Antibody Recognition of Chlamydia LPS: Structural Insights of Inherited Immune Responses

The increasing utility of carbohydrate-specific antibodies in diagnostic and therapeutic medicine, in disease bio-marker identification, and in carbohydrate-based vaccine design has underlined the need to understand these important interactions at the molecular level (Holmgren et al. 1984; Hakomori 1984, 1989; Fung et al. 1990; Cygler et al. 1991; Casadevall et al. 1992; MacLean et al. 1992, 1993; Bundle et al. 1994; Pirofski et al. 1995; Fukuda 1996; Mari et al. 1999; van Ree 2000; Hemmer et al. 2001; Kudryashov et al. 2001; Foetisch et al. 2003; Ebo et al. 2004; Lo-Man et al. 2004; Manimala et al. 2005; Muuller-Loennies et al. 2006; Ni et al. 2006; Vliegenthart 2006; de Geus et al. 2009; Hecht et al. 2009; Astronomo and Burton 2010; Avci and Kasper 2010; Collot et al. 2010). One of the premiere methods to study the specific recognition of carbohydrates by antibodies is through crystal structure determination via X-ray diffraction; however, this requires relatively large quantities of pure proteins and antigens.