AFM investigation of Pseudomonas aeruginosa lectin LecA (PA-IL) filaments induced by multivalent glycoclusters.

Delphine Sicard (1) , Samy Cecioni (2, 3) , Maksym Iazykov (1) , Yann Chevolot (1) , Susan E Matthews , Jean-Pierre Praly (2) , Eliane Souteyrand (1) , Anne Imberty (3) , Sébastien Vidal (2) , Magali Phaner-Goutorbe (1)

1 INL - C&N - INL - Chimie et Nanobiotechnologies
2 ICBMS - Institut de Chimie et Biochimie Moléculaires et Supramoléculaires
3 CERMAV - Centre de Recherches sur les Macromolécules Végétales

Atomic force microscopy reveals that Pseudomonas aeruginosa LecA (PA-IL) and a tetra-galactosylated 1,3-alternate calix[4]arene-based glycocluster self-assemble according to an aggregative chelate binding mode to create monodimensional filaments. Lectin oligomers are identified along the filaments and defects in chelate binding generate branches and bifurcations. A molecular model with alternate 90° orientation of LecA tetramers is proposed to describe the organisation of lectins and glycoclusters in the filaments.

Domaines: Chimie organique

Delphine Sicard, Samy Cecioni, Maksym Iazykov, Yann Chevolot, Susan E Matthews, et al.. AFM investigation of Pseudomonas aeruginosa lectin LecA (PA-IL) filaments induced by multivalent glycoclusters.. Chemical Communications, 2011, 47 (33), pp.9483-5. ⟨10.1039/c1cc13097h⟩. ⟨hal-00691504⟩