Статья

Phylogenetically defined isoforms of listeria monocytogenes invasion factor InlB Differently activate intracellular signaling pathways and interact with the receptor gC1q-R

Y. Chalenko, E. Kalinin, V. Marchenkov, E. Sysolyatina, A. Surin, K. Sobyanin, S. Ermolaeva,
2021

The pathogenic Gram-positive bacterium Listeria monocytogenes has been evolving into a few phylogenetic lineages. Phylogenetically defined substitutions were described in the L. monocytogenes virulence factor InlB, which mediates active invasion into mammalian cells via interactions with surface receptors c-Met and gC1q-R. InlB internalin domain (idInlB) is central to interactions with c-Met. Here we compared activity of purified recombinant idInlB isoforms characteristic for L. monocytogenes phylogenetic lineage I and II. Size exclusion chromatography and intrinsic fluorescence were used to characterize idInlBs. Western blotting was used to study activation of c-Met-dependent MAPK- and PI3K/Akt-pathways. Solid-phase microplate binding and competition assay was used to quantify interactions with gCq1-R. Isogenic recombinant L. monocytogenes strains were used to elucidate the input of idInlB isoforms in HEp-2 cell invasion. Physicochemical parameters of idInlB isoforms were similar but not identical. Kinetics of Erk1/2 and Akt phosphorylation in response to purified idInlBs was lineage specific. Lineage I but not lineage II idInlB specifically bound gC1q-R. Antibody against gC1q-R amino acids 221-249 inhibited invasion of L. monocytogenes carrying lineage I but not lineage II idInlB. Taken together, obtained results suggested that phylogenetically defined substitutions in idInlB provide functional distinctions and might be involved in phylogenetically determined differences in virulence potential. © 2019 by the authors. Licensee MDPI, Basel, Switzerland.

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  • 1. Version of Record от 2021-04-27

Метаданные

Об авторах
  • Y. Chalenko
    Laboratory of Ecology of Pathogenic Bacteria, Gamaleya Research Center of Epidemiology and Microbiology, Moscow, 123098, Russian Federation
  • E. Kalinin
    Laboratory of Molecular Microbiology, Nizhny Novgorod Research Veterinary Institute, Branch of Federal Research Center For Virology And Microbiology, Nizhny Novgorod, 603022, Russian Federation
  • V. Marchenkov
    Laboratory of Protein Physics, Institute for Protein Research RAS, Puschino, 142290, Russian Federation
  • E. Sysolyatina
    Laboratory of Active Media, Moscow Institute of Physics and Technology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Dolgoprudnyi, 141701, Russian Federation
  • A. Surin
    Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Pushchino, 142290, Russian Federation
  • K. Sobyanin
  • S. Ermolaeva
Название журнала
  • International Journal of Molecular Sciences
Том
  • 20
Выпуск
  • 17
Страницы
  • -
Ключевые слова
  • binding protein; gc1 qr; gentamicin; invasion factor inib; unclassified drug; virulence factor; bacterial protein; C1QBP protein, human; carrier protein; inlB protein, Listeria monocytogenes; isoprotein; membrane protein; mitochondrial protein; mitogen activated protein kinase; phosphatidylinositol 3 kinase; protein binding; virulence factor; Article; bacterial virulence; cell invasion; cell invasion assay; competitive binding assay; controlled study; enzyme linked immunosorbent assay; fluorescence; gene expression; HEp-2 cell line; human; human cell; Listeria monocytogenes; MAPK signaling; nonhuman; phosphorylation; phylogeny; physical chemistry; protein purification; signal transduction; size exclusion chromatography; Western blotting; amino acid sequence; cell line; chemistry; classification; genetics; Listeria monocytogenes; metabolism; pathogenicity; physiology; protein domain; Amino Acid Sequence; Bacterial Proteins; Carrier Proteins; Cell Line; Humans; Listeria monocytogenes; Membrane Proteins; Mitochondrial Proteins; Mitogen-Activated Protein Kinases; Phosphatidylinositol 3-Kinases; Phylogeny; Protein Binding; Protein Interaction Domains and Motifs; Protein Isoforms; Signal Transduction; Virulence Factors
Издатель
  • MDPI AG
Тип документа
  • journal article
Тип лицензии Creative Commons
  • CC
Правовой статус документа
  • Свободная лицензия
Источник
  • scopus