Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0014118 (endocarditis)
 15,629 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mortality of non-toxigenic Corynebacterium diphtheriae endocarditis is high (27%). One explanation could be tolerance to amoxicillin. The aim of this work was to evaluate in vivo the tolerance phenomenon, in a rabbit endocarditis experimental model. Two strains of non-toxigenic Corynebacterium diphtheriae were compared: a tolerant one and a non-tolerant one. EACH ANIMAL WAS RANDOMLY ASSIGNED TO ONE OF THE FOLLOWING GROUPS: no treatment, continuous infusion of amoxicillin simulating 200 mg/kg/24 h in humans, or fractionated infusion of amoxicillin simulating 66 mg/kg/8 h in humans. Surviving bacteria were counted in vegetations after one or three days of treatment. The 24 h fractionated amoxicillin infusion was more efficacious on the non-tolerant strain than on the tolerant strain. On the tolerant strain, 24 h amoxicillin was more efficacious as a continuous infusion than as a fractionated one.
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PMID:[In vivo activity of amoxicillin in a non-toxigenic Corynebacterium diphtheriae rabbit endocarditis experimental model]. 1249 Apr 12

Activation and invasion of the vascular endothelium by Staphylococcus aureus is a major cause of sepsis and endocarditis. For endothelial cell invasion, S. aureus triggers actin polymerization through Cdc42, N-WASp (also known as WASL) and the Arp2/3 complex to assemble a phagocytic cup-like structure. Here, we show that after stimulating actin polymerization staphylococci recruit Cdc42GAP (also known as ARHGAP1) which deactivates Cdc42 and terminates actin polymerization in the phagocytic cups. Cdc42GAP is delivered to the invading bacteria on recycling endocytic vesicles in concert with the exocyst complex. When Cdc42GAP recruitment by staphylococci was prevented by blocking recycling endocytic vesicles or the exocyst complex, or when Cdc42 was constitutively activated, phagocytic cup closure was impaired and endothelial cell invasion was inhibited. Thus, to complete invasion of the endothelium, staphylococci reorient recycling endocytic vesicles to recruit Cdc42GAP, which terminates Cdc42-induced actin polymerization in phagocytic cups. Analogous mechanisms might govern other Cdc42-dependent cell functions.
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PMID:Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells. 2731 80