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  1. Article ; Online: "Unique choline-containing phosphoglycolipids in Mycoplasma fermentans".

    Rottem, Shlomo

    Chemistry and physics of lipids

    2016  Volume 194, Page(s) 94–100

    MeSH term(s) Choline/chemistry ; Choline/metabolism ; Glycolipids/chemistry ; Glycolipids/metabolism ; Molecular Structure ; Mycoplasma fermentans/chemistry ; Mycoplasma fermentans/metabolism
    Chemical Substances Glycolipids ; Choline (N91BDP6H0X)
    Language English
    Publishing date 2016-01
    Publishing country Ireland
    Document type Journal Article ; Review
    ZDB-ID 213869-4
    ISSN 1873-2941 ; 0009-3084
    ISSN (online) 1873-2941
    ISSN 0009-3084
    DOI 10.1016/j.chemphyslip.2015.10.003
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  2. Article ; Online: Unique choline-containing phosphoglycolipids in Mycoplasma fermentans.

    Rottem, Shlomo

    Chemistry and physics of lipids

    2015  Volume 191, Page(s) 61–67

    MeSH term(s) Animals ; Apoptosis ; Arthritis, Rheumatoid/etiology ; Arthritis, Rheumatoid/microbiology ; Astrocytes/cytology ; Astrocytes/microbiology ; Calcium-Binding Proteins/metabolism ; Choline/metabolism ; Fatty Acids, Nonesterified/metabolism ; Humans ; Immune System ; Mycoplasma fermentans/metabolism ; Mycoplasma fermentans/physiology ; Phosphorylcholine/immunology ; Phosphorylcholine/metabolism ; Rats
    Chemical Substances Calcium-Binding Proteins ; Fatty Acids, Nonesterified ; Phosphorylcholine (107-73-3) ; calpastatin (79079-11-1) ; Choline (N91BDP6H0X)
    Language English
    Publishing date 2015-10
    Publishing country Ireland
    Document type Journal Article
    ZDB-ID 213869-4
    ISSN 1873-2941 ; 0009-3084
    ISSN (online) 1873-2941
    ISSN 0009-3084
    DOI 10.1016/j.chemphyslip.2015.07.016
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  3. Article ; Online: Novel synthetic lipopeptides derived from Mycoplasma hyorhinis upregulate calpastatin in SH-SY5Y neuroblastoma cells and induce a neuroprotective effect against amyloid-β-peptide toxicity.

    Kornspan, Jonathan D / Kosower, Nechama S / Vaisid, Tali / Katzhandler, Joshua / Rottem, Shlomo

    FEMS microbiology letters

    2020  Volume 367, Issue 10

    Abstract: Previously, we showed that contamination of SH-SY5Y neuroblastoma cells by Mycoplasma hyorhinis strains NDMh and MCLD leads to increased levels of calpastatin (the endogenous, specific inhibitor of the Ca2+-dependent protease calpain), resulting in ... ...

    Abstract Previously, we showed that contamination of SH-SY5Y neuroblastoma cells by Mycoplasma hyorhinis strains NDMh and MCLD leads to increased levels of calpastatin (the endogenous, specific inhibitor of the Ca2+-dependent protease calpain), resulting in inhibition of calpain activation. We have found that the increased calpastatin level is promoted by the lipoprotein fraction (MhLpp) of the mycoplasmal membrane. Here, we present MhLpp-based novel synthetic lipopeptides that induce upregulation of calpastatin in SH-SY5Y neuroblastoma cells, leading to protection of the treated cells against Ca2+/amyloid-β-peptide toxicity. These lipopeptides present a new class of promising agents against calpain-induced cell toxicity.
    MeSH term(s) Amyloid beta-Peptides/toxicity ; Calcium-Binding Proteins/genetics ; Cell Line, Tumor ; Drug-Related Side Effects and Adverse Reactions/prevention & control ; Humans ; Lipopeptides/chemical synthesis ; Lipopeptides/pharmacology ; Mycoplasma hyorhinis/chemistry ; Mycoplasma hyorhinis/genetics ; Neuroblastoma ; Neuroprotective Agents/pharmacology ; Up-Regulation/drug effects
    Chemical Substances Amyloid beta-Peptides ; Calcium-Binding Proteins ; Lipopeptides ; Neuroprotective Agents ; calpastatin (79079-11-1)
    Language English
    Publishing date 2020-04-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 752343-9
    ISSN 1574-6968 ; 0378-1097
    ISSN (online) 1574-6968
    ISSN 0378-1097
    DOI 10.1093/femsle/fnaa073
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  4. Article: Sterols and acylated proteins in mycoplasmas.

    Rottem, Shlomo

    Biochemical and biophysical research communications

    2002  Volume 292, Issue 5, Page(s) 1289–1292

    MeSH term(s) Acylation ; Bacterial Proteins/metabolism ; Cell Membrane/metabolism ; Mycoplasma/metabolism ; Sterols/metabolism
    Chemical Substances Bacterial Proteins ; Sterols
    Language English
    Publishing date 2002-04-19
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1006/bbrc.2001.2023
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  5. Article: Interaction of mycoplasmas with host cells.

    Rottem, Shlomo

    Physiological reviews

    2003  Volume 83, Issue 2, Page(s) 417–432

    Abstract: The mycoplasmas form a large group of prokaryotic microorganisms with over 190 species distinguished from ordinary bacteria by their small size, minute genome, and total lack of a cell wall. Owing to their limited biosynthetic capabilities, most ... ...

    Abstract The mycoplasmas form a large group of prokaryotic microorganisms with over 190 species distinguished from ordinary bacteria by their small size, minute genome, and total lack of a cell wall. Owing to their limited biosynthetic capabilities, most mycoplasmas are parasites exhibiting strict host and tissue specificities. The aim of this review is to collate present knowledge on the strategies employed by mycoplasmas while interacting with their host eukaryotic cells. Prominant among these strategies is the adherence of mycoplasma to host cells, identifying the mycoplasmal adhesins as well as the mammalian membrane receptors; the invasion of mycoplasmas into host cells including studies on the role of mycoplasmal surface molecules and signaling mechanisms in the invasion; the fusion of mycoplasmas with host cells, a novel process that raises intriguing questions of how microinjection of mycoplasma components into eukaryotic cells subvert and damage the host cells. The observations of diverse interactions of mycoplasmas with cells of the immune system and their immunomodulatory effects and the discovery of genetic systems that enable mycoplasmas to rapidly change their surface antigenic composition have been important developments in mycoplasma research over the past decade, showing that mycoplasmas possess an impressive capability of maintaining a dynamic surface architecture that is antigenically and functionally versatile, contributing to the capability of the mycoplasmas to adapt to a large range of habitats and cause diseases that are often chronic in nature.
    MeSH term(s) Animals ; Bacterial Adhesion ; Cell Fusion ; Humans ; Mycoplasma/cytology ; Mycoplasma/immunology ; Mycoplasma/pathogenicity ; Mycoplasma/physiology ; Mycoplasma Infections/immunology ; Mycoplasma Infections/physiopathology
    Language English
    Publishing date 2003-04
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 209902-0
    ISSN 1522-1210 ; 0031-9333
    ISSN (online) 1522-1210
    ISSN 0031-9333
    DOI 10.1152/physrev.00030.2002
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  6. Article: Choline-containing lipids in mycoplasmas.

    Rottem, Shlomo

    Microbes and infection

    2002  Volume 4, Issue 9, Page(s) 963–968

    Abstract: Choline-containing lipids were identified and characterized in the cell membrane of Mycoplasma fermentans and were shown to participate in the adhesion to the surface of eukaryotic cells, to stimulate mycoplasma fusion with eukaryotic cells, and to ... ...

    Abstract Choline-containing lipids were identified and characterized in the cell membrane of Mycoplasma fermentans and were shown to participate in the adhesion to the surface of eukaryotic cells, to stimulate mycoplasma fusion with eukaryotic cells, and to induce cytokine secretion by cells of the immune system. These findings suggest that choline-containing lipids are important mediators of tissue pathology in the infectious process caused by M. fermentans.
    MeSH term(s) Adhesins, Bacterial/chemistry ; Apoptosis ; Bacterial Adhesion ; Choline/analysis ; Choline/chemistry ; Glycolipids/chemistry ; Glycolipids/immunology ; Lipids/chemistry ; Molecular Structure ; Mycoplasma fermentans/chemistry ; Mycoplasma fermentans/pathogenicity
    Chemical Substances 6'-O-(3''-phosphocholine-2''-aminio-1'-phospho-1'',3''-propanediol)-glucopyranosyl-(1'-3')-1,2-diacylglycerol ; Adhesins, Bacterial ; Glycolipids ; Lipids ; Choline (N91BDP6H0X)
    Language English
    Publishing date 2002-07-09
    Publishing country France
    Document type Journal Article ; Review
    ZDB-ID 1465093-9
    ISSN 1769-714X ; 1286-4579
    ISSN (online) 1769-714X
    ISSN 1286-4579
    DOI 10.1016/s1286-4579(02)01622-2
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    Zs.A 5014: Show issues Location:
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  7. Article ; Online: The phospholipid profile of mycoplasmas.

    Kornspan, Jonathan D / Rottem, Shlomo

    Journal of lipids

    2012  Volume 2012, Page(s) 640762

    Abstract: The de novo synthesized polar lipids of Mycoplasma species are rather simple, comprising primarily of the acidic glycerophospholipids PG and CL. In addition, when grown in a medium containing serum, significant amounts of PC and SPM are incorporated into ...

    Abstract The de novo synthesized polar lipids of Mycoplasma species are rather simple, comprising primarily of the acidic glycerophospholipids PG and CL. In addition, when grown in a medium containing serum, significant amounts of PC and SPM are incorporated into the mycoplasma cell membrane although these lipids are very uncommon in wall-covered bacteria. The exogenous lipids are either incorporated unchanged or the PC incorporated is modified by a deacylation-acylation enzymatic cycle to form disaturated PC. Although their small genome, in some Mycoplasma species, other genes involved in lipid biosynthesis were detected, resulting in the synthesis of a variety of glycolipis, phosphoglycolipids and ether lipids. We suggest that analyses and comparisons of mycoplasma polar lipids may serve as a novel and useful tool for classification. Nonetheless, to evaluate the importance of polar lipids in mycoplasma, further systematic and extensive studies on more Mycoplasma species are needed. While studies are needed to elucidate the role of lipids in the mechanisms governing the interaction of mycoplasmas with host eukaryotic cells, the finding that a terminal phosphocholine containing glycolipids of M. fermentans serves both as a major immune determinants and as a trigger of the inflammatory responses, and the findings that the fusogenicity of M. fermentans with host cells is markedly stimulated by lyso-ether lipids, are important steps toward understanding the molecular mechanisms of M. fermentans pathogenicity.
    Language English
    Publishing date 2012-07-15
    Publishing country Egypt
    Document type Journal Article
    ZDB-ID 2582309-7
    ISSN 2090-3049 ; 2090-3049
    ISSN (online) 2090-3049
    ISSN 2090-3049
    DOI 10.1155/2012/640762
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  8. Article ; Online: Phospholipase A and glycerophosphodiesterase activities in the cell membrane of Mycoplasma hyorhinis.

    Kornspan, Jonathan D / Rottem, Shlomo

    FEMS microbiology letters

    2012  Volume 332, Issue 1, Page(s) 34–39

    Abstract: Mycoplasma hyorhinis, the major contaminant of tissue cultures, has been implicated in a variety of diseases in swine. Most human and animal mycoplasmas remain attached to the surface of epithelial cells. Nonetheless, we have recently shown that M. ... ...

    Abstract Mycoplasma hyorhinis, the major contaminant of tissue cultures, has been implicated in a variety of diseases in swine. Most human and animal mycoplasmas remain attached to the surface of epithelial cells. Nonetheless, we have recently shown that M. hyorhinis is able to invade and survive within nonphagocytic melanoma cells. The invasion process may require the damaging of the host cell membrane by either chemical, physical or enzymatic means. In this study, we show that M. hyorhinis membranes possess a nonspecific phospholipase A (PLA) activity capable of hydrolyzing both position 1 and position 2 of 1-acyl-2-(12-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)] aminododecanoyl) phosphatidylcholine. In silico analysis of the M. hyorhinis genome shows that the PLA of M. hyorhinis shares no homology to described phospholipases. The PLA activity of M. hyorhinis was neither stimulated by Ca (2+) nor inhibited by EGTA and had a broad pH spectrum. Mycoplasma hyorhinis also possess a potent glycerophosphodiesterase (GPD), which apparently cleaves the glycerophosphodiester formed by PLA to yield glycerol-3-phosphate. Possible roles of PLA and GPD in invading host eukaryotic cells and in forming mediators upon the interaction of M. hyorhinis with eukaryotic cells are suggested.
    MeSH term(s) 4-Chloro-7-nitrobenzofurazan/analogs & derivatives ; 4-Chloro-7-nitrobenzofurazan/metabolism ; Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Cell Membrane/enzymology ; Fluorescent Dyes ; Hydrolysis ; Molecular Sequence Data ; Mycoplasma hyorhinis/cytology ; Mycoplasma hyorhinis/enzymology ; Phosphatidylcholines/metabolism ; Phospholipases A/chemistry ; Phospholipases A/metabolism ; Phosphoric Diester Hydrolases/chemistry ; Phosphoric Diester Hydrolases/metabolism ; Sequence Alignment
    Chemical Substances Bacterial Proteins ; Fluorescent Dyes ; Phosphatidylcholines ; 1-oleoyl-2-(12-((7-nitro-2,1,3-benzoxadiazol-4-yl)amino)dodecanoyl)phosphatidylcholine (131479-28-2) ; Phospholipases A (EC 3.1.1.32) ; Phosphoric Diester Hydrolases (EC 3.1.4.-) ; glycerophosphodiester phosphodiesterase (EC 3.1.4.46) ; 4-Chloro-7-nitrobenzofurazan (EQF2794IRE)
    Language English
    Publishing date 2012-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 752343-9
    ISSN 1574-6968 ; 0378-1097
    ISSN (online) 1574-6968
    ISSN 0378-1097
    DOI 10.1111/j.1574-6968.2012.02571.x
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  9. Article ; Online: Mycoplasma gallisepticum inactivated by targeting the hydrophobic domain of the membrane preserves surface lipoproteins and induces a strong immune response.

    Atalla, Hazem / Lysnyansky, Inna / Raviv, Yossef / Rottem, Shlomo

    PloS one

    2015  Volume 10, Issue 3, Page(s) e0120462

    Abstract: An innovative approach for inactivation of Mycoplasma gallisepticum using the hydrophobic photoinduced alkylating probe 1, 5-iodonaphthylazide (INA) is described. Treatment of washed M. gallisepticum mid-exponential culture (0.2 mg cell protein /mL) with ...

    Abstract An innovative approach for inactivation of Mycoplasma gallisepticum using the hydrophobic photoinduced alkylating probe 1, 5-iodonaphthylazide (INA) is described. Treatment of washed M. gallisepticum mid-exponential culture (0.2 mg cell protein /mL) with INA followed by irradiation with far-ultraviolet light (310-380 nm) completely abolished viability. Transmission electron microscopy showed that the majority of the inactivated M. gallisepticum were comparable in size to intact cells, but that part of the INA-treated M. gallisepticum preparation also contained low density cells and membrane vesicles. Confocal microscopy revealed that untreated M. gallisepticum cells were internalized by chicken red blood cells (c-RBCs), whereas the INA-inactivated cells remained attached to the outer surface of the c-RBCs. INA treatment of M. gallisepticum resulted in a complete inactivation of F0F1 -ATPase and of the L-arginine uptake system, but the cytoplasmatic soluble NADH2 dehydrogenase was only partially affected. Western blot analysis of the lipoprotein fraction showed that the INA-treated M. gallisepticum retained their lipoproteins. Following subcutaneous injection of M. gallisepticum INA-bacterin, 100% and 68.8% of chickens were positive by the rapid serum agglutination test and enzyme-linked immunosorbent assay respectively, 2 weeks post-injection. These data suggest that the photoinducible alkylating agent INA inactivates M. gallisepticum but preserves its surface lipoproteins and thus has the potential to be used as a general approach for the inactivation of mycoplasmas for vaccine development.
    MeSH term(s) Animals ; Bacterial Proteins/chemistry ; Bacterial Proteins/immunology ; Bacterial Vaccines/chemistry ; Bacterial Vaccines/immunology ; Chickens/immunology ; Hydrophobic and Hydrophilic Interactions ; Lipoproteins/chemistry ; Lipoproteins/immunology ; Male ; Mycoplasma gallisepticum/chemistry ; Mycoplasma gallisepticum/immunology ; Protein Structure, Tertiary
    Chemical Substances Bacterial Proteins ; Bacterial Vaccines ; Lipoproteins
    Language English
    Publishing date 2015
    Publishing country United States
    Document type Journal Article
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0120462
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  10. Article ; Online: The Phospholipid Profile of Mycoplasmas

    Jonathan D. Kornspan / Shlomo Rottem

    Journal of Lipids, Vol

    2012  Volume 2012

    Keywords Physiology ; QP1-981 ; Science ; Q ; DOAJ:Physiology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences ; Biochemistry ; QD415-436 ; Organic chemistry ; QD241-441 ; Chemistry ; QD1-999 ; DOAJ:Biochemistry ; DOAJ:Life Sciences
    Language English
    Publishing date 2012-01-01T00:00:00Z
    Publisher Hindawi Publishing Corporation
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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