Legionella pneumophila replicates in the distal pulmonary airspace, causing legionnaires' pneumonia. Legionella organisms replicate within alveolar macrophages and recruited blood monocytes; however, when these cells are activated, they become potent inhibitors of L. pneumophila proliferation. L. pneumophila may replicate in other cells and thereby avoid the host defenses of macrophages. Experiments demonstrated that L. pneumophila replicate within primary cultures of rat pulmonary alveolar epithelial cells. Double-label immunofluorescent and electron microscopy demonstrated L. pneumophila within epithelial cells. Replication of L. pneumophila required similar numbers of alveolar epithelial cells or alveolar macrophages, required viable epithelial cells, and took place intracellularly. While replication of L. pneumophila occurred in both serum-free and serum-containing media, it was enhanced in the presence of serum. Pulmonary alveolar epithelial cells may represent an alternative site for replication of Legionella species in the terminal airspace and thus clarify some previously unexplained aspects of the pathogenesis of legionnaires' disease.

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BackgroundHepatocellular carcinoma is a highly progressive cancer in the case of late diagnosis which is frequently associated with HBV and HCV viral infections.ObjectivesTo identify differentially expressed serum proteins among three main stages of HCV infection and healthy individuals, and their comparisons with sera from patients with the same stage of HBV infection.Patients and MethodsTwo-dimensional polyacrylamide gel electrophoresis combined with liquid chromatography-tandem mass spectrometry was performed on 47 sera from healthy volunteers, those with chronic active hepatitis, cirrhosis and HCC patients associated with HBV and HCV infections.ResultsAmong these, 62 spots were differentially expressed (≥ 1.5 fold; P < 0.05), of which 42 spots that corresponded to 15 proteins were identified by liquid chromatography-tandem mass spectrometry. CD5-like antigen (CD5L) was differentially expressed between cirrhosis and HCC patients with HCV infection. Leucine-rich α2-glycoprotein (LRG) and haptoglobin (HP) α2 isoforms differed in the HCC that was associated with either HCV or HBV infections.ConclusionsCD5L might be a useful biomarker for early diagnosis of HCC in HCV cirrhotic patients. LRG and HP α2 isoforms could be potential markers for distinguishing viral HCC. Our results also further support the presence of varying molecules involved in hepatocarcinogenesis in HBV when compared with HCV infection.

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R-factors of the P-2(prototype R-factor R931) incompatibility group of plasmidsdetected in Pseudomonas are compatible with group P,C,W, and NR-factors which areplasmids that can be transferred to Pseudomonas aeruginosa recipients. Members of the P-2 group (R130,R931) have significant homology by DNA-DNA hybridization. R-factors of the P-group (RP1, RP9) and F-group (R1) exhibited homology with P-2 R-factors but to a lesser extent than R130 with R931. Members of the I, C, and W groups showed no significant homology with P-2 R-factors. Minicircular DNA of strain 931(R931) was not homologous with R931 DNA. The host range of R931 and R130 is limited mainly to certain Pseudomonas species including P. aeruginosa, P. fluorescens, P. putida, and P. stutzeri. These R-factors could not be transferredat detectable frequencies to any member of the Enterobacteriaceae examined. R-factor-specified pili were strongly suggested by the detection of pili by electron microscopyin R-+ but not R- non-piliated mutants of P. aeruginosa strain PA01. The combinedproperties of R-factors 931 and similar R-factors reported before and in this study strongly support our previous contention that this group of R-factors form a significant new group of plasmids. A classification scheme previously proposed for plasmids occurring in Pseudomonas has been modified and four groups have been specified.

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Exoenzyme S from Pseudomonas aeruginosa has been studied as an adhesin for glycosphingolipids and buccal cells. Binding of exoenzyme S to gangliotriosylceramide (GalNAcfll-4Gal,l-4Glci3l-1Cer), gangliotetraosylceramide (Gall-3GaINAcTIIl-4Gal1l-4Glcil-lCer), and lactosylceramide (Gal31-4Glco1-lCer) separated on thin-layer chromatograms was observed. Binding curves for exoenzyme S with dilutions of gangliotetraosylceramide immobilized on plastic plates were similar to previously reported results for the intact bacteria. Binding of exoenzyme S to sialylated counterparts of these glycosphingolipids was not seen, indicating that the addition of a sialic acid residue interferes with binding. Exoenzyme S and monoclonal antibody to exoenzyme S inhibit the binding of P. aeruginosa to buccal cells. The presence of exoenzyme S on the surface of P. aeruginosa was detected by immunogold labeling of bacteria with antibodies to exoenzyme S. Results of these studies led us to conclude that exoenzyme S is an important adhesin of P. aeruginosa. Pseudomonas aeruginosa is an important opportunistic pathogen of immunocompromised patients (7). Infections of the respiratory tract are of particular concern because they are associated with high mortality rates (2). Cystic fibrosis patients are at high risk for lung infections due to P. aeruginosa which lead to significant morbidity and contribute to death of the patients (15, 17). Identification of the factors responsible for colonization of the lungs of cystic fibrosis patients by P. aeruginosa is particularly important since the organism is virtually impossible to eradicate once a chronic infection has been established.