is a causative agent for pulmonary infection and meningoencephalitis. Understanding the host's response to infection is critical for developing effective treatment. Even though some have elucidated the host response at the transcriptome level, little is known about how it modulates its defense machinery through the proteome mechanism or how protein posttranslational modification responds to the infection. In this work, we employed a murine infection model and mass spectrometry to systematically determine the proteome and acetylome statuses of lungs and brains in the early stage of infection. To extensively analyze the host response, we integrated the proteome data to the transcriptome results. Critical genes, including genes involved in phagosome, lysosome, and platelet activation are significantly altered in protein and gene expression during infection. In the acetylome analysis, we demonstrated that lung and brain tissues differentially regulate protein acetylation during infection. The three primary groups of proteins altered in acetylation status are histones, proteins involved in glucose and fatty acid metabolism, and proteins from the immune system. These analyses provide an integrative regulation network of the host responding to and shed new light on understanding the host's regulation mechanism when responding to .
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http://dx.doi.org/10.3389/fmicb.2020.00575 | DOI Listing |
PLoS One
December 2024
Research Group Energy Metabolism and Epigenetics, Research Institute for Farm Animal Biology (FBN), Dummerstorf, Germany.
Butyrate has been proposed as a drug therapy by acting as a lysine deacetylase (KDAC) inhibitor and elevating protein acetylation, in particular on histones. Nonetheless, recent studies suggest that tissues such as the gut can utilize butyrate as a metabolite. We have previously shown that the addition of butyrate induces a rapid increase of oxygen consumption in whole Drosophila melanogaster heads.
View Article and Find Full Text PDFJ Proteome Res
January 2025
College of Life Sciences and Shandong Engineering Research Center of Plant-Microbial Restoration for Saline-Alkali Land, Shandong Agricultural University, Tai'an 271018, China.
Int J Biol Macromol
December 2024
Department of Nuclear Medicine, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, China; College of Medicine and Biological Information Engineering, Northeastern University, Shenyang, Liaoning 110167, China. Electronic address:
Elucidation of post-translational modifications (PTMs), such as lysine acetylation (Kac), is crucial for understanding protein function and regulation. Although traditional experimental methods for identifying Kac sites are accurate, they are time-consuming and costly, leading to incomplete acetylome mapping. Computational approaches, particularly those incorporating machine learning, offer a rapid alternative, but face challenges owing to dataset imbalance, limited feature space, and the need for more effective feature-selection algorithms.
View Article and Find Full Text PDFMicrolife
September 2024
Laboratory of Gene Technology, Department of Biosystems, KU Leuven, Kasteelpark Arenberg 21 box 2462, 3001 Heverlee, Belgium.
Bacteria employ a myriad of regulatory mechanisms to adapt to the continuously changing environments that they face. They can, for example, use post-translational modifications, such as Nε-lysine acetylation, to alter enzyme activity. Although a lot of progress has been made, the extent and role of lysine acetylation in many bacterial strains remains uncharted.
View Article and Find Full Text PDFCommun Biol
October 2024
Aix Marseille Univ, INSERM, Marseille Medical Genetics, Marseille, France.
Rubinstein-Taybi syndrome (RTS) is a rare and severe genetic developmental disorder characterized by multiple congenital anomalies and intellectual disability. CREBBP and EP300, the two genes known to cause RTS encode transcriptional coactivators with a catalytic lysine acetyltransferase (KAT) activity. Loss of CBP or p300 function results in a deficit in protein acetylation, in particular at histones.
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