Interaction of the C-polysaccharide ofStreptococcus pneumoniaewith the receptor asialo-GM1

1996 ◽  
Vol 21 (4) ◽  
pp. 223-234 ◽  
Author(s):  
Marianne Sundberg-Kövamees ◽  
T. Holme ◽  
AnnMargret Sjögren
Keyword(s):  
Asialo Gm1

scholarly journals The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kenichi Kamata ◽  
Kenji Mizutani ◽  
Katsuya Takahashi ◽  
Roberta Marchetti ◽  
Alba Silipo ◽  
...  
Keyword(s):  
Immune System ◽  
Sialic Acid ◽  
Ligand Binding ◽  
Steric Hindrance ◽  
Sequence Similarity ◽  
Binding Assays ◽  
Subunit Interface ◽  
Nmr Techniques ◽  
And Control ◽  
Asialo Gm1

AbstractSeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac$$\alpha$$ α (2-3)Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the $$\beta$$ β -trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1.

scholarly journals Titration of serum anti-ganglioside antibodies in patients with chronic medular injury previous to treatment with GM1 ganglioside

2003 ◽  
Vol 11 (2) ◽  
pp. 69-71
Author(s):  
Tarcísio Eloy Pessoa Barros Filho ◽  
Ciro da Silva Filho
Keyword(s):  
Spinal Cord ◽  
Spinal Cord Injury ◽  
Side Effects ◽  
Spinal Cord Lesion ◽  
Gm1 Ganglioside ◽  
Chronic Spinal Cord Injury ◽  
Cord Injury ◽  
Ganglioside Antibodies ◽  
Asialo Gm1 ◽  
Cord Lesion

Anti-ganglioside serum titers were evaluated by ELISA in 150 patients with complete spinal cord lesion for 6 to 12 months (IgG monosialo GM1, IgM monosialo GM1, IgG asialo GM1, IgM asialo GM1, IgG disialo GD1b e IgM disialo GD1b) prior to treatment with GM1 100 mg/day i.m. Only 4 patients showed positive titers for anti-asialo-GM1 (IgM) antibodies . All patients were clinically examined during and after treatment. No important side effects were observed with GM1 therapy. These results suggest that GM1-ganglioside administration in patients with chronic spinal cord injury is safe.

Presence of Asialo GM1 and Glucosylcerainide in the Intestinal Mucosa of Mice and Induction of Fucosyl Asialo GM1 by Conventionalization of Germ-Free Mice1

1981 ◽  
Vol 90 (6) ◽  
pp. 1731-1738 ◽  
Author(s):  
Yoshiniori UMESAKI ◽  
Akemi SUZUKI ◽  
Takeshi KASAMA ◽  
Kiyoshi TOHYAMA ◽  
Masahiko MUTAI ◽  
...  
Keyword(s):  
Intestinal Mucosa ◽  
Germ Free ◽  
Asialo Gm1

ACCELERATION OF METASTATIC GROWTH IN ANTI-ASIALO GM1-TREATED MICE

1982 ◽  
pp. 1331-1337 ◽  
Author(s):  
E. Gorelik ◽  
R. Wiltrout ◽  
K. Okumura ◽  
S. Habu ◽  
R.B. Herberman
Keyword(s):  
Metastatic Growth ◽  
Asialo Gm1

Specific interaction of peanut agglutinin with the glycolipid asialo GM1

FEBS Letters ◽  
1982 ◽  
Vol 141 (1) ◽  
pp. 6-10 ◽  
Author(s):  
Takashi Momoi ◽  
Tohru Tokunaga ◽  
Yoshitaka Nagai
Keyword(s):  
Specific Interaction ◽  
Peanut Agglutinin ◽  
Asialo Gm1

Glycosphingolipids of Rat T Cells. Predominance of Asialo-GM1 and GD1c

Biochemistry ◽  
1994 ◽  
Vol 33 (15) ◽  
pp. 4661-4666 ◽  
Author(s):  
Keiko Nohara ◽  
Hiromitsu Nakauchi ◽  
Sarah Spiegel
Keyword(s):  
T Cells ◽  
Asialo Gm1
Sign in / Sign up

Export Citation Format

Share Document