Literature DB >> 8132353

Analysis of hydrolytic products from choline-labeled host cell phospholipids during growth of Rickettsia prowazekii.

H H Winkler1, L Day, R Daugherty.   

Abstract

A phospholipase activity has been associated with the interaction of Rickettsia prowazekii with the surface of erythrocytes and competent host cells as well as during the growth of the rickettsiae within their host cells. Both fatty acid and lysophosphatides have been found in the interaction of rickettsiae with the surface of eucaryotic cells; this finding provided strong evidence for the activity of a phospholipase A. However, fatty acids, but not lysophosphatides, were found during the growth of rickettsiae within cells in which the phospholipids had been radiolabeled with oleic acid; this observation left the type of phospholipase activity in doubt. In this study, the water-soluble components of phospholipid hydrolysis by phospholipase A plus lysophospholipase and phospholipase C were determined following the growth of rickettsiae in host cells in which the phospholipids had been radiolabeled with choline. In infected cells relative to mock-infected cells, there was a loss of phosphatidylcholine with a corresponding increase not in lysophosphatidylcholine but in the water-soluble components. There was a large increase in glycerylphosphorylcholine (185%) and a smaller increase in phosphorylcholine (16%). These results indicate that both phospholipase A activity (plus a lysophospholipase activity) and phospholipase C were increased during infection by R. prowazekii and that the former was the predominant activity.

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Year:  1994        PMID: 8132353      PMCID: PMC186302          DOI: 10.1128/iai.62.4.1457-1459.1994

Source DB:  PubMed          Journal:  Infect Immun        ISSN: 0019-9567            Impact factor:   3.441


  16 in total

Review 1.  Rickettsia species (as organisms).

Authors:  H H Winkler
Journal:  Annu Rev Microbiol       Date:  1990       Impact factor: 15.500

Review 2.  Rickettsia prowazekii and the host cell: entry, growth and control of the parasite.

Authors:  H H Winkler; J Turco
Journal:  Curr Top Microbiol Immunol       Date:  1988       Impact factor: 4.291

3.  Early events in the interaction of the obligate intracytoplasmic parasite, Rickettsia prowazekii, with eucaryotic cells: entry and lysis.

Authors:  H H Winkler
Journal:  Ann Inst Pasteur Microbiol (1985)       Date:  1986 May-Jun

4.  Penetration of host cells by Rickettsia rickettsii appears to be mediated by a phospholipase of rickettsial origin.

Authors:  D J Silverman; L A Santucci; N Meyers; Z Sekeyova
Journal:  Infect Immun       Date:  1992-07       Impact factor: 3.441

5.  Formation of diacylglycerol by a phospholipase D-phosphatidate phosphatase pathway specific for phosphatidylcholine in endothelial cells.

Authors:  T W Martin
Journal:  Biochim Biophys Acta       Date:  1988-10-14

6.  Analysis of the water-soluble products of phosphatidylcholine breakdown by ion-exchange chromatography. Bombesin and TPA (12-O-tetradecanoylphorbol 13-acetate) stimulate choline generation in Swiss 3T3 cells by a common mechanism.

Authors:  S J Cook; M J Wakelam
Journal:  Biochem J       Date:  1989-10-15       Impact factor: 3.857

7.  Effect of gamma interferon on phospholipid hydrolysis and fatty acid incorporation in L929 cells infected with Rickettsia prowazekii.

Authors:  H H Winkler; L Day; R Daugherty; J Turco
Journal:  Infect Immun       Date:  1993-08       Impact factor: 3.441

8.  Phospholipase A and the interaction of Rickettsia prowazekii and mouse fibroblasts (L-929 cells).

Authors:  H H Winkler; E T Miller
Journal:  Infect Immun       Date:  1982-10       Impact factor: 3.441

9.  Phospholipase A activity associated with the growth of Rickettsia prowazekii in L929 cells.

Authors:  H H Winkler; R M Daugherty
Journal:  Infect Immun       Date:  1989-01       Impact factor: 3.441

10.  Phospholipase A activity in the hemolysis of sheep and human erythrocytes by Rickettsia prowazeki.

Authors:  H H Winkler; E T Miller
Journal:  Infect Immun       Date:  1980-08       Impact factor: 3.441

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  3 in total

1.  The Rickettsia prowazekii ExoU homologue possesses phospholipase A1 (PLA1), PLA2, and lyso-PLA2 activities and can function in the absence of any eukaryotic cofactors in vitro.

Authors:  Nicole A Housley; Herbert H Winkler; Jonathon P Audia
Journal:  J Bacteriol       Date:  2011-07-15       Impact factor: 3.490

2.  pH and calcium dependence of hemolysis due to Rickettsia prowazekii: comparison with phospholipase activity.

Authors:  D M Ojcius; M Thibon; C Mounier; A Dautry-Varsat
Journal:  Infect Immun       Date:  1995-08       Impact factor: 3.441

3.  Wholly Rickettsia! Reconstructed Metabolic Profile of the Quintessential Bacterial Parasite of Eukaryotic Cells.

Authors:  Timothy P Driscoll; Victoria I Verhoeve; Mark L Guillotte; Stephanie S Lehman; Sherri A Rennoll; Magda Beier-Sexton; M Sayeedur Rahman; Abdu F Azad; Joseph J Gillespie
Journal:  mBio       Date:  2017-09-26       Impact factor: 7.867

  3 in total

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