Lipids of a T Strain of
            <i>Mycoplasma</i>

Romano, Nino; Smith, Paul F.; Mayberry, W. R.

doi:10.1128/jb.109.2.565-569.1972

Cited by 29 publications

(13 citation statements)

References 11 publications

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“…The propensity of ureaplasmas harvested after growth in vitro to be associated with noncellular materials from the growth medium has been previously observed (16,25,27). This has also been observed for some classical mycoplasmas and is known to influence the antigenic character (2,26,28) and the ability of the mycoplasmas to react in various diagnostic tests (4).…”

Section: Discussionmentioning

confidence: 70%

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Masover¹,

Razin²,

Hayflick³

1977

J Bacteriol

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Ureaplasma urealyticum cells were lysed by osmotic shock or by digitonin. The membrane fraction contained four to ten times as much protein as the cytoplasmic fraction. These values are in large excess of those reported for classical mycoplasmas, suggesting that the Ureaplasma membrane fraction was heavily contaminated with proteins derived from the growth medium. The U. urealyticum urease activity was localized in the cytoplasmic fraction, whereas the adenosine triphosphatase activity was localized in the membrane fraction. Significant urease activity could be detected also in nonviable cells. Urea, at concentrations above 0.25 M, was mycoplasmastatic to Acholeplasma laidlawii, Mycoplasma hominis, and U. urealyticum, so that the Ureaplasma urease did not afford preferential protection against urea toxicity. The intracellular localization of the urease would be expected to release ammonia from urea in the cytoplasm. The ammonia will take up protons to become ammonium ions. It can be hypothesized that the intracellular NH4+ plays a role in proton elimination or acid-base balance, which might be coupled to an energy producing ion gradient and/or transport mechanisms.

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Section: Discussionmentioning

confidence: 70%

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Masover¹,

Razin²,

Hayflick³

1977

J Bacteriol

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“…In A. modicum there is a greater concentration of the fully acylated glycerophosphoryl glycerophosphoryl glycerol than previously found in other mycoplasmas. Nevertheless, the phospholipids of this organism are not unique, in contrast to a T-strain (14) and A. axanthum (12).…”

Section: Discussionmentioning

confidence: 81%

Heptose-Containing Pentaglycosyl Diglyceride Among the Lipids of Acholeplasma modicum

1974

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A pentaglycosyl diglyceride with the tentative structure of galactosyl-galactosyl-mannoheptosyl-glucosyl-glucosyl diglyceride was found to be the major glycolipid in Acholeplasma modicum. The heptose is D-glycero-D-mannoheputose. The diglyceride-terminating moiety possesses the structure O-a-D-glucopyranosyl-(1 -2)-O-a-D-glucopyranosyl-sn-1, 2-diglyceride. Other glycolipids occurring in this organism are a diglucosyl diglyceride and a monoglucosyl diglyceride with structures identical to the terminal segments of the pentaglycosyl diglyceride. More fully acylated derivatives -f these two glycolipids also occur. The phospholipids are all of the glycerophosphoryl type. The neutral lipids are composed of diglycerides and four polyterpenes. The polyterpenes consist of both colored and colorless carotenoids and become radiolabeled with both ["C ]acetate and ["C ]mevalonate.on July 15, 2020 by guest

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“…All mycoplasmas appear to possess phosphatidyl glycerol (9,33,40,44,49,50,52). Mycoplasmas may disrupt the activity of pulmonary surfactant through interference with the metabolism of not only phosphatidyl glycerol but also the surfaceactive pulmonary component phosphatidyl ethanolamine (18,40) and the phospholipid precursor dihydroxyacetone (1,35). During infection, mycoplasmas might also interfere in the synthesis of PPL by lysophospholipase activity, which has been observed in another species, Acholeplasma laidlawii B (58,59).…”

Section: Discussionmentioning

confidence: 96%

“…Phosphatidyl glycerol presumably contributes to the in situ ability of pulmonary surfactant to lower surface tension (11,14,41); however, the magnitude of this contribution to surface activity is not clear, but it is less than that of PPL. All mycoplasmas appear to possess phosphatidyl glycerol (9,33,40,44,49,50,52). Mycoplasmas may disrupt the activity of pulmonary surfactant through interference with the metabolism of not only phosphatidyl glycerol but also the surfaceactive pulmonary component phosphatidyl ethanolamine (18,40) and the phospholipid precursor dihydroxyacetone (1,35).…”

Section: Discussionmentioning

confidence: 99%

Lecithin Changes in Murine Mycoplasma pulmonis Respiratory Infection

1979

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We examined the lipid content of bronchoalveolar (BA) washes from both mice and rats infected with Mycoplasma pulmonis, an etiological agent of murine pneumonia. During a 30-day period after intranasal inoculation, the total lipid content from infected and control rats (in milligrams per animal) remained relatively equal and unchanged. The saturated, unsaturated, and total lecithin contents in infected rats (in milligrams per animal) all increased. The maximum lecithin values were detected at 7 to 10 days after infection; later, the levels fell to control values. There was essentially no change in any lecithin value from uninfected animals. Although in BA washes from infected animals the mass of disaturated lecithins increased, the percentage of this fraction in the total lecithin pool decreased. The fatty acids of the lecithins from BA washes of infected mice had significantly less palmitic and significantly more oleic and linoleic acids than the lecithins isolated from the BA washes of control animals. Both the relative decrease in the mass of disaturated lecithins in the BA washes and the increase in the percentage of esterified unsaturated fatty acids in the lecithins may be directly related to the reduced lung function reported to occur during the course of murine M. pulmonis pneumonia.Excised lungs from rodents infected with a mycoplasma or influenza virus are more difficult to distend, i.e. have lower pulmonary compliance, than those from animals free of respiratory disease (22,53). There are two major determinants of lung compliance: surface tension at the air-tissue interface and elasticity of the lung tissue. In the case of these infections, the lower compliance was due primarily to increased surface tension rather than to changes in the elasticity of lung tissue. Loosli et al. (25) also have shown a decrease in the pulmonary surface properties of mice infected with influenza virus A.Pulmonary surfactant, a lipoprotein material which coats the alveolar walls, is responsible for decreasing surface tension at the air-tissue interface in lungs (31). By decreasing alveolar surface tension, surfactant reduces the work required to inflate the lungs. Surfactant also promotes alveolar stability at low lung volumes and minimizes pulmonary transcapillary pressure gradients (30). An increase in surface tension is reflected by a decrease in the compliance of the lungs.Klaus et al. (21) established that the active material in pulmonary surfactant is a phospholipid. The major active component has been identified as a disaturated lecithin, dipalmitoyl phosphatidylcholine (4,19,29,64). It is not clear whether other components of pulmonary surfactant contribute to the modification of surface forces occurring in situ or of those observed in experiments using alveolar washes (18,20,26,45). Several investigators have demonstrated a relationship between changes in lung compliance and either respiratory infection or altered lung surfactant, or both. Hakuno (13) found low surface activity and lowered levels of saturated fatty...

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Lipids of a T Strain of Mycoplasma

Cited by 29 publications

References 11 publications

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Heptose-Containing Pentaglycosyl Diglyceride Among the Lipids of Acholeplasma modicum

Lecithin Changes in Murine Mycoplasma pulmonis Respiratory Infection

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