacha Khan University, Charsadda, Pakistan.
Institute of Basic Medical Sciences, Khyber Medical University, Peshawar, Pakistan.
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2023 (engelsk)Inngår i: International Journal of Environmental Research and Public Health, ISSN 1661-7827, E-ISSN 1660-4601, Vol. 20, nr 3, artikkel-id 2530Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
MDPI, 2023. Vol. 20, nr 3, artikkel-id 2530
Emneord [en]
diagnosis, genomes, MPT64, mutations, mycobacterium, tuberculosis
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-205013DOI: 10.3390/ijerph20032530PubMedID: 36767896Scopus ID: 2-s2.0-85147872166OAI: oai:DiVA.org:umu-205013DiVA, id: diva2:1738678
Tilgjengelig fra: 2023-02-22 Laget: 2023-02-22 Sist oppdatert: 2023-02-22bibliografisk kontrollert

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