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real time label free analysis of native bacterial cells binding to carbohydrate microarray

descriptionPublicationkeyboard_double_arrow_right Article 01 Feb 2011Publisher:Elsevier BVJournal:Biophysical Journal, volume 100, page 485a (issn: 0006-3495,

Authors: Carlito B. Lebrilla; Jay V. Solnick; Xiangdong Zhu; Yiyan Fei; Thomas Borén;

doi: 10.1016/j.bpj.2010.12.2842

real time label free analysis of native bacterial cells binding to carbohydrate microarray

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Abstract

We present a novel experimental system based on glycoconjugates microarray and oblique-incidence reflectivity difference (OI-RD) microscopy to analyze binding of the onco-pathogen Helicobacter pylori to surface immobilized carbohydrates. The results confirm the recognized high-affinity binding of H. pylori BabA to the fucosylated Leb antigen, and suggest the presence of additional Leb binding adhesins not previously detected. OI-RD microscopy is a recently developed method for analyses of label-free biomolecules binding to immobilized targets by measuring small changes in phase and amplitude of a reflected optical wave from a solid surface due to the reaction of a solution-phase probe with the target. Besides applications of OI-RD in DNA hybridization, antigen-antibody interactions and small molecule libraries screening, we apply OI-RD microscopy to the binding analyses of whole bacterial cells to their host receptors presented on surfaces. Glycoconjugates microarrays consisting of Lea-HSA, Leb-HSA, Lex-HSA, and Ley-HSA were probed with H. pylori, H. pylori BabA deletion mutant and recombinant BabA protein. H. pylori demonstrated specific binding to Leb antigen, but did not bind to the closely related Lea, Lex or Ley antigens. The specificity in binding to the Leb antigen and not to Lea, Lex or Ley antigens was faithfully reproduced by recombinant BabA protein. Besides, H. pylori BabA deletion mutant does not express BabA and does not bind to Leb-HSA in solution, also demonstrated specific albeit reduced binding to Leb antigen. These results suggest that some H. pylori strains exhibit a complementary Leb-binding activity (independent of BabA) that has not been previously detected. The OI-RD technology with real-time analyses of whole cell bacterial binding to multivalently presented receptors in solid phase combined with magnified sensitivity for weaker adherence properties, offers new possibilities for identification of discrete attachment mechanisms essential for the infectious.

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Biophysics

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