Mass spectrometric detection of neutrophil elastase cleaved corticosteroid binding globulin and its association with Asn347 site glycosylation, in septic shock patients.

Background: Corticosteroid-binding globulin (CBG) modulates tissue cortisol availability via modification of cortisol:CBG binding affinity in response to multiple factors, including neutrophil elastase (NE) cleavage of the reactive centre loop (RCL), converting high affinity CBG (haCBG) to low affinity CBG (laCBG). In vitro, glycosylation of the RCL at Asn347 affects NE cleavage susceptibility. To date, no direct measurement of laCBG, which would verify NE cleavage, has been reported.

Nonbacterial Thrombotic Endocarditis in a 78-Year-Old Female With Recurrent Acute Ischemic Stroke: A Case Report.

Nonbacterial thrombotic endocarditis (NBTE) is a rare but serious complication, particularly in patients with malignancies like acute myeloid leukemia (AML), where a hypercoagulable state increases the risk of embolic events. This case report describes a rare and complex presentation of marantic endocarditis in a 78-year-old female with relapsed AML. The uniqueness of this case lies in the intersection of a hypercoagulable state induced by AML and the resultant NBTE, leading to recurrent embolic strokes, despite oral anticoagulation.

Combinations of Bacteriophage Are Efficacious against Multidrug-Resistant and Enhance Sensitivity to Carbapenem Antibiotics.

The Gram-negative ESKAPE bacterium has become a pathogen of serious concern due its extensive multi-drug resistance (MDR) profile, widespread incidences of hospital-acquired infections throughout the United States, and high occurrence in wound infections suffered by warfighters serving abroad. Bacteriophage (phage) therapy has received renewed attention as an alternative therapeutic option against recalcitrant bacterial infections, both as multi-phage cocktails and in combination with antibiotics as synergistic pairings. Environmental screening and phage enrichment has yielded three lytic viruses capable of infecting the MDR strain PAO1.

Comparing Methods to Genetically Engineer Bacteriophage and Increase Host Range.

Introduction: Antibacterial resistance is an emerging problem in military medicine. Disruptions to the health care systems in war-torn countries that result from ongoing conflict can potentially exacerbate this problem and increase the risk to U.S.

Hydrophobic residues in S1 modulate enzymatic function and voltage sensing in voltage-sensing phosphatase.

The voltage-sensing domain (VSD) is a four-helix modular protein domain that converts electrical signals into conformational changes, leading to open pores and active enzymes. In most voltage-sensing proteins, the VSDs do not interact with one another, and the S1-S3 helices are considered mainly scaffolding, except in the voltage-sensing phosphatase (VSP) and the proton channel (Hv). To investigate its contribution to VSP function, we mutated four hydrophobic amino acids in S1 to alanine (F127, I131, I134, and L137), individually or in combination.