Femoral Neuropathy Secondary to Compression by Spontaneous Iliac Hematoma.

Introduction: Femoral neuropathy is a rare condition typically resulting from compression of the femoral nerve. While it is commonly associated with anticoagulated patients due to psoas hematomas, spontaneous iliacus muscle hematomas without any evident trauma or coagulation disorders are exceedingly uncommon. This case report details the occurrence and management of a spontaneous iliacus muscle hematoma in an adolescent patient.

Remodulation of bacterial transcriptome after acquisition of foreign DNA: the case of -HPI high-pathogenicity island in .

The high-pathogenicity island -HPI is widespread in and encodes the siderophore piscibactin, as well as the regulator PbtA that is essential for its expression. In this work, we aim to study whether PbtA directly interacts with -HPI promoters. Furthermore, we hypothesize that PbtA, and thereby the acquisition of -HPI island, may also influence the expression of other genes elsewhere in the bacterial genome.

Structural Requirements for Ga Coordination in Synthetic Analogues of the Siderophore Piscibactin Deduced by Chemical Synthesis and Density Functional Theory Calculations.

Stereoselective total synthesis of several analogues of piscibactin (Pcb), the siderophore produced by different pathogenic Gram-negative bacteria, was performed. The acid-sensitive αmethylthiazoline moiety was replaced by a more stable thiazole ring, differing in the configuration of the OH group at the C-13 position. The ability of these Pcb analogues to form complexes with Ga as a mimic of Fe showed that the configuration of the hydroxyl group at C-13 as 13 is crucial for the chelation of Ga to preserve the metal coordination, while the presence of a thiazole ring instead of the αmethylthiazoline moiety does not affect such coordination.

Identification of Key Functions Required for Production and Utilization of the Siderophore Piscibactin Encoded by the High-Pathogenicity Island -HPI in .

Piscibactin is a widespread siderophore system present in many different bacteria, especially within the family. Previous works showed that most functions required for biosynthesis and transport of this siderophore are encoded by the high-pathogenicity island -HPI. In the present work, using as a model, we could identify additional key functions encoded by -HPI that are necessary for piscibactin production and transport and that have remained unknown.

The Temperature-Dependent Expression of the High-Pathogenicity Island Encoding Piscibactin in Results From the Combined Effect of the AraC-Like Transcriptional Activator PbtA and Regulatory Factors From the Recipient Genome.

The high-pathogenicity island -HPI is widespread among encoding the piscibactin siderophore system. The expression of piscibactin genes in the fish pathogen is favored by low temperatures. However, information about the regulatory mechanism behind -HPI gene expression is scarce.

FrpA is the outer membrane piscibactin transporter in Vibrio anguillarum: structural elements in synthetic piscibactin analogues required for transport.

Piscibactin (Pcb) is a labile siderophore widespread among Vibrionaceae. Its production is a major virulence factor of some fish pathogens such as Photobacterium damselae subsp. piscicida and Vibrio anguillarum.

The Expression of Virulence Factors in Is Dually Regulated by Iron Levels and Temperature.

causes a hemorrhagic septicemia that affects cold- and warm-water adapted fish species. The main goal of this work was to determine the temperature-dependent changes in the virulence factors that could explain the virulence properties of for fish cultivated at different temperatures. We have found that although the optimal growth temperature is around 25°C, the degree of virulence of RV22 is higher at 15°C.

The Siderophore Piscibactin Is a Relevant Virulence Factor for Favored at Low Temperatures.

causes vibriosis, a hemorrhagic septicaemia that affects many cultured marine fish species worldwide. Two catechol siderophores, vanchrobactin and anguibactin, were previously identified in this bacterium. While vanchrobactin is a chromosomally encoded system widespread in all pathogenic and environmental strains, anguibactin is a plasmid-encoded system restricted to serotype O1 strains.

The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability.

The shape of bacteria is maintained by the cell wall. The main component of the cell wall is peptidoglycan (PG) that is synthesized by penicillin binding proteins (PBPs). The correct positioning of PBPs is essential for the maintenance of cell shape.