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Innate Immunity, Vol. 14, No. 1,
39-49 (2008)
DOI: 10.1177/1753425907087257
Structural investigations into the interaction of hemoglobin and part structures with bacterial endotoxins
Jörg Howe
Forschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel, Germany
Patrick Garidel
Institut für Physikalische Chemie, Martin-Luther-Universität Halle-Wittenberg, Halle (Saale), Germany
Manfred Roessle
European Molecular Biology Laboratory, c/o DESY, Hamburg, Germany
Walter Richter
Elektronenmikroskopisches Zentrum der Medizinischen Fakultät, Friedrich-Schiller-Universität Jena, Jena, Germany
Christian Alexander
Forschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel, Germany
Karin Fournier
Institute de Biochemie, Université de Lausanne, Lausanne, Switzerland
Jean Pierre Mach
Institute de Biochemie, Université de Lausanne, Lausanne, Switzerland
Thierry Waelli
Clinique La Prairie, Montreux, Switzerland
Reginald M. Gorczynski
Department of Surgery and Immunology, University Health Network, Toronto, Canada
Artur J. Ulmer
Forschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel, Germany
Ulrich Zähringer
Forschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel, Germany
Alfred Hartmann
Clinique La Prairie, Montreux, Switzerland
Ernst Th. Rietschel
Leibniz-Gemeinschaft, Berlin, Germany
Klaus Brandenburg
Forschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel, Germany, Kbranden{at}fz-borstel.de
An understanding of details of the interaction mechanisms of bacterial endotoxins (lipopolysaccharide, LPS) with the oxygen transport protein hemoglobin is still lacking, despite its high biological relevance. Here, a biophysical investigation into the endotoxin:hemoglobin interaction is presented which comprises the use of various rough mutant LPS as well as free lipid A; in addition to the complete hemoglobin molecule from fetal sheep extract, also the partial structure  -chain and the heme-free sample are studied. The investigations comprise the determination of the gel-to-liquid crystalline phase behaviour of the acyl chains of LPS, the ultrastructure (type of aggregate structure and morphology) of the endotoxins, and the incorporation of the hemoglobins into artificial immune cell membranes and into LPS. Our data suggest a model for the interaction between Hb and LPS in which hemoglobins do not react strongly with the hydrophilic or with the hydrophobic moiety of LPS, but with the complete endotoxin aggregate. Hb is able to incorporate into LPS with the longitudinal direction parallel to the lipid A double-layer. Although this does not lead to a strong disturbance of the LPS acyl chain packing, the change of the curvature leads to a slightly conical molecular shape with a change of the three-dimensional arrangement from unilamellar into cubic LPS aggregates. Our previous results show that cubic LPS structures exhibit strong endotoxic activity. The property of Hb on the physical state of LPS described here may explain the observation of an increase in LPS-mediating endotoxicity due to the action of Hb.
Key Words: Hemoglobin • endotoxin • lipid A • FTIR • SAXS • phase transition
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