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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : Carbohydrate research

Binding of modified fragments of the Shigella dysenteriae type 1 O-specific polysaccharide to monoclonal IgM 3707 E9 and docking of the immunodeterminant to its modeled Fv

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Carbohydrate research - 01 Jul 1998

Miller CE, Mulard LA, Padlan EA, Glaudemans CP

Link to Pubmed [PMID] – 9742688

Carbohydr. Res. 1998 Jul;309(3):219-26

The O-specific polysaccharide (O-SP) of Shigella dysenteriae type 1 has been shown by others to have the structure–>3)-alpha-L-Rhap-(1–>3)-alpha-L-Rhap-(1–>2)-alp ha-D- Galp-(1–>3)-alpha-D-GlcpNAc-(1–>. We have shown in the past that IgM 3707 E9, an anti S. dysenteriae type 1 O-SP monoclonal antibody, binds specifically to the -alpha-L-Rhap-(1–>2)-alpha-D-Galp-determinant of the polysaccharide. In this report we show that determinant to have hydrogen bonds, necessary for binding to the antibody, involving positions 3, 4 and 6 of the galactopyranosyl residue. The hydroxyl groups of the rhamnopyranosyl moiety of the immunodeterminant appear not to partake in hydrogen-bond interactions with the antibody. A model is presented of the Fv of IgM 3707 E9 based on our previously established cDNA-sequence and two known, highly homologous immunoglobulin crystal structures. The methyl glycoside of the immunodeterminant alpha-L-rhamnopyranosyl-(1–>2)-alpha-D-galactopyranose is docked to the combining area of the Fv.

http://www.ncbi.nlm.nih.gov/pubmed/9742688