Small bowel obstruction and covered perforation in childhood caused by bizarre bezoars and foreign bodies.

BACKGROUND: Small bowel obstruction with perforation is an unusual and rare complication of bezoars. OBJECTIVE: To describe our use of emergency laparotomy to treat intestinal obstruction caused by bizarre bezoars. CONCLUSIONS: An aggressive surgical approach to intestinal obstruction in the pediatric disabled or mentally retarded population is recommended.

A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix.

Streptococcus pyogenes binds to the extracellular matrix (ECM) and a variety of host cells and tissues, causing diverse human diseases. Protein F, a S.pyogenes adhesin that binds fibronectin (Fn), contains two binding domains. A repeated domain (RD2) and an additional domain (UR), located immediately N-terminal to RD2. Both domains are required for maximal Fn binding. In this study, we characterize RD2 and UR precisely and compare their functions and binding sites in Fn. The minimal functional unit of RD2 is of 44 amino acids, with contributions from two adjacent RD2 repeats flanked by a novel 'MGGQSES' motif. RD2 binds to the N-terminal fibrin binding domain of Fn. UR contains 49 amino acids, of which six are from the first repeat of RD2. It binds to Fn with higher affinity than RD2, and recognizes a larger fragment that contains fibrin and collagen binding domains. Expression of UR and RD2 independently on the surface-exposed region of unrelated streptococcal protein demonstrates that both mediate adherence of the bacteria to the ECM. We describe here a mechanism of adherence of a pathogen that involves two pairs of sites located on a single adhesin molecule and directed at the same host receptor.

ST segment reelevation after acute myocardial infarction: marked differences in the electrocardiographic pattern between early and late episodes.

This study assesses the electrocardiographic (ECG) morphologic differences between early (< 24 h) and late (> 24 h) episodes of ST segment reelevation after acute myocardial infarction. We studied the records of 101 consecutive patients with acute myocardial infarction whose admission ECG demonstrated ST segment elevation with positive T waves, without pathological Q waves in the relevant leads, and without signs of bundle branch block or left ventricular hypertrophy. Thirty-five patients had 44 episodes of early ST segment reelevation, while 22 patients experienced 26 late episodes of ST segment reelevation. Seven patients experienced both early and late episodes. Early episodes of ST segment reelevation was seen more often after thrombolytic therapy: 43% (32 of 74 patients) versus 11% (3 of 27 patients) (P < 0.006). No differences were found in the incidence of late episodes between those who underwent (23%) or did not undergo (19%) thrombolytic therapy. Two patterns of ST segment elevation were distinguished. Pattern A with positive T waves, ST segment elevation (> or = 0.1 mV), but without distortion of the terminal portion of the QRS complex. Pattern B characterized by positive T waves, ST segment elevation (> or = 0.1 mV) with distortion of the terminal portion of the QRS complex. Each ECG was categorized according to these two patterns. The admission ECG pattern was A in 75 patients, and B in 26. No significant differences were found between patients with early, late, or no episodes of ST segment reelevation in the appearance of pattern A or B on admission.(ABSTRACT TRUNCATED AT 250 WORDS)

Protein F: an adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains.

The binding of Streptococcus pyogenes to fibronectin (FN) enables the adherence of this pathogen to target epithelial cells, which is the first necessary step for initiation of infection. Binding is mediated by a bacterial surface protein termed protein F. Here we provide the complete structure of protein F and identify two domains responsible for binding to fibronectin. The first domain is located towards the C-terminal end of the molecule and is composed of five repeats of 37 amino acids that are completely repeated four times and a fifth time partially. The second domain is adjacent to the first domain and is located on the N-terminal side of it. It is composed of a single stretch of 43 amino acids. Protein F expressed in Escherichia coli completely blocked the binding of fibronectin to S. pyogenes. However, mutant proteins that contained only one or the other of the two domains were only capable of partial blockage of binding. Complete blockage of binding of fibronectin could be achieved when a protein extract containing the N-terminal domain was mixed in a binding reaction with a protein extract containing the C-terminal domain. Similarly, a purified recombinant protein containing the two domains only, blocked the binding completely. In contrast, a purified recombinant protein containing just the C-terminal domain, blocked the binding partially. A clone exclusively expressing the C-terminal domain, completely blocked the binding of the 30 kDa N-terminal fragment of fibronectin to S. pyogenes, whereas a clone expressing the N-terminal domain failed to block the binding of this FN fragment.(ABSTRACT TRUNCATED AT 250 WORDS)