Role of Glycolipids and Phosphatidylglycerol in the Serological Activity of
            <i>Mycoplasma pneumoniae</i>

Razin, Shmuel; Prescott, Benjamin; Caldes, George; James, Walter D.; Chanock, Robert M.

doi:10.1128/iai.1.4.408-416.1970

Cited by 44 publications

(23 citation statements)

References 21 publications

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“…However, the cross-reaction between A. axanthum and M. neurolyticum disappeared. M. neurolyticum 1 4 1,024 2 4 1,024 3 4 4,096 4 4 1,024 DISCUSSION The glycolipids of four of the five organisms were shown to behave as antigens in the complement-fixation reaction, as has been reported by others (6,7,10,11,13,17,18,20). In addition, the phosphoglycolipid of A. laidlawii also was competent in this serological reaction.…”

Section: Resultssupporting

confidence: 63%

Immunological Analysis of Glycolipids and Lipopolysaccharides Derived from Various Mycoplasmas

et al. 1974

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The lipids and lipopolysaccharides of five mycoplasmas were examined for complement-fixing activity to antimembrane rabbit sera. Total glycolipid fractions and the aqueous phenol fractions (lipopolysaccharides) from the membranes of Acholeplasma laidlawii, A. modicum, A. axanthum, and Mycoplasma neurolyticum exhibited significant antigenic activity. The glycolipids and phosphoglycolipids from Thermoplasma acidophilum were either anticomplementary or did not react due to their extreme hydrophobic nature. High activity was found using the lipopolysaccharide of T. acidophilum. The pure glycolipids and phosphoglycolipids of the Acholeplasma and Mycoplasma species also exhibited significant complement-fixing activity. Acylation of the sugar residues of these lipids reduced or negated complement-fixing activity. Double cross-reactions between the glycolipids of A. laidlawii and A. modicum appeared to be due to mono-and diglucosyl diglycerides of identical structure. Specificity of glycolipid structure was noted by the absence of cross-reactions between A. laidlawii and M. neurolyticum, the glycolipids of which differ only in the nature of the glucose linkages. The existence of lipopolysaccharides in the membranes of mycoplasmas and their complement-fixing activity in the presence of antimembrane sera suggest their possible importance as specific antigenic determinants.

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Section: Resultssupporting

confidence: 63%

Immunological Analysis of Glycolipids and Lipopolysaccharides Derived from Various Mycoplasmas

et al. 1974

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“…To begin characterization of the a t t a c h m e n t mechanism, monolayer cultures of radiolabeled mycoplasmas were exposed to specific enzymes to measure their influence on the subsequent host-parasite interaction. Crude lipase was initially employed because of its k n o w n effect on M. pneumoniae aggregates (14) and the a p p a r e n t existence of m e m b r a n e glycolipids on surfaces of M. pneumoniae (10,11).…”

Section: R E S U L T Smentioning

confidence: 99%

Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium.

Hu¹,

Collier²,

Baseman³

1977

The Journal of Experimental Medicine

194

152

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The mechanisms by which virulent microorganisms mediate host cell injury in respiratory tissue are unclear. To better understand the cellular and subcellular events which accompany these infections requires the establishment of experimental models which permit monitoring of the infectious process under experimentally controlled conditions. During the past several years we have examined the capacity of virulent Mycoplasma pneumoniae organisms, human pathogens of the respiratory tract, to parasitize and produce cell injury in the respiratory epithelium (1-4). Tracheal organ culture served as the highly sensitive host indicator system and its feasibility for other models is recognized (5-9). Based upon our earlier studies we outlined a two step parasitism: (a) the specific attachment of virulent M. pneumoniae via their tip-like organelle to a sialic acid-associated receptor region on the respiratory epithelium and (b) early abnormal host cell function at the transcriptional or translational levels with subsequent tissue cytopathology resulting from the colonization, multiplication, and continued metabolic activity of attached virulent mycoplasmas. The success of this parasitism appeared initially and critically dependent upon the intimate physical association between the membranes ofM. pneumoniae and respiratory epithelial cells. However, the chemical nature of M. pneumoniae surfaces responsible for attachment was unknown.Limited information is available concerning external membrane components of M. pneumoniae. Razin et al. (10,11) extracted from M. pneumoniae a glycolipid which reacts with complement-fixing and metabolic-and growth-inhibiting antibodies raised against intact organisms suggesting a possible surface location of the glycolipid moiety. Additional nonprotein haptens have been demonstrated in other mycoplasma species (12, 13). Boatman and Kenny (14) reported that spherules of M. pneumoniae organisms which form during growth can be disaggregated into individual and viable mycoplasmas by treatment with crude lipase. This observation implied that a lipid moiety on the surface of M. pneumoniae might be responsible for their "stickiness." Other studies with Mycoplasma hominis indicated that membrane proteins exist as receptors for the adsorption of HeLa cells (15) and for indirect hemagglutination activity (16). In this report we examine the unique interaction between virulent M. pneumo-

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“…analysis of Mycoplasma pneumoniae lipids (31). The polar lipid fraction eluted with chloroform-methanol (1: 1) comprised about 40% by weight of the total lipid.…”

Section: Vol 116 1973mentioning

confidence: 99%

Isolation, Chemical Composition, and Ultrastructural Features of the Cell Membrane of the Mycoplasma-Like Organism Spiroplasma citri

et al. 1973

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Thin sections of Spiroplasma citri, a mycoplasma-like organism isolated from citrus infected with "Stubborn" disease, showed the organisms to be limited by a single trilaminar plasma membrane. An additional outer layer could, however, be frequently seen in freeze-etched preparations of unwashed cells. The organisms were found to be extremely sensitive to lysis by osmotic shock. The cell membrane of S. citri isolated in this way resembled that of mycoplasmas in ultrastructure and gross chemical composition. The isolated membranes showed the characteristic trilaminar shape in section and the typical particle-studded fracture faces in freeze-etched preparations. Protein and lipid formed over 80% of the total dry weight of the membrane, which had a density of-1.180 g/cm3. Cholesterol constituted over 20% of the total membrane lipid. Phosphatidylglycerol, synthesized by the organisms, was the major phospholipid. Significant amounts of hexosamine (15 to 35 ,ug/mg of membrane protein) could be found in the membrane preparations. Our results support the thesis that S. citri does not possess a cell wall, either of the gram-positive or the gram-negative type, though it may be coated by some other type of an envelope or by a slime layer, at least temporarily.

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Role of Glycolipids and Phosphatidylglycerol in the Serological Activity of Mycoplasma pneumoniae

Cited by 44 publications

References 21 publications

Immunological Analysis of Glycolipids and Lipopolysaccharides Derived from Various Mycoplasmas

Immunological Analysis of Glycolipids and Lipopolysaccharides Derived from Various Mycoplasmas

Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium.

Isolation, Chemical Composition, and Ultrastructural Features of the Cell Membrane of the Mycoplasma-Like Organism Spiroplasma citri

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