title: Use of real-time, label-free analysis in revealing low-affinity binding to blood group antigens by Helicobacter pylori.
abstract: Infectious diseases are often initiated by microbial adherence that is mediated by the binding of attachment molecules, termed adhesins, to cell surface receptors on host cells. We present an experimental system, oblique-incidence reflectivity difference (OI-RD) microscopy, which allows the detection of novel, low-affinity microbial attachment mechanisms that may be essential for infectious processes. OI-RD microscopy was used to analyze direct binding of the oncopathogen, Helicobacter pylori ( H. pylori ) to immobilized glycoconjugates in real time with no need for labeling tags. The results suggest the presence of additional Lewis b blood group antigen (Le(b)) binding adhesins that have not been detected previously. OI-RD microscopy also confirmed the high-affinity binding of H. pylori outer-membrane protein BabA to Le(b). The OI-RD microscopy method is broadly applicable to real-time characterization of intact microbial binding to host receptors and offers new strategies to elucidate the molecular interactions of infectious agents with human host cells.
authors: Department of Physics, University of California, Davis, Davis, California 95616, United States.
authors: Y Y
authors: YY
authors: Fei
authors: A
authors: A
authors: Schmidt
authors: G
authors: G
authors: Bylund
authors: D X
authors: DX
authors: Johansson
authors: S
authors: S
authors: Henriksson
authors: C
authors: C
authors: Lebrilla
authors: J V
authors: JV
authors: Solnick
authors: T
authors: T
authors: Borén
authors: X D
authors: XD
authors: Zhu
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001422:Bacterial Adhesion; D003001:Cloning, Molecular; D004926:Escherichia coli; D006001:Glycoconjugates / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D016481:Helicobacter Infections / Q000276:immunology / Q000378:metabolism / Q000382:microbiology; D016480:Helicobacter pylori / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D007983:Lewis Blood Group Antigens / Q000276:immunology / Q000378:metabolism; D008853:Microscopy / Q000379:methods*; D010957:Plasmids; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D018829:Adhesins, Bacterial; C400429:BabA protein, Helicobacter pylori; D006001:Glycoconjugates; D007983:Lewis Blood Group Antigens; D011994:Recombinant Proteins