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Protease S of entomopathogenic bacterium Photorhabdus laumondii: expression, purification and effect on greater wax moth Galleria mellonella

Svetlova, Anastasia O. ; Karaseva, Maria A. ; Berdyshev, Igor M. ; Chukhontseva, Ksenia N. ; Pobeguts, Olga V. ; Galyamina, Maria A. ; Smirnov, Igor P. ; Polyakov, Nikita B. ; Zavialova, Maria G. ; Kostrov, Sergey V. ; Demidyuk, Ilya V.

Molecular biology reports, 2024-12, Vol.51 (1), p.713, Article 713 [Periódico revisado por pares]

Dordrecht: Springer Netherlands

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Título:
Protease S of entomopathogenic bacterium Photorhabdus laumondii: expression, purification and effect on greater wax moth Galleria mellonella
Autor: Svetlova, Anastasia O. ; Karaseva, Maria A. ; Berdyshev, Igor M. ; Chukhontseva, Ksenia N. ; Pobeguts, Olga V. ; Galyamina, Maria A. ; Smirnov, Igor P. ; Polyakov, Nikita B. ; Zavialova, Maria G. ; Kostrov, Sergey V. ; Demidyuk, Ilya V.
Assuntos: Animal Anatomy ; Animal Biochemistry ; Animals ; Bacteria ; Bacterial infections ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biomedical and Life Sciences ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Galleria mellonella ; Hemolymph ; Hemolymph - metabolism ; Histology ; Immune response ; Life Sciences ; Morphology ; Moths - microbiology ; Original Article ; Peptide Hydrolases - metabolism ; Photorhabdus ; Proteinase ; Proteomics ; Proteomics - methods ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Toxicity
É parte de: Molecular biology reports, 2024-12, Vol.51 (1), p.713, Article 713
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SourceType-Scholarly Journals-1
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Descrição: Background Protease S (PrtS) from Photorhabdus laumondii belongs to the group of protealysin-like proteases (PLPs), which are understudied factors thought to play a role in the interaction of bacteria with other organisms. Since P. laumondii is an insect pathogen and a nematode symbiont, the analysis of the biological functions of PLPs using the PrtS model provides novel data on diverse types of interactions between bacteria and hosts. Methods and results Recombinant PrtS was produced in Escherichia coli . Efficient inhibition of PrtS activity by photorin, a recently discovered emfourin-like protein inhibitor from P. laumondii , was demonstrated. The Galleria mellonella was utilized to examine the insect toxicity of PrtS and the impact of PrtS on hemolymph proteins in vitro. The insect toxicity of PrtS is reduced compared to protease homologues from non-pathogenic bacteria and is likely not essential for the infection process. However, using proteomic analysis, potential PrtS targets have been identified in the hemolymph. Conclusions The spectrum of identified proteins indicates that the function of PrtS is to modulate the insect immune response. Further studies of PLPs’ biological role in the PrtS and P. laumondii model must clarify the details of PrtS interaction with the insect immune system during bacterial infection.
Editor: Dordrecht: Springer Netherlands
Idioma: Inglês

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Protease S of entomopathogenic bacterium Photorhabdus laumondii: expression, purification and effect on greater wax moth Galleria mellonella

Svetlova, Anastasia O. ; Karaseva, Maria A. ; Berdyshev, Igor M. ; Chukhontseva, Ksenia N. ; Pobeguts, Olga V. ; Galyamina, Maria A. ; Smirnov, Igor P. ; Polyakov, Nikita B. ; Zavialova, Maria G. ; Kostrov, Sergey V. ; Demidyuk, Ilya V.

Dordrecht: Springer Netherlands

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