Publications by authors named "Alemayehu Godana Birhanu"

Article Synopsis
  • Human macrophages produce reactive nitrogen species in response to Mycobacterium tuberculosis infection, which causes stress in the bacteria and affects protein modifications.
  • Researchers analyzed the acylation of Mtb proteins after exposure to low levels of nitric oxide, identifying 6,437 acylation events in 1,496 proteins, predominantly O-acylation.
  • The study highlights how protein acylation may influence Mtb's responses to stress and antimicrobial resistance, marking the first comprehensive profiling of Mtb's acylation due to nitrosative stress, which could inform global health strategies.
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The emergence and spread of antibiotic resistance (ABR) have been a public health challenge globally. The burden is even higher in low-income countries where there is a lack of appropriate healthcare systems, and inappropriate antibiotic disposal practices and utilization. Due to poor solid waste disposal practices in developing nations, municipal solid waste dumpsite (MSWDS) can be a reservoir for ABR bacteria.

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Antimicrobial resistance (AMR) represents a major threat to global health. Infection caused by Methicillin-resistant (MRSA) is one of the well-recognized global public health problem globally. In some regions, as many as 90% of infections are reported to be MRSA, which cannot be treated with standard antibiotics.

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Mass spectrometry (MS)-based proteomics have been increasingly implemented in various disciplines of laboratory medicine to identify and quantify biomolecules in a variety of biological specimens. MS-based proteomics is continuously expanding and widely applied in biomarker discovery for early detection, prognosis and markers for treatment response prediction and monitoring. Furthermore, making these advanced tests more accessible and affordable will have the greatest healthcare benefit.

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Reactive nitrogen species (RNS) are secreted by human cells in response to infection by (Mtb). Although RNS can kill Mtb under some circumstances, Mtb can adapt and survive in the presence of RNS by a process that involves modulation of gene expression. Previous studies focused primarily on stress-related changes in the Mtb transcriptome.

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Despite the discovery of the tubercle bacillus more than 130 years ago, its physiology and the mechanisms of virulence are still not fully understood. A comprehensive analysis of the proteomes of members of the human-adapted complex (MTBC) lineages 3, 4, 5, and 7 was conducted to better understand the evolution of virulence and other physiological characteristics. Unique and shared proteomic signatures in these modern, pre-modern and ancient MTBC lineages, as deduced from quantitative bioinformatics analyses of high-resolution mass spectrometry data, were delineated.

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Multiple regulatory mechanisms including post-translational modifications (PTMs) confer complexity to the simpler genomes and proteomes of Mycobacterium tuberculosis (Mtb). PTMs such as glycosylation play a significant role in Mtb adaptive processes. The glycoproteomic patterns of clinical isolates of the Mycobacterium tuberculosis complex (MTBC) representing the lineages 3, 4, 5 and 7 were characterized by mass spectrometry.

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Increasing evidence demonstrates that lysine acetylation is involved in Mycobacterium tuberculosis (Mtb) virulence and pathogenesis. However, previous investigations in Mtb have only monitored acetylation at lysine residues using selected reference strains. We analyzed the global N- and O-acetylation of three Mtb isolates: two lineage 7 clinical isolates and the lineage 4 H37Rv reference strain.

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