scholarly journals Preservation Evaluation of Mycoplasma fermentans in Different Conditions

2020 ◽  
Vol 9 (02) ◽  
pp. 24-27
Author(s):  
Rivera A. ◽  
Rodriguez-Preval N ◽  
Giono-Cerezo S ◽  
Sanchez-Hernandez JA
Keyword(s):  
Mycoplasma Fermentans

A model of the deciliation process caused by Mycoplasma fermentans strain incognitus on respiratory epithelium

Scanning ◽  
2006 ◽  
Vol 28 (4) ◽  
pp. 212-218 ◽  
Author(s):  
Christian T. K.-H. Stadtländer
Keyword(s):  
Respiratory Epithelium ◽  
Mycoplasma Fermentans

Detection of Mycoplasma fermentans in human saliva with a polymerase chain reaction-based assay

1996 ◽  
Vol 41 (3) ◽  
pp. 311-314 ◽  
Author(s):  
Marianne in Chinghingyong ◽  
Christopher V. Hughes
Keyword(s):  
Polymerase Chain Reaction ◽  
Human Saliva ◽  
Chain Reaction ◽  
Mycoplasma Fermentans ◽  
Polymerase Chain

scholarly journals Identification and Functional Mapping of the Mycoplasma fermentans P29 Adhesin

2002 ◽  
Vol 70 (9) ◽  
pp. 4925-4935 ◽  
Author(s):  
Spencer A. Leigh ◽  
Kim S. Wise
Keyword(s):  
Disulfide Bond ◽  
Hela Cells ◽  
Mammalian Cells ◽  
Flow Cytometric Analysis ◽  
Phase Variation ◽  
Surface Proteins ◽  
Mycoplasma Species ◽  
Phase Variable ◽  
Binding Region ◽  
Mycoplasma Fermentans

ABSTRACT Initial adherence interactions between mycoplasmas and mammalian cells are important for host colonization and may contribute to subsequent pathogenic processes. Despite significant progress toward understanding the role of specialized, complex tip structures in the adherence of some mycoplasmas, particularly those that infect humans, less is known about adhesins through which other mycoplasmas of this host bind to diverse cell types, even though simpler surface components are likely to be involved. We show by flow cytometric analysis that a soluble recombinant fusion protein (FP29), representing the abundant P29 surface lipoprotein of Mycoplasma fermentans, binds human HeLa cells and inhibits M. fermentans binding to these cells, in both a quantitative and a saturable manner, whereas analogous fusion proteins representing other mycoplasma surface proteins did not. Constructs representing nested N- or C-terminal truncations of FP29 allowed initial mapping of this specific adherence function to a central region of the P29 sequence containing a 36-amino-acid disulfide loop. A derivative of FP29 containing a mutation converting one participating Cys to Ser, precluding intrachain disulfide bond formation, retained full activity. Together these results suggest that the direct interaction of M. fermentans with a ligand on the HeLa cell surface involves a limited segment of the P29 surface lipoprotein and requires neither the disulfide bond nor the contribution of adjacent portions of the protein. Earlier results indicating phase-variable display of monoclonal antibody surface epitopes on P29, now recognized to be outside this ligand binding region, raise the possibility that variation of mycoplasma surface architecture might alter the presentation of the binding region and the adherence phenotype. Preliminary results further indicated that FP29 could inhibit binding to HeLa cells by Mycoplasma hominis, a distinct human mycoplasma species displaying the phase-variable adhesin Vaa, but not that by Mycoplasma capricolum, an organism infecting caprine species. This result raises the additional, testable possibility that a common host cell ligand for two human mycoplasma species may be recognized through structurally dissimilar adhesins that undergo phase variation by two distinct mechanisms, governing protein expression (Vaa) or surface masking (P29).

Characterization of MHC Induction by Mycoplasma fermentans (Incognitus Strain)

1993 ◽  
Vol 152 (1) ◽  
pp. 261-270 ◽  
Author(s):  
P.Michael Stuart ◽  
Rita M. Egan ◽  
Jerold G. Woodward
Keyword(s):  
Mycoplasma Fermentans

scholarly journals Variation of Genes Encoding GGPLs Syntheses among Mycoplasma fermentans Strains

2010 ◽  
Vol 72 (6) ◽  
pp. 805-808 ◽  
Author(s):  
Masatoshi FUJIHARA ◽  
Noriko ISHIDA ◽  
Kozo ASANO ◽  
Kazuhiro MATSUDA ◽  
Nobuo NOMURA ◽  
...  
Keyword(s):  
Mycoplasma Fermentans ◽  
Genes Encoding

Mycoplasma fermentans in acute Crohn’s Disease. A preliminary report of a putative aetio-pathogenic agent*

2021 ◽  
Author(s):  
William E. Roediger ◽  
Adrian Cummins ◽  
Jennie Burke ◽  
Ross Philpot
Keyword(s):  
Crohn’S Disease ◽  
Crohn's Disease ◽  
Preliminary Report ◽  
Mycoplasma Fermentans ◽  
Pathogenic Agent

Abstract The authors have requested that this preprint be removed from Research Square.

Mycoplasma fermentans (Incognitus Strain) Cells Are Able to Fuse with T Lymphocytes

1993 ◽  
Vol 17 (Supplement_1) ◽  
pp. S305-S308 ◽  
Author(s):  
D. S. Dimitrov ◽  
G. Franzoso ◽  
M. Salman ◽  
R. Blumenthal ◽  
M. Tarshis ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Mycoplasma Fermentans

scholarly journals Ether lipids in the cell membrane of Mycoplasma fermentans

2000 ◽  
Vol 267 (20) ◽  
pp. 6276-6286 ◽  
Author(s):  
Frauke Wagner ◽  
Shlomo Rottem ◽  
Heinz-Dieter Held ◽  
Stefan Uhlig ◽  
Ulrich Zähringer
Keyword(s):  
Cell Membrane ◽  
Ether Lipids ◽  
Mycoplasma Fermentans

An evaluation of PCR methods to detect strains of Mycoplasma fermentans

Biologicals ◽  
2008 ◽  
Vol 36 (2) ◽  
pp. 117-121 ◽  
Author(s):  
Baharak Afshar ◽  
David Pitcher ◽  
Robin A.J. Nicholas ◽  
Roger J. Miles
Keyword(s):  
Mycoplasma Fermentans
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