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Lmo0171, a novel internalin-like protein, determines cell morphology of Listeria monocytogenes and its ability to invade human cell lines.

ABSTRACT: Internalins comprise a class of Listeria monocytogenes proteins responsible for activation of signalling pathways leading to phagocytic uptake of the bacterium by the host cell. In this paper, a possible role of Lmo0171-a new member of the internalin family was investigated. Disruption of the lmo0171 gene resulted in important cell morphology alterations along with a decrease in the ability to invade three eukaryotic cell lines, that is Int407, Hep-2 and HeLa and diminished adhesion efficiency to int407, thereby suggesting bifunctionality of the newly characterised Lmo0171 internalin.

SUBMITTER: Stachowiak R

PROVIDER: S-EPMC4293459 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Lmo0171, a novel internalin-like protein, determines cell morphology of Listeria monocytogenes and its ability to invade human cell lines.

Stachowiak Radosław R Jagielski Tomasz T Roeske Katarzyna K Osińska Olga O Gunerka Paweł P Wiśniewski Jarosław J Bielecki Jacek J

Current microbiology 20141017 2

Internalins comprise a class of Listeria monocytogenes proteins responsible for activation of signalling pathways leading to phagocytic uptake of the bacterium by the host cell. In this paper, a possible role of Lmo0171-a new member of the internalin family was investigated. Disruption of the lmo0171 gene resulted in important cell morphology alterations along with a decrease in the ability to invade three eukaryotic cell lines, that is Int407, Hep-2 and HeLa and diminished adhesion efficiency t ...[more]

PMID: 25323012

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Project description:Hepatocyte growth factor (HGF) is critical for tissue homeostasis and repair in many organs including the lung, heart, kidney, liver, nervous system, and skin. HGF is a heterodimeric protein containing 20 disulfide bonds distributed among an amino-terminal hairpin, four kringle domains, and a serine protease-like domain. Due to its complex structure, recombinant production of HGF in prokaryotes requires denaturation and refolding, processes that are impractical for large-scale manufacture. Thus, pharmaceutical quantities of HGF are not available despite its potential applications. A fragment of the Listeria monocytogenes internalin B protein from amino acids 36-321 (InlB₃₆₋₃₂₁) was demonstrated to bind to and partially activate the HGF receptor Met. InlB₃₆₋₃₂₁ has a stable β-sheet structure and is easily produced in its native conformation by Escherichia coli. We cloned InlB₃₆₋₃₂₁ (1×InlB₃₆₋₃₂₁) and engineered a head-to-tail repeat of InlB₃₆₋₃₂₁ with a linker peptide (2×InlB₃₆₋₃₂₁); 1×InlB₃₆₋₃₂₁ and 2×InlB₃₆₋₃₂₁ were purified from E. coli. Both 1× and 2×InlB₃₆₋₃₂₁ activated the Met tyrosine kinase. We subsequently compared signal transduction of the two proteins in primary lung endothelial cells. 2×InlB₃₆₋₃₂₁ activated ERK1/2, STAT3, and phosphatidylinositol 3-kinase/Akt pathways, whereas 1×InlB₃₆₋₃₂₁ activated only STAT3 and ERK1/2. The 2×InlB₃₆₋₃₂₁ promoted improved motility compared with 1×InlB₃₆₋₃₂₁ and additionally stimulated proliferation equivalent to full-length HGF. Both the 1× and 2×InlB₃₆₋₃₂₁ prevented apoptosis by the profibrotic peptide angiotensin II in cell culture and ex vivo lung slice cultures. The ease of large-scale production and capacity of 2×InlB₃₆₋₃₂₁ to mimic HGF make it a potential candidate as a pharmaceutical agent for tissue repair.

Dataset Information

Lmo0171, a novel internalin-like protein, determines cell morphology of Listeria monocytogenes and its ability to invade human cell lines.

Publications

Lmo0171, a novel internalin-like protein, determines cell morphology of Listeria monocytogenes and its ability to invade human cell lines.

Similar Datasets

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