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Henri Monteil

Researcher at University of Strasbourg

Publications -  138
Citations -  4812

Henri Monteil is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Antibacterial agent & High-performance liquid chromatography. The author has an hindex of 37, co-authored 137 publications receiving 4657 citations.

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Regulation of virulence determinants in Staphylococcus aureus: complexity and applications.

TL;DR: The virulence of Staphylococcus aureus is essentially determined by cell wall associated proteins and secreted toxins that are regulated and expressed according to growth phases and/or growth conditions.
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Panton-Valentine leucocidin and gamma-hemolysin from Staphylococcus aureus ATCC 49775 are encoded by distinct genetic loci and have different biological activities.

TL;DR: The cosecretion of these five proteins led to six possible synergistic combinations between F and S components, two of which had dermonecrotic activity on rabbit skin, and all six were leukocytolytic on glass-adsorbed leukocytes.
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Epidemiological data on Staphylococcus aureus strains producing synergohymenotropic toxins

TL;DR: DNA hybridisation of 309 consecutive Staphylococcus aureus clinical isolates with oligonucleotide probes specific for genes encoding Panton-Valentine leucocidin (luk-PV) and gamma-haemolysin (hlg) revealed that 99% of randomly selected strains carried the hlg locus whereas only 2% harboured the luk-pV as well as the hLg loci.
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Characterization of a novel structural member, LukE-LukD, of the bi-component staphylococcal leucotoxins family.

TL;DR: LukE+LukD was as effective as the Panton‐Valentine leucocidin for inducing dermonecrosis when injected in the rabbit skin, but not hemolytic and poorlyLeucotoxic compared to other leucotoxins expressed by Staphylococcus aureus.
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Ion channels and bacterial infection: the case of β-barrel pore-forming protein toxins of Staphylococcus aureus

TL;DR: X‐ray crystallography of the α‐hemolysin pore has shown it is a mushroom‐shaped, hollow heptamer, almost entirely consisting of β‐structure, and γ‐Hemolysin pores seem to be organized as α‐ Hemolysin, but should contain an even number of each component, alternating in a 1:1 stoichiometry.