Native valve endocarditis and vertebral osteomyelitis caused by Staphylococcus epidermidis.
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Biomedical subjects
Publications and source records attributed to T Gottlieb.
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The susceptibilities of 900 clinical isolates of anaerobic bacteria to 14 antimicrobial agents were determined by an agar dilution technique. Chloramphenicol, imipenem and metronidazole were found to be active against virtually all of the strains; only a single Bacteroides fragilis isolate was resistant to both imipenem and metronidazole. The addition of clavulanic acid to amoxycillin and ticarcillin potentiated the activities of these agents against all anaerobes including members of the B. fragilis group. Ampicillin/sulbactam and clindamycin were the next most active agents, 91 and 89% of isolates respectively being susceptible. Seventy-three per cent of the bacteria tested were susceptible to cefoxitin and 65% to cefotetan, with the MICs of almost 50% of the isolates clustering between 16 and 32 mg/L. There was also clustering around the breakpoint (64 mg/L) of piperacillin. Azithromycin exhibited poor activity against the B. fragilis group; only 18% of isolates were susceptible to < or = 4 mg/L. However, 92% of non-B. fragilis Bacteroides group strains were susceptible to this agent. We conclude that imipenem, metronidazole, chloramphenicol, ticarcillin/clavulanate, co-amoxiclav and, to a lesser extent, ampicillin/sulbactam are suitable as empirical therapy for infections caused by anaerobic bacteria.
Five Veterans' Administration Medical Centers formed a consortium to promote nursing research. Consortium arrangements focusing on research are reviewed based on the literature, the consortium's experience, and a survey of 171 VA facilities. Consortiums are suggested for multisite facilities, such as city, state, proprietary, and religious hospital systems, to increase the quality and quantity of nursing research where institutional mechanisms for overcoming the difficulties of meeting and sharing information are already in place.
The role of viruses and atypical organisms in pneumonia is well known in western populations, yet very little documentation is available about their role in pneumonia in developing countries. In a study of 175 adults with community-acquired pneumonia in Papua New Guinea, serological methods were used to assess this issue. Five patients had high influenza A titres suggestive of recent infection. Adenovirus titres rose significantly in one patient with Haemophilus influenzae pneumonia, whilst no evidence of past or recent infection was found in the remainder of patients when tested for all pathogens. Bacterial cultures revealed the continued predominance of Streptococcus pneumoniae in the pathogenesis of pneumonia in this population. We conclude that viruses and atypical organisms (including Mycoplasma and Legionella) play a very limited role in this setting.
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When synthesized in polarized epithelial cells, the envelope glycoproteins hemagglutinin of influenza and G of vesicular stomatitis virus are targeted to the apical and basolateral plasma membranes, respectively. To determine which portions of these transmembrane proteins contain information necessary for their sorting, the behavior of two different G-hemagglutinin chimeric polypeptides, consisting of all or nearly all the luminal portion of the vesicular stomatitis virus G protein linked to C-terminal segments of influenza hemagglutinin that included its transmembrane and cytoplasmic domains, was studied in MDCK cells transformed with the corresponding cDNAs. Both chimeras were transported from the endoplasmic reticulum to the Golgi apparatus and from there to the cell surface with the same rapid kinetics as the intact G protein. By using a cell surface immunoprecipitation assay with monolayers cultured on permeable filters that allows the recovery of labeled protein molecules present in each cell surface domain, it was found that both chimeric proteins as well as the intact G protein were delivered almost exclusively to the basolateral surface. This polarized distribution of the polypeptides did not change during a subsequent 90-min chase period, although during this time a large fraction of the glycoprotein molecules underwent degradation. In addition, a small fraction of the cell surface-associated glycoprotein molecules shed their ectoplasmic segments into the basolateral compartment, apparently as a result of a proteolytic cleavage. Immunofluorescence on transverse frozen sections and immunoelectron microscopy revealed a prominent accumulation of the chimeric polypeptides in the lateral cell membranes, with lesser amounts on the basal and apical surfaces. These results indicate that information specifying the basolateral transport of the G glycoprotein is located within the first 426 N-terminal amino acids of its ectoplasmic portion.
We describe the first case report of community-acquired Acinetobacter pneumonia in Australia. Well recognised risk factors for this entity (alcoholism, diabetes mellitus and chronic lung disease) were present in our patient. His pneumonia ran a fulminant course, with death occurring within 24 hours of presentation to hospital. Whilst rare, this infection is being described with increasing frequency, particularly in developing countries including Papua New Guinea.
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The demonstration that the envelope glycoproteins G of vesicular stomatitus virus and hemagglutinin of influenza virus synthesized in polarized epithelial cells transfected with the corresponding genes are effectively segregated to the basolateral or apical plasma membrane domains, respectively, implies that the information determining this segregation resides within the structures of the proteins themselves. To localize the sorting information within these proteins, the polarity of secretion of truncated hemagglutinin and G glycoproteins secreted from confluent monolayers of MDCK cells transformed with vectors containing the corresponding truncated cDNAs was examined. It was found that, even though the transformed cells continued to secrete a major endogenous glycoprotein exclusively from the apical surface, the modified viral glycoproteins were secreted in a nonpolarized fashion from both sides of the monolayers. These observations suggest that important information for the sorting of the viral glycoprotein is contained within their membrane anchoring or cytoplasmic segments or that, if sorting signals are luminally located, these signals must be present in a conformation that is not attainable when the polypeptides are not attached to the membrane.
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