MORPHOLOGICAL, CHEMICAL, AND SEROLOGICAL STUDIES OF THE CELL WALLS OF<i>RICKETTSIA MOOSERI</i>

Schaechter, Moselio; Tousimis, A. J.; Cohn, Zanvil A.; Rosen, Harvey M.; Campbell, Jennifer; Hahn, Fred E.

doi:10.1128/jb.74.6.822-829.1957

Cited by 32 publications

(19 citation statements)

References 26 publications

(19 reference statements)

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“…The plasma membrane shown in the present study to be a consistent feature of R. quintana has so far been described only in R. tsutsugamushi (Schaechter et al, 1957). Although this difference might be ascribed to species variation in basic structure, it seems more likely that it results from the differences in the techniques used to prepare rickettsiae for electron microscopy.…”

Section: Ncontrasting

confidence: 53%

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Fine Structure of Rickettsia quintana Cultivated In Vitro and in the Louse

Ito

Vinson

1965

J Bacteriol

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structure of Rickettsia quintana cultivated in vitro and in the louse. J. Bacteriol. 89: 481-495. 1965.-Usually rod-shaped, Rickettsia quintana cells measure about 0.2 to 0.5 , wide and up to 1.6 IA long. The rickettsiae have both an outer cell wall, about 80 A thick, and a plasma membrane, about 70 A thick, each of which is trilaminar. Occasional vesicular invaginations of the plasma membrane occur. The nuclear material, distributed in irregular zones throughout the cytoplasm, appears as a loose network of fine fibrils when postfixed with uranyl acetate and as thick strands or clumps after routine OS04 fixation. The cytoplasm is densely packed with numerous granules, presumably ribosomes, about 150 A in diameter. Histochemical studies revealed the presence of both ribonucleic and deoxyribonucleic acids. During binary fission, a constricting furrow is formed by the cell wall and plasmalemma. No difference in fine structure was observed between R. quintana propagated on cell-free media and in the louse. Rickettsiae constitute a grotul) of microorganisms regarded as intermediate between bacteria and viruses. Although their morphological and physiological characteristics more closely resemble those of certain bacteria, they depend, like viruses, on living host cells for their multiplication. With the exception of Rickettsia quintana, rickettsiae are obligatory intracellular parasites. R. quintana, the etiological agent of trench fever, multiplies extracellularly in the gut of its arthropod vector, Pediculus humanus var. corporis (Wolbach, Todd, and Palfrey, 1922); and, recently, Vinson and Fuller (1961) and Vinson, Varela, and Molina (in preparation) reported the cultivation of R. quintana on cell-free media, as well as in lice, in cells cultivated in vitro, and in the yolk sac of the developing chick embryo. Although studies on the fine structure of several rickettsiae have been reported by various investigators (

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Section: Ncontrasting

confidence: 53%

“…The chemical composition of rickettsial cell walls has been found to resemble bacterial cell walls and contain amino acids and polysaccharides (Moulder, 1962;Schaechter et al, 1957).…”

Section: Nmentioning

confidence: 99%

Fine Structure of Rickettsia quintana Cultivated In Vitro and in the Louse

Ito

Vinson

1965

J Bacteriol

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“…Intrinsic labeling of carbohydrates. The cell envelope fraction of typhus group rickettsiae contains carbohydrates comprised of several sugars, including galactose (16,22), and it was of Co-electrophoresis of R. prowazekii proteins labeled with tyrosine or amino acids. Symbols: 0, [3HWtyrosine; *, "C-labeled amino acids.…”

Section: Resultsmentioning

confidence: 99%

Surface proteins of typhus and spotted fever group rickettsiae

Osterman¹,

Eisemann²

1978

Infect Immun

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Six proteins, previously established as major constituents of intact organisms were identified in cell envelopes obtained from intrinsically radiolabeled Rickettsia prowazekii. Extrinsic radioiodination of intact organisms conducted at 0.5 !LM iodide indicated that protein 4 was the most peripheral, although protein 1 also had reactive groups exposed on the surface of the organisms. A 10-fold increase in iodide concentration resulted in labeling of protein 2, and at 50 ,uM iodide, all six major proteins were radiolabeled. Similar selective labeling was not achieved with R. conorii. Analysis of both typhus and spotted fever group organisms radiolabeled with galactose suggested that carbohydrate was associated with proteins 1, 3, and 4. Typhus soluble antigen included all major proteins except protein 2, which remained attached to particulate rickettsiae after ether extraction. Protein 4 appeared to be prominent in the surface topography of R. prowazekii, was a component of soluble antigen and may have an important role in rickettsiae-host interactions.

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“…Bands 1 and 2 of soluble antigen have identical electropherograms. They each consist of nine proteins corresponding to proteins 2, 3, 5,6,12,19,26,28, and 29 of the whole cell. Band 3, which consists of partially disintegrated cells, has all the proteins present in whole cells.…”

Section: Methodsmentioning

confidence: 99%

Origin and Structure of the Group-Specific, Complement-Fixing Antigen of Rickettsia rickettsii

Tzianabos

Palmer

Obijeski

et al. 1974

Applied Microbiology

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Rickettsia rickettsii was treated with ether and examined by negative-contrast electron microscopy. Group-specific complement-fixing antigen was seen to be originating from the cell wall. The antigen was composed predominately of round particles 10 to 60 nm in diameter. Intact R. rickettsii and antigen from ether-treated organisms were purified by density gradient centrifugation and analyzed by polyacrylamide gel electrophoresis. The whole rickettsial cell was composed of a minimum of 30 proteins which ranged in molecular weight from about 23,000 to 155,000. The "soluble" antigen contained nine proteins ranging in molecular weight from about 28,000 to 150,000.

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MORPHOLOGICAL, CHEMICAL, AND SEROLOGICAL STUDIES OF THE CELL WALLS OFRICKETTSIA MOOSERI

Cited by 32 publications

References 26 publications

Fine Structure of Rickettsia quintana Cultivated In Vitro and in the Louse

Fine Structure of Rickettsia quintana Cultivated In Vitro and in the Louse

Surface proteins of typhus and spotted fever group rickettsiae

Origin and Structure of the Group-Specific, Complement-Fixing Antigen of Rickettsia rickettsii

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