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Chapter 14 : β-Lactamase Inhibitory Proteins
This chapter discusses structure and function studies of β-lactamase inhibitory protein (BLIP) with a focus on the interactions between TEM-1 β-lactamase and BLIP. The first proteinaceous inhibitor of β-lactamases, BLIP, was isolated from Streptomyces clavuligerus by a researcher's group in 1990. A BLIP nonproducer mutant and a BLIP/clavulanic acid nonproducer double mutant were constructed with the aim of elucidating BLIP's physiological function. Two hypotheses have been proposed for the function of BLIP. First, BLIP may be produced in response to the production of β-lactamases by other organisms in the surrounding environment in order to inhibit these β-lactamases and prevent the hydrolysis of antibiotics produced by S. clavuligerus. Alternatively, BLIP may play a role in cell wall growth or morphogenesis. Protein-protein interactions play a significant role in most cellular processes. The importance of such interactions in biology has made protein-protein recognition an area of considerable interest. The two domains join with each other to form an 8-strand antiparallel β-sheet. The study of a series of homologous interfaces provides an opportunity to study specificity as well as overall affinity determinants.