Proteomics

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Identification of pspA-3’UTR-regulated proteins by quantitative proteomics

ABSTRACT: RNA-mediated control of virulence gene expression is widespread among pathogenic bacteria. However, in some major human pathogens such as Streptococcus pneumoniae, its role remains poorly understood. In this study we identify a regulatory function for the 3’-untranslated region (3’UTR) of the mRNA encoding the pneumococcal surface protein A (PspA), a multifunctional surface protein and major virulence factor. Using quantitative proteomics, we identify the protein chaperone Caseinolytic protease L (ClpL) as a regulatory target of the pspA-3’UTR. Downstream analysis reveals that the pspA-3’UTR represses ClpL expression in a temperature-dependent manner. Altogether, this study unveils a riboregulatory role for the pspA mRNA, revealing another layer of PspA-mediated virulence in the human pathogen S. pneumoniae.

INSTRUMENT(S):

ORGANISM(S): Streptococcus Pneumoniae Serotype 2 (strain D39 / Nctc 7466)

SUBMITTER: Jens Pettersen  

LAB HEAD: Mikkel Girke Jørgensen

PROVIDER: PXD040356 | Pride | 2026-05-27

REPOSITORIES: Pride

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Publications

3' UTR-mediated regulation of a protein chaperone by the pspA mRNA in Streptococcus pneumoniae.

Pettersen Jens S JS   Lund Anette A   Kirpekar Finn F   Hansen Nikolaj V NV   Svenningsen Sine L SL   Paton James C JC   Møller-Jensen Jakob J   Jørgensen Mikkel G MG  

Nucleic acids research 20260501 9

RNA-mediated control of virulence gene expression plays a crucial role in many pathogenic bacteria. However, our understanding of these processes in Streptococcus pneumoniae, a major human pathogen, remains limited. Here we discover a novel regulatory element located in the 3'-untranslated region (3' UTR) of the mRNA encoding a major pneumococcal virulence factor, pneumococcal surface protein A (PspA). Quantitative proteomics and western blot analysis reveal that this 3' UTR acts as a trans-acti  ...[more]

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