Phylogenetically Defined Isoforms of Listeria monocytogenes Invasion Factor InlB Differently Activate Intracellular Signaling Pathways and Interact with the Receptor gC1q-R

Autor: Alexey K. Surin, Svetlana Ermolaeva, Yaroslava Chalenko, Victor V. Marchenkov, Egor Kalinin, E. V. Sysolyatina, Konstantin A. Sobyanin
Jazyk: angličtina
Rok vydání: 2019
Předmět:
0301 basic medicine
gC1q-R
bacterial virulence factors
medicine.disease_cause
Virulence factor
law.invention
lcsh:Chemistry
Phosphatidylinositol 3-Kinases
law
Protein Isoforms
lcsh:QH301-705.5
mammalian surface receptors
Spectroscopy
Phylogeny
General Medicine
Computer Science Applications
Cell biology
Blot
host-parasite interactions
Recombinant DNA
Mitogen-Activated Protein Kinases
Protein Binding
Signal Transduction
Gene isoform
Lineage (genetic)
Listeria
Virulence Factors
030106 microbiology
Virulence
Biology
Catalysis
Article
Cell Line
Inorganic Chemistry
InlB
Mitochondrial Proteins
03 medical and health sciences
Listeria monocytogenes
Bacterial Proteins
evolution
medicine
Humans
Internalin
Protein Interaction Domains and Motifs
Amino Acid Sequence
Physical and Theoretical Chemistry
Molecular Biology
c-Met
Organic Chemistry
Membrane Proteins
virulence
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Carrier Proteins
Zdroj: International Journal of Molecular Sciences
Volume 20
Issue 17
International Journal of Molecular Sciences, Vol 20, Iss 17, p 4138 (2019)
ISSN: 1422-0067
Popis: 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&ndash
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.
Databáze: OpenAIRE
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