Umeå University's logo

umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
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.
Show others and affiliations
2023 (English)In: International Journal of Environmental Research and Public Health, ISSN 1661-7827, E-ISSN 1660-4601, Vol. 20, no 3, article id 2530Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
MDPI, 2023. Vol. 20, no 3, article id 2530
Keywords [en]
diagnosis, genomes, MPT64, mutations, mycobacterium, tuberculosis
National Category
Medical Genetics
Identifiers
URN: urn:nbn:se:umu:diva-205013DOI: 10.3390/ijerph20032530PubMedID: 36767896Scopus ID: 2-s2.0-85147872166OAI: oai:DiVA.org:umu-205013DiVA, id: diva2:1738678
Available from: 2023-02-22 Created: 2023-02-22 Last updated: 2023-02-22Bibliographically approved

Open Access in DiVA

fulltext(1748 kB)118 downloads
File information
File name FULLTEXT01.pdfFile size 1748 kBChecksum SHA-512
01822245943b61cd727c29ce7a9f5ea4d926c72303d16d10c7584f3787d2b8c302d778b5b5a996b79e357770ad57e8fda9d6380993bb73073ffd1ca9ab7cd200
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMedScopus

Authority records

Ullah, Nadeem

Search in DiVA

By author/editor
Ullah, Nadeem
By organisation
Department of Clinical Microbiology
In the same journal
International Journal of Environmental Research and Public Health
Medical Genetics

Search outside of DiVA

GoogleGoogle Scholar
Total: 118 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 180 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf