scholarly journals Structural characterization of a novel glycosyl-phosphatidylinositol from the protozoan Tetrahymena mimbres

1991 ◽  
Vol 279 (2) ◽  
pp. 605-608 ◽  
Author(s):  
U Weinhart ◽  
J R Thomas ◽  
Y Pak ◽  
G A Thompson ◽  
M A J Ferguson

A glycolipid metabolically labelled with [14C]GlcN was isolated from the free-living protozoan Tetrahymena mimbres. The glycolipid was sensitive to a bacterial phosphatidylinositol-specific phospholipase C, and the headgroup was shown to contain a phosphorylated Man alpha 1-2Man alpha 1-4Man alpha 1-4GlcN glycan. The Tetrahymena glycolipid is structurally unique among the glycosylphosphatidylinositols that have so far been characterized, including those from several protozoan parasites of humans.

1991 ◽  
Vol 273 (2) ◽  
pp. 301-301 ◽  
Author(s):  
N M Hooper ◽  
S J Broomfield ◽  
A J Turner

Two polyclonal antisera were raised in rabbits to the phospholipase C-solubilized forms of pig renal dipeptidase (EC 3.4.13.11) and pig aminopeptidase P (EC 3.4.11.9). These antisera were purified and shown to cross-react with other glycosyl-phosphatidylinositol (G-PI)-anchored proteins isolated from pig, human and trypanosomes. The epitopes involved in this cross-reactivity were characterized by Western-blot analysis after mild acid or nitrous acid treatment of the G-PI-anchored proteins and by a competitive e.l.i.s.a. with other G-PI-anchored proteins and individual components of the anchor structure. These studies revealed that the primary epitope for both antisera is the inositol 1.2-(cyclic)monophosphate that is formed on phospholipase C cleavage of the intact G-PI anchor. Other minor epitopes, such as phosphoethanolamine, probably involve side-chain modifications to the core anchor structure that may be species-specific.


PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e53460 ◽  
Author(s):  
Daniela P. Almenara ◽  
Joselene P. de Moura ◽  
Cristiane P. Scarabotto ◽  
Russolina B. Zingali ◽  
Carlos E. Winter

Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.


2011 ◽  
Vol 44 (06) ◽  
Author(s):  
A Bracher ◽  
C Kozany ◽  
AK Thost ◽  
F Hausch

Planta Medica ◽  
2014 ◽  
Vol 80 (10) ◽  
Author(s):  
YH Wang ◽  
B Avula ◽  
N Abe ◽  
F Wei ◽  
M Wang ◽  
...  

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