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

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

We characterized urinary excretion of C3 fragments among patients with systemic lupus erythematosus (SLE) as a possible indicator of renal involvement. 28 patients, representing a broad range of disease activity were admitted to our study. Urinary proteins were separated on 4-20% gradient SDS-PAGE gels, under reducing conditions, and transblotted to nitrocellulose. Western blots were developed with a polyvalent goat-anti-human C3d antiserum, and an alkaline phosphatase-conjugated rabbit anti-goat IgG. Three patterns were obtained: 1) no bands detected; 2) bands suggesting the presence of intact C3; and 3) samples with additional low molecular (< 4 x 10(4)) bands. The 12 patients with no C3 bands had minimal disease activity (e.g. fatigue, arthralgia, arthritis, rash, oral ulcers). The seven patients with intact C3 patterns also had minimally active disease. Their primary clinical findings included fatigue, pleurisy, renal disease which had been treated, hemolytic anemia, and arthritis. Patients with low molecular weight C3 fragments in their urine formed two sub-sets, based upon their presenting features. The first group had severe disease and contained all patients with active lupus nephritis (n = 4), while the second consisted of non-renal patients with primary clinical findings of moderate disease activity (e.g. thrombocytopenia, pneumonitis, arthritis). Our results suggest urinary excretion of low molecular weight C3 fragments correlates with active renal disease, but is a variable finding among SLE patients with non-renal manifestations of disease activity.
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PMID:Complement C3 fragments in urine: detection in systemic lupus erythematosus patients by western blotting. 819 18

A 74-year-old female developed pneumonia following herpes simplex encephalitis. Her white blood cell counts reached 28,400/microliters, about 90% of which consisted of granulocytes. The polymorphonuclear (PMN) elastase/alpha 1-antitrypsin complex levels increased and reached the maximum of 5,019 ng/ml, indicating the release of a large amount of elastase derived from the granulocytes. The mechanism of PMN elastase release was most likely to be granulocyte destruction associated with phagocytosis. The cleavage of fibrinogen and fibrin by PMN elastase, independent of plasmin, was indicated by the presence of the fragments in immunoprecipitated plasma from the patient corresponding to elastase-induced FDP D and DD fragments and the absence of fragments corresponding to plasmin-induced FDP D and DD fragments on SDS-PAGE. These findings suggested that the large amount of PMN elastase released from the excessive numbers of granulocytes in this patient with herpes simplex encephalitis and pneumonia, induced the cleavage of fibrinogen and fibrin without the participation of plasmin.
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PMID:An alternative elastase-mediated degradation of fibrinogen and fibrin observed in a patient with herpes simplex encephalitis and pneumonia. 886 27

An R. equi vaccine, prepared under conditions which induce the expression of many antigens, and which has given encouraging results in field trials, was analyzed by SDS-PAGE and immunoblots and compared with other R. equi preparations: a preparation made in with the same technique from a nonvirulent isolate (virulence associated protein negative, VapA-negative); a whole cell preparation of a VapA-positive R. equi, prepared as a standard bacterin; and a semipurified VapA preparation (APTX). The antigens in these preparations were analyzed using hyperimmune sera (from adult horses vaccinated with the R. equi vaccine), passively and actively immunized foals' sera, asymptomatic but serologically positive foals' sera sera from R. equi pneumonic foals, an equine APTX antiserum, and a VapA monoclonal antibody (Mab). The vaccine under study had many proteins in high concentrations. Hyperimmune sera reacted strongly with vaccine antigens in the high molecular weight regions. In the low molecular weight range, it reacted in the 14 and less kDa zone. Sera from passively immunized foals reacted similarly but not so strongly. Actively immunized foals gave very weak reactions. With the APTX extract, the Mab reacted with bands at 15-17, 44 and 66 kDa; it reacted weakly with the whole cell and not with the VapA-negative preparations. The APTX antiserum and the Mab reacted strongly with the vaccine at the 14 and less kDa zone, and also with bands at 21, 44 and 66 kDa and very tenuously at 18 kDa, but not in the expected 15-17 kDa zone, suggesting that the native form of VapA is altered but without loss of antigenicity in the vaccine preparation. Our results suggest that other higher molecular weight antigens, in addition to VapA, may be important in inducing antibodies that protect young foals from R. equi pneumonia. These antigens are in high concentrations and in an immunogenic form in the vaccine.
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PMID:Antigenic analysis of Rhodococcus equi preparations using different horse sera. 922 39

A putative structural gene cluster containing four open reading frames (ORFs) located downstream of the omp1 gene of Chlamydia trachomatis mouse pneumonitis (MoPn) was cloned and sequenced. A GenBank survey indicated that the identified cluster is similar to the rpsB-tsf-pyrH(smbA)-frr region of Escherichia coli. The second ORF was 846 bp encoding a 282-amino-acid polypeptide with a calculated M(r) 30,824. Alignment of this deduced protein sequence and E. coli elongation factor Ts (EF-Ts, product of tsf) demonstrated 34% identity and an additional 14% similarity. The putative chlamydial tsf gene was expressed in E. coli as a nonfusion protein and as a 6x His-tagged fusion protein. By SDS-PAGE analysis, the molecular weights of the nonfusion recombinant protein and a protein of chlamydial elementary bodies (EBs), which was recognized by monoclonal antibodies derived from the nonfusion recombinant protein, are 34 kDa. The purified recombinant 6x His-tagged fusion protein increased the rate of GDP exchange with both Chlamydia and E. coli elongation factor Tu (EF-Tu). These data show that the second gene of the identified cluster is tsf. Unlike EF-Ts from any other species, its activity was comparable to that of E. coli EF-Ts in exchange reaction with E. coli EF-Tu.
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PMID:Elongation factor Ts of Chlamydia trachomatis: structure of the gene and properties of the protein. 924 80

Ps. aeruginosa is a frequent and prominent cause of nosocomial pneumonia especially in persons on assisted ventilation in the intensive care units. In a year long surveillance of ventilator associated pneumonia (VAP) we isolated 42 strains from broncho alveolar lavage samples collected and processed from 102 patients. By pyocin typing 40 of the 42 strains could be typed into 39 types but this designation changed each time the test was repeated. SDS-PAGE analysis of the whole cell proteins grouped the 42 strains of Ps. aeruginosa into 20 groups. After ribotyping, using an 18 mer DIG labelled oligonucleotide to the conserved region of 16S rRNA gene, the strains were designated into 18 types. The major type contained 8 isolates, but there was no clustering of isolates, indicating that each infecting strain was acquired separately and not from a common source. It would, therefore, appear that cross infection with a single clone was not the predominant mode of Ps. aeruginosa infection causing VAP in our ICU.
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PMID:Study of Pseudomonas aeruginosa causing ventilator associated pneumonia. 954 Feb 79

The Mycoplasma pneumoniae FH strain routinely used in our laboratory for over 25 years as antigen in serological tests, 2 reference M. pneumoniae strains from ATCC (29342 and M129) and 3 isolates of M. pneumoniae obtained in 1995 from pneumonia patients were compared by SDS-PAGE, complement fixation test (CFT) and by Western-immunoblotting against human and rabbit serum samples with high level of mycoplasmal antibodies. On SDS-PAGE all M. pneumoniae strains showed the same number of 23 polypeptides on the gel with identical molecular weights. The same strains on immunoblotting against human and rabbit serum samples showed six bands: 170, 89, 75, 55, 38 and 33 kDa with the strongest antibody staining in 170-(P1 protein) and 89-kDa bands. Because of its known antigenic relationships Mycoplasma genitalium was used for comparison. The pattern of M. genitalium proteins on SDS-PAGE was similar to pattern of M. pneumoniae but distinguishable. On immunoblotting six proteins of M. genitalium (135, 127, 110, 95, 75 and 45 kDa) reacted with human and rabbits immunoglobulins for M. pneumoniae antigens. Furthermore in complement fixation test both antigens, prepared from M. pneumoniae and M. genitalium, reacted as well with human and rabbit immunoglobulins for M. pneumoniae and with rabbit immunoglobulins for M. genitalium. These cross-reactions observed in serological techniques could give false positive results in routine diagnosis of M. pneumoniae infections. In such situations showing on immunoblott of presence in tested serum sample of antibodies to 170- and 89 kDa proteins could confirm M. pneumoniae infection.
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PMID:[Electrophoretic and immunologic comparative analysis of Mycoplasma pneumoniae and Mycoplasma genitalium proteins]. 1022 41

To understand how neutrophils are recruited to the lung in pneumococcal pneumonia, the ability of pneumococcal components to elicit the chemokine interleukin (IL)-8 from monolayers of cultured human type II cells was assessed. Heat-killed clinical and laboratory strains of Streptococcus pneumoniae and secreted proteins from exponentially growing pneumococci elicited significant quantities of IL-8 from A549 cells. All strains that elicited IL-8 production secreted a protein ( approximately 90 kDa) that comigrated on SDS-PAGE with a C3-binding protein previously identified in S. pneumoniae. As little as 7 pmol of the purified 90-kDa protein readily elicited levels of IL-8 production equivalent to those obtained with 1 U of IL-1alpha. Supernatant proteins and heat-killed cells of an isogenic mutant that failed to produce the C3-binding protein elicited significantly less IL-8 than did supernatant proteins or heat-killed cells of the parent strain. These results implicate the C3-binding protein of S. pneumoniae in a novel pathway of pulmonary inflammation.
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PMID:A pneumococcal protein that elicits interleukin-8 from pulmonary epithelial cells. 1076 64

Several mycoplasma species produce various diseases in different animal species. M. bovis has been described as the cause of mastitis, arthritis, pneumonia and infertility in cattle. Furthermore, this species has been the most frequently isolated agent producing bovine mastitis. The objective of this study was to isolate and typify mycoplasma strains from a clinical mastitis outbreak in a dairy farm of Buenos Aires Province. A total of 279 samples were studied (276 from pooled quarter milk of cows with clinical mastitis that did not respond to antibiotic therapy, 1 from bulk tank milk and 2 preputial swabs from bulls). The isolated mycoplasma strains (n = 12) were further characterized by biochemical analysis, serological studies and electrophoretic analysis of the protein profiles (SDS-PAGE). Based upon these studies, the isolated strains were identified as Mycoplasma bovis. This is the first report of isolation of this microorganism in Argentina. Therefore the results described here could be very useful to improve mastitis control in dairy farms.
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PMID:[Isolation of Mycoplasma bovis during an outbreak of bovine mastitis at a dairy farm in the province of Buenos Aires. 1st report in the Republic of Argentina]. 1094 23

Pasteurella haemolytica serovar A1 is the causative agent of acute fibrinohemorrhagic pneumonia also known as shipping fever. Many pathogens, including P. haemolytica, survive in their respective hosts through the up-regulation of an iron acquisition system. In this study we identified, purified and characterized a 35-kDa periplasmic iron-regulated protein. The N-terminal sequence of the iron-regulated protein ANEVNVYSYRQP YLIEPMLK was identical to the deduced amino acid sequence of the ferric binding protein, FbpA, of P. haemolytica. Growth of P. haemolytica in a synthetic medium (RPMI-1640), without iron and supplemented with 50 gM 2,2' dipyridyl, facilitated the expression, isolation and purification of the native P. haemolytica FbpA. The protein was purified to homogeneity by using ammonium sulfate precipitation followed by CM-Sepharose ion exchange chromatography. SDS-PAGE showed a single band with a molecular weight of 35,369. Isoelectric focusing showed multiple bands with pIs of 5.5, 5.6, 5.8, and one major band with pI of 6.4. The molecular weight obtained by electrospray mass spectrometry was 35,822. Equilibrium velocity ultracentrifugation established that the protein existed as a monomer under native conditions with an apparent molecular weight of 33,795. Analysis of secondary structure of FbpA by circular dichroism showed 42.1% alpha helical structure. This protein is the second periplasmic iron-regulated protein described for P. haemolytica.
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PMID:Purification and characterization of the Pasteurella haemolytica 35 kilodalton periplasmic iron-regulated protein. 1106 79


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