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Query: UMLS:C0032285 (pneumonia)
 54,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During staphylococcal pneumonia massive destruction of lung tissue is often observed. Staphylococcal serine proteinase (SSP) inactivates alpha-1-proteinase inhibitor (alpha 1PI) a major factor which protects lungs from phagocyte proteases. We investigated the effect of SSP on elastin degradation by porcine pancreatic elastase (PE) and crude extract of human neutrophil elastase (NE) in solution and gel containing alpha 1PI. SSP having no elastase activity enhanced PE and NE-induced elastinolysis in solution when added to alpha 1PI before mixing with elastase and then with elastin. SSP added simultaneously with alpha 1PI to PE had no influence on elastin degradation. However, SSP added simultaneously, 30 min before or 30 min after PE significantly increased elastin digestion in elastin-agarose plate with alpha 1PI. Maximal increase in elastinolysis about 3-fold was for SSP added 30 min prior to PE. Since elastin is the major component of the alveolar walls it is possible that lung damage in the course of staphylococcal infection may partly depend on action of SSP.
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PMID:Serine proteinase from Staphylococcus aureus enhances elastin degradation by elastases in the presence of human alpha-1-proteinase inhibitor. 185 84

Several strains of Staphylococcus aureus have been found to secrete proteases that activate infectivity of influenza virus by proteolytic cleavage of the hemagglutinin. The enzymes of the bacterial strains Wood 46 and M 86/86 have been characterized in some detail and were found to be serine proteases. In their substrate specificities and inhibitor sensitivities they proved to be similar to, but not identical with trypsin and plasmin. The hemagglutinin of an individual virus strain could be cleaved by the proteases of some but not all staphylococcal strains, and a given enzyme could cleave only some but not all hemagglutinins analyzed. When mice were coinfected intranasally with the appropriate strains of influenza virus and S. aureus, the hemagglutinin was readily activated allowing multiple cycles of virus replication in the lung. Under these conditions, the animals came down with a fatal disease exhibiting extended lesions in the lung tissue. In contrast, after infection with virus or bacteria alone, there were no significant pathological changes. When the staphylococcal strain did not contain a protease that was able to activate the hemagglutinin of the coinfecting virus strain, the animals did not exhibit disease. These observations demonstrate that coinfecting bacteria can play an essential role in the development of influenza pneumonia by providing a protease suitable for cleavage activation of the hemagglutinin.
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PMID:Synergistic role of staphylococcal proteases in the induction of influenza virus pathogenicity. 302 81

A total of 29 Pasteurella multocida strains were isolated in cases of atypical fowl cholera with swelling of the wattles as well as from pigs and calves with pneumonia. All strains were used to study the metabolism of 10 amino acids. Glutaminic acid was found to be metabolized by all investigated strains. Arginine was metabolized by Pasteurella organisms isolated from mammals (calves and pigs), and was metabolized by Pasteurellae isolated from birds. By their positive reaction with proline and their negative one with alanine the Pasteurella strains isolated in cases of acute cholera differed from all other Pasteurella organisms. Asparagine was metabolized only by Pasteurellae isolated in cases of atypical fowl cholera, and serine--only by Pasteurellae isolated from pigs.
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PMID:[Metabolism of free amino acid in strains of Pasteurella multocida and their division into biological types]. 650 59

The sequences of the genes encoding the putative attachment (G) proteins of pathogenic (strain J3666) mouse lung-passaged and nonpathogenic (strain 15) tissue culture-passaged strains of pneumonia virus of mice (PVM) have been determined. In both cases the major polypeptide was synthesised from the second open reading frame (ORF), a feature also found in the G gene of respiratory syncytial (RS) virus, another pneumovirus. However, the ORFs of the G genes of the two PVM strains were initiated at different nucleotide positions in the mRNA and comparison of hydrophobicity profiles revealed the presence of the putative amino-terminal cytoplasmic domain in the strain J3666 G protein and its absence in the predicted G protein of PVM strain 15. In common with the G protein of RS virus, the gene product of both PVM strains contained a high serine, threonine, and proline content. Indirect immunofluorescence analysis of BSC-1 cells expressing the G gene products confirmed the surface location of the proteins. Thus, the absence of a cytoplasmic domain does not interfere with the translocation of the G protein of PVM strain 15. In vitro translation of mRNA from the two PVM genes directed the synthesis of a larger polypeptide with the G gene of PVM strain J3666 than was seen with strain 15 G gene. In addition, a second protein was seen with strain J3666 mRNA which was the same size as the strain 15 G protein.
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PMID:Nucleotide sequences of the genes encoding the putative attachment glycoprotein (G) of mouse and tissue culture-passaged strains of pneumonia virus of mice. 787 33

In this study we have assessed the action of a novel glycoprotease, secreted by the bovine pneumonia pathogen Pasteurella haemolytica, on epitectin expressed on the surface of human laryngeal carcinoma (H.Ep.2) cells. Epitectin has been previously characterized as a high buoyant density glycoprotein of mass of over 350 kDa extensively glycosylated on serine and threonine by small oligosaccharides. Purified metabolically labeled epitectin was very effectively hydrolyzed by the glycoprotease. However, short- and long-term treatments yielded a complex mixture of products which could not be resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) or column chromatography, probably because of the heterogeneity of the structure and the distribution of the saccharides. Treatment of H.Ep.2 cells with glycoprotease followed by flow cytometric analysis revealed a significant loss in the cell surface epitopes detected by the anti-epitectin Ca2 monoclonal antibody. The action of the glycoprotease on cell surface epitectin was blocked by anti-glycoprotease antisera and was absent in an extract of a glycoprotease-negative strain of P. haemolytica. When extracts of cells treated with glycoprotease for 4 h were subjected to SDS-PAGE followed by 125I-wheat germ agglutinin overlay and autoradiography, the intensity of the characteristic epitectin bands was found to be drastically reduced compared to controls. H.Ep.2 cells metabolically labeled with [3H]glucosamine were also incubated with or without the glycoprotease and the released products were fractionated and analyzed. The enzyme-released products were found to be enriched in mucin-type glycopeptides. Thus the P. haemolytica glycoprotease could be used to selectively degrade mucin glycoproteins on cancer cell surface.
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PMID:Cleavage of epitectin, a mucin-type sialoglycoprotein, from the surface of human laryngeal carcinoma cells by a glycoprotease from Pasteurella haemolytica. 817 12

Sfericase is an important intracellular proteinase produced by Bacillus sphaericus in the stationary phase of growth. It is a Ca(2+)-dependent serine proteinase with optimal activity at pH 9.0 to 9.3. The molecular mass of sfericase is 32 kDa, as determined by sedimentation equilibrium. It seems to be involved in the interplay of various elements of the mosquitocidal activity of B. sphaericus, and hence is important for biological mosquito control. Sfericase significantly reduces viscosity of human pathological bronchial secretions and has recently shown good clinical effects in treatment of bronchitis, pneumonia and sinusitis. This enzyme was isolated from B. sphaericus and single crystals were obtained by the hanging drop vapor diffusion method. The crystals belong to the monoclinic space group P2, with cell dimensions of a = 46.94 A, b = 64.55 A, c = 86.23 A and beta = 95.4 degrees. These crystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1.8 A resolution. The cell dimensions are consistent with four molecules per unit cell and two molecules in the asymmetric unit. A complete native data set to 1.77 A resolution has been collected on a Rigaku R-AXIS-IIc Imaging Plate Detector system and a heavy-atom derivative search is presently in progress.
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PMID:Crystallization and preliminary crystallographic analysis of sfericase. A Bacillus sphaericus calcium-dependent serine proteinase. 828 93

A 65-year-old man was admitted to our hospital because of syncope, hyperthermia and urinary disturbance. Neurological examination revealed cerebellar ataxia, muscular rigidity, hyperreflexia with Babinski sign in both sides, and various autonomic dysfunctions including anisocoria, orthostatic hypotension and neurogenic bladder. He was diagnosed as having Shy-Drager syndrome (SDS). Oral administration of L-threo-3,4-dihydroxyphenyl-serine (L-DOPS) (300 mg/day) was started for orthostatic hypotension. After discharge he suffered from pneumonia at his house, and he kept himself warm because of a chill. The patient then fell into hyperthermia (44.0 degrees C), resulting in unconsciousness and a state of shock. He was transferred to our hospital again and was treated by body cooling and drip infusion of dopamine after which he recovered completely within one day. Control of body temperature and blood pressure was examined by heat loading and head-up tilt after heat loading, with or without administration of L-DOPS. These examinations showed that his rectal body temperature rose easily during heat loading and that this phenomenon was enhanced by the administration of L-DOPS. Moreover as his body temperature became higher, he more easily developed syncope due to orthostatic hypotension. It is suggested that in SDS patients, L-DOPS facilitates orthostatic hypotension and syncope in high temperature conditions.
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PMID:[Hyperthermia in a Shy-Drager syndrome patient--pathophysiological effects of body temperature and L-DOPS on orthostatic hypotension]. 833 78

Pneumocystis carinii causes life-threatening pneumonia in immunocompromised patients. The inability to culture P. carinii has hampered basic investigations of the organism's life cycle, limiting the development of new therapies directed against it. Recent investigations indicate that P. carinii is a fungus phylogenetically related to other ascomycetes such as Schizosaccharomyces pombe. The cell cycles of S. pombe and homologous fungi are carefully regulated by cell-division-cycle molecules (cdc), particularly cell-division-cycle 2 (Cdc2), a serine-threonine kinase with essential activity at the G1 restriction point and for entry into mitosis. Antibodies to the proline-serine-threonine-alanine-isoleucine-arginine (PSTAIR) amino-acid sequence conserved in Cdc2 proteins specifically precipitated, from P. carinii extracts, a molecule with kinase activity consistent with a Cdc2-like protein. Cdc2 molecules exhibit differential activity throughout the life cycle of the organisms in which they occur. In accord with this, the P. carinii Cdc2 showed greater specific activity in P. carinii trophic forms (trophozoites) than in spore-case forms (cysts). In addition, complete genomic and complementary DNA (cDNA) sequences of P. carinii Cdc2 were cloned and found to be most closely homologus to the corresponding sequences of other pathogenic fungi. The function of P. carinii cdc2 cDNA was further documented through its ability to complement the DNA of mutant strains of S. pombe with temperature-sensitive deficiencies in Cdc2 activity. The P. carinii cdc2 cDNA restored normal Cdc2 function in these mutant strains of S. pombe, and promoted fungal proliferation. These studies represent the first molecular analysis of the cell-cycle-regulatory machinery in P. carinii. Further understanding of P. carinii's life cycle promises novel insights for preventing and treating the intractable infection it causes in immunocompromised patients.
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PMID:Pneumocystis carinii contains a functional cell-division-cycle Cdc2 homologue. 949 Jun 47

Chlamydia are obligate intracellular eubacteria that are phylogenetically separated from other bacterial divisions. C. trachomatis and C. pneumoniae are both pathogens of humans but differ in their tissue tropism and spectrum of diseases. C. pneumoniae is a newly recognized species of Chlamydia that is a natural pathogen of humans, and causes pneumonia and bronchitis. In the United States, approximately 10% of pneumonia cases and 5% of bronchitis cases are attributed to C. pneumoniae infection. Chronic disease may result following respiratory-acquired infection, such as reactive airway disease, adult-onset asthma and potentially lung cancer. In addition, C. pneumoniae infection has been associated with atherosclerosis. C. trachomatis infection causes trachoma, an ocular infection that leads to blindness, and sexually transmitted diseases such as pelvic inflammatory disease, chronic pelvic pain, ectopic pregnancy and epididymitis. Although relatively little is known about C. trachomatis biology, even less is known concerning C. pneumoniae. Comparison of the C. pneumoniae genome with the C. trachomatis genome will provide an understanding of the common biological processes required for infection and survival in mammalian cells. Genomic differences are implicated in the unique properties that differentiate the two species in disease spectrum. Analysis of the 1,230,230-nt C. pneumoniae genome revealed 214 protein-coding sequences not found in C. trachomatis, most without homologues to other known sequences. Prominent comparative findings include expansion of a novel family of 21 sequence-variant outer-membrane proteins, conservation of a type-III secretion virulence system, three serine/threonine protein kinases and a pair of parologous phospholipase-D-like proteins, additional purine and biotin biosynthetic capability, a homologue for aromatic amino acid (tryptophan) hydroxylase and the loss of tryptophan biosynthesis genes.
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PMID:Comparative genomes of Chlamydia pneumoniae and C. trachomatis. 1019 88

A unique family of genes encoding serine endoproteases related to the Saccharomyces cerevisiae serine endoprotease kexin was identified in Pneumocystis carinii. Unlike previously described serine endoprotease genes that are single copies, multiple copies of the P. carinii serine endoprotease are distributed throughout the genome. The proteins predicted by these variant genes demonstrate sequence variability, but they retain the conserved active sites associated with endoprotease activity. The serine endoprotease was localized to the organism surface by immunohistochemical and immunofluorescence studies and to the electron lucent layer of the cyst wall by immunoelectron microscopy. The findings of multiple copies of the serine endoprotease gene in the P. carinii genome, and its localization to the cell surface, suggest that this protease plays an important role in the biology of P. carinii and that antigenic variation of the surface-expressed serine endoprotease may be a strategy for immune evasion. P. carinii serine endoprotease provides a novel target for chemotherapeutic and immune-based approaches to the treatment of P. carinii pneumonia.
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PMID:Characterization of a multicopy family of genes encoding a surface-expressed serine endoprotease in rat Pneumocystis carinii. 1041 43


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