Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0032285 (pneumonia)
54,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proteolytic activation of Sendai virus in the lungs of mice is necessary to cause pneumopathogenicity. Using Sendai virus-infected lung block cultures, protease inhibitors were tested for their antiviral effect by examining inhibition of proteolytic activation. Among the inhibitors tested, a serine protease, aprotinin, was shown to be most effective. In vivo protection experiments demonstrated that aprotinin, when administered intranasally, could confer protection on mice against lethal Sendai virus pneumonia through the same mechanism as observed in the in vitro system. The present study provides an experimental basis for the use of protease inhibitors as antiviral drugs.
J Gen Virol 1991 Apr
PMID:Protection of mice by a protease inhibitor, aprotinin, against lethal Sendai virus pneumonia. 170 50

The complete nucleotide sequence of gene 3 of pneumonia virus of mice has been determined, and the 5' end of the mRNA mapped using a modification of the polymerase chain reaction technique. The gene contains a single open reading frame, beginning with a 5'-proximal AUG initiation codon, encoding a polypeptide with a predicted Mr of 43141. Expression of the gene 3 protein in Escherichia coli and in vitro showed that it reacted with virus-specific antiserum and comigrated with the major nucleocapsid (N) polypeptide. The predicted amino acid sequence has extensive identity with that of the N protein of human respiratory syncytial virus. Comparisons with the amino acid sequences of N proteins of other paramyxoviruses, vesicular stomatitis virus and Ebola virus suggest that these proteins may have retained much of the same structure. These regions of conserved structure would most likely have the common functions of RNA binding and protein/protein interactions in the virus nucleocapsid.
J Gen Virol 1991 Mar
PMID:Sequence of the major nucleocapsid protein gene of pneumonia virus of mice: sequence comparisons suggest structural homology between nucleocapsid proteins of pneumoviruses, paramyxoviruses, rhabdoviruses and filoviruses. 184 2

Genes 1 and 2 of pneumonia virus of mice (PVM) consist of 410 and 571 nucleotides and encode proteins of 113 and 156 amino acids respectively. The proteins show no extensive (gene 1 analogous to 1C) or low (gene 2 analogous to 1B) homology to their presumed counterparts in human respiratory syncytial virus (HRSV). The strongest homology is between regions of approximately 35 amino acids located near the carboxy termini of the gene 2 product and the 1B protein with 29% identity, although a lower level of homology can be detected throughout much of these proteins (18% identity overall). These observations contrast with the conservation of 1C and 1B proteins between subgroups of HRSV and with the conservation of nucleocapsid proteins between HRSV and PVM.
J Gen Virol 1991 Oct
PMID:Genes 1 and 2 of pneumonia virus of mice encode proteins which have little homology with the 1C and 1B proteins of human respiratory syncytial virus. 191 30

Pulmonary A2 strain respiratory syncytial virus infection of BALB/c laboratory mice persisted for up to 7 days after initial infection with peak virus titres being recovered on day 4. Virus antigen within the lungs was found to be restricted essentially to the alveolar regions. Similarly, pulmonary histopathological changes remained confined to the peri-alveolar regions being consistent with mild pneumonia. Infection was found to elicit a pulmonary major histocompatibility complex-restricted cytotoxic T lymphocyte (CTL) response which was first detectable 6 days after infection and optimal 7 to 9 days after infection. This local CTL response was preceded by a rapid transient virus-specific lymphocyte transformation response which was detectable only 3 days after intranasal infection. In addition, infection induced rapid interferon production within the lungs which was accompanied by an equally rapid rise in pulmonary natural killer (NK) cell cytotoxic activity. Enhanced NK cell cytotoxicity could be detected after only 1 day post-infection and continued to rise to maximum levels on day 3. This response like the acute CTL response was found to be restricted to the lower respiratory tract. IgG was the first class of virus-specific immunoglobulin to be detected in the lungs of infected animals after experimental infection. However, IgG was not detected until day 10 post-infection, 5 days after the initial decline of virus shedding. Virus-specific IgA although detectable did not appear in the lung until day 24.
J Gen Virol 1990 Jul
PMID:Analysis of the local and systemic immune responses induced in BALB/c mice by experimental respiratory syncytial virus infection. 219 71

Antigenic relatedness between the virion-associated proteins of caprine arthritis-encephalitis, visna and progressive pneumonia viruses was examined. Antigenic cross-reactivity was assessed by immunoprecipitation of disrupted, radiolabelled virus with goat, sheep and rabbit antisera, followed by resolution of the immunoprecipitation products by SDS-polyacrylamide gel electrophoresis. The results indicate that antigenic cross-reactivity between the caprine and ovine virus isolates involves all of the major virion-associated proteins and glycoproteins. The common antigenic determinants exhibited by virion structural proteins are immunogenic in goats, sheep and rabbits.
J Gen Virol 1985 Jun
PMID:Antigenic cross-reactivity between caprine arthritis-encephalitis, visna and progressive pneumonia viruses involves all virion-associated proteins and glycoproteins. 240 23

The p28 core polypeptides of four isolates of caprine arthritis-encephalitis virus (CAEV) from goats was compared with those of visna virus (VV) and progressive pneumonia virus (PPV) from sheep. Monoclonal antibodies recognized p28 epitopes common to all six retrovirus isolates, a p28 epitope on four CAEV isolates, but not VV and PPV isolates, a p28 epitope on four CAEV isolates and VV, but not PPV and a p28 epitope unique to the CAEV isolate used for immunizing the mouse spleen donor. Comparison of two-dimensional maps of tyrosine containing tryptic peptides of p28 demonstrated that three CAEV isolates had similar maps while a fourth CAEV isolate, VV and PPV had several different from the three closely related CAEV p28s and from each other.
J Gen Virol 1987 Aug
PMID:Antigenic and structural variation of the p28 core polypeptide of goat and sheep retroviruses. 244 Sep 85

Mycoplasma pneumoniae was isolated for first time in Panama and identified from a nine years old girl with pneumonia. SP4 medium was used to isolate the bacteria. Confirmatory serological results were obtained by indirect immunofluorescence and were also suggested by the presence of cryoagglutinins in the sera of this patient. DNA hybridization tests (Gen--Probe) were carried out.
...
PMID:[The first isolation of Mycoplasma pneumoniae in Panama]. 250 60

A murine polyclonal antiserum and monoclonal antibodies have been employed to identify pneumonia virus of mice (PVM) polypeptides in infected cells and to study post-translational modifications. Immunoprecipitation experiments using a murine polyclonal antiserum and a monoclonal antibody directed against a 39K protein have established an antigenic relationship between two PVM proteins and the N and P proteins of human respiratory syncytial virus. Although 20 virus-specific polypeptides have been identified in lysates of infected cells, evidence is presented that some of these are related and that the number of unique polypeptides probably does not exceed 11 or 12. The phosphoproteins of PVM have a pattern of mobilities more like that of the recently described pneumovirus causing rhinotracheitis in turkeys than that of human or bovine respiratory syncytial virus.
J Gen Virol 1989 Jun
PMID:Polypeptides of pneumonia virus of mice. I. Immunological cross-reactions and post-translational modifications. 273 19

The kinetics of synthesis and the nature of the oligosaccharides of the glycoproteins of pneumonia virus of mice (PVM) were studied. Tryptic peptide mapping showed that the two major glycosylated polypeptides G1 and G2 were different forms of the same protein. G2 was derived from G1 which in turn appeared to be derived from an unidentified precursor. The G1/G2 protein of PVM is probably a haemagglutinin since a monoclonal antibody directed against it has a high haemagglutination inhibition titre. On the basis of experiments with inhibitors and glycosidases it was deduced that G1 and G2 have both N-linked and O-linked oligosaccharides. The putative fusion protein-equivalent of PVM was shown to possess N-linked oligosaccharides. In the presence of tunicamycin a high mobility form (F1t) appeared to be derived from a precursor (F0t) with the same mobility as the fully glycosylated protein. If by analogy with other paramyxoviruses this represents a cleavage event, the difference in mobility of the precursor and product suggests that the putative F2 product is smaller than the corresponding F2 protein of other paramyxoviruses. However, no F2 candidate protein was detected and evidence for an F1,2 dimer was inconclusive. The glycoproteins of PVM resemble those of respiratory syncytial virus in terms of their pattern of glycosylation, but differ in their processing.
J Gen Virol 1989 Jun
PMID:Polypeptides of pneumonia virus of mice. II. Characterization of the glycoproteins. 273 20

The authors evaluated the financial and health implications of treatment choices for three serious classes of infection: hospital-acquired pneumonia, intra-abdominal infection, and sepsis of unknown origin. Data were obtained from a systematic review of clinical literature and published data bases, by written questionnaire from a panel of infectious disease authorities, and from actual costs at a tertiary-care hospital. For pneumonia and sepsis, the third-generation cephalosporin evaluated (ceftizoxime) was found to be less expensive than other regimens, when costs of dose preparation and administration, monitoring, and toxicity were added to drug acquisition costs. The lowest-cost regimen for intra-abdominal infection was metronidazole plus gentamicin. Modest differences in efficacy would easily outweigh differences in toxicity, however, and could justify the use of more expensive regimens (e.g., mezlocillin plus gentamicin for hospital-acquired pneumonia, and cefoxitin plus gentamicin for intra-abdominal infection). If all regimens are assumed to be equally efficacious, then the third-generation cephalosporin was both lowest in cost and, owing to its low toxicity, greatest in net health benefit.
J Gen Intern Med
PMID:Cost-effective choice of antimicrobial therapy for serious infections. 309 40


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