Characterization of glycoconjugates and sialic acid modification in the olfactory bulb of the Chinese fire‐bellied newt (Cynops orientalis)

2020 ◽  
Vol 49 (2) ◽  
pp. 260-269
Author(s):  
Toshiyasu Matsui ◽  
Kazuyuki Komamoto ◽  
Hitomi Igarashi ◽  
Masamichi Kurohmaru
Cell Calcium ◽  
2021 ◽  
Vol 94 ◽  
pp. 102334
Author(s):  
Xin Su ◽  
Tamara Vasilkovska ◽  
Nicole Fröhlich ◽  
Olga Garaschuk

1985 ◽  
Vol 260 (8) ◽  
pp. 4941-4951
Author(s):  
D H Joziasse ◽  
M L Bergh ◽  
H G ter Hart ◽  
P L Koppen ◽  
G J Hooghwinkel ◽  
...  

Biochemistry ◽  
1972 ◽  
Vol 11 (14) ◽  
pp. 2559-2564 ◽  
Author(s):  
John F. Codington ◽  
Barbara H. Sanford ◽  
Roger W. Jeanloz

2021 ◽  
Author(s):  
Nageswari Yarravarapu ◽  
Rohit Sai Reddy Konada ◽  
Narek Darabedian ◽  
Nichole J. Pedowtiz ◽  
Soumya N. Krishnamurthy ◽  
...  

Glycan binding often mediates extracellular macromolecular recognition events. Accurate characterization of these binding interactions can be difficult because of dissociation and scrambling that occur during purification and analysis steps. Use of photocrosslinking methods has been pursued to covalently capture glycan-dependent interactions in situ however use of metabolic glycan engineering methods to incorporate photocrosslinking sugar analogs is limited to certain cell types. Here we report an exo-enzymatic labeling method to add a diazirine-modified sialic acid (SiaDAz) to cell surface glycoconjugates. The method involves chemoenzymatic synthesis of diazirine-modified CMP-sialic acid (CMP-SiaDAz), followed by sialyltransferase-catalyzed addition of SiaDAz to desialylated cell surfaces. Cell surface SiaDAz-ylation is compatible with multiple cell types and is facilitated by endogenous extracellular sialyltransferase activity present in Daudi B cells. This method for extracellular addition of α2-6-linked SiaDAz enables UV-induced crosslinking of CD22, demonstrating the utility for covalent capture of glycan-mediated binding interactions.


2014 ◽  
Vol 30 (S1) ◽  
pp. A119-A120
Author(s):  
Hung V. Trinh ◽  
Ousman Jobe ◽  
Guofen Gao ◽  
Carl R. Alving ◽  
Venigalla Rao ◽  
...  

Viruses ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 653
Author(s):  
Mario Mietzsch ◽  
Robert McKenna ◽  
Elina Väisänen ◽  
Jennifer C. Yu ◽  
Maria Ilyas ◽  
...  

Several members of the Protoparvovirus genus, capable of infecting humans, have been recently discovered, including cutavirus (CuV) and tusavirus (TuV). To begin the characterization of these viruses, we have used cryo-electron microscopy and image reconstruction to determine their capsid structures to ~2.9 Å resolution, and glycan array and cell-based assays to identify glycans utilized for cellular entry. Structural comparisons show that the CuV and TuV capsids share common features with other parvoviruses, including an eight-stranded anti-parallel β-barrel, depressions at the icosahedral 2-fold and surrounding the 5-fold axes, and a channel at the 5-fold axes. However, the viruses exhibit significant topological differences in their viral protein surface loops. These result in three separated 3-fold protrusions, similar to the bufaviruses also infecting humans, suggesting a host-driven structure evolution. The surface loops contain residues involved in receptor binding, cellular trafficking, and antigenic reactivity in other parvoviruses. In addition, terminal sialic acid was identified as the glycan potentially utilized by both CuV and TuV for cellular entry, with TuV showing additional recognition of poly-sialic acid and sialylated Lewis X (sLeXLeXLeX) motifs reported to be upregulated in neurotropic and cancer cells, respectively. These structures provide a platform for annotating the cellular interactions of these human pathogens.


1974 ◽  
Vol 140 (3) ◽  
pp. 557-560 ◽  
Author(s):  
Cesare Balduini ◽  
Carlo Luigi Balduini ◽  
Edoardo Ascari

Glycopeptides were extracted by papain digestion from old and young human erythrocyte membranes and fractionated on DEAE-Sephadex A-25. Chemical characterization of the unfractionated samples and of the main peak eluted from the column indicates that glycoproteins of the erythrocyte membrane undergo significant decreases in sialic acid and galactosamine content with aging.


2012 ◽  
Vol 354 ◽  
pp. 21-31 ◽  
Author(s):  
Davide Bini ◽  
Maria Gregori ◽  
Ugo Cosentino ◽  
Giorgio Moro ◽  
Angeles Canales ◽  
...  

1987 ◽  
Vol 33 (12) ◽  
pp. 2214-2219
Author(s):  
H Matsue ◽  
K Takagaki ◽  
K Honda ◽  
Y Nakagawa ◽  
F Gejyo ◽  
...  

Abstract We prepared human urinary glycopeptides from the supernatant liquid remaining after precipitation of the nondialyzable fraction with cetylpyridinium chloride. Using cation exchange and affinity chromatographies and gel filtration, we obtained 28 glycopeptide subfractions. By compositional analyses of sugar and amino acid, and by reducing-terminal analyses after reduction with NaBH4, we determined the size of the carbohydrate moiety and the types of carbohydrate-peptide linkage involved. We isolated several glycopeptides not previously described: six with sialic acid, two with fucose, two with glucose, and one with N-acetylgalactosamine. The sialic acid glycopeptides had a short carbohydrate chain of the O-glycoside type. The fucose-containing glycopeptides were fucosyllactosaminoglycans. The glucose glycopeptides were polymers linked to a small peptide moiety. The N-acetylgalactosamine-rich glycopeptide was found in an N-glycoside-type fraction, with N-acetylgalactosamine at the nonreducing terminal.


Sign in / Sign up

Export Citation Format

Share Document