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Chapter 14 : β-Lactamase Inhibitory Proteins

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β-Lactamase Inhibitory Proteins, Page 1 of 2

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Abstract:

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 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 . 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.

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14

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Inorganic Chemicals
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Enzyme-Linked Immunosorbent Assay
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Bacterial Cell Wall
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Human Growth Hormone
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Figures

Image of Figure 14.1
Figure 14.1

Structure of TEM-1 β-lactamase. The image was generated using Swiss-PdbViewer and rendered by POV-Ray using Protein Data Bank coordinates 1BTL ( ).

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14
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Image of Figure 14.2
Figure 14.2

Hydrolysis of β-lactam antibiotics.

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14
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Image of Figure 14.3
Figure 14.3

Structure of the TEM-1/BLIP and TEM1/BLIP-II complexes. BLIP and BLIP-II are shown in ribbon format. TEM-1 β-lactamase is shown in spacefill format. The darkened region is the loop-helix domain of TEM-1 that interacts with BLIP (99-114). The active-site residue (S70) of TEM-1 β-lactamase is shown in black. The images were generated with Molscript using Protein Data Bank coordinates 1JTG (TEM-1/BLIP) and 1JTD (TEM-1/BLIP-II).

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14
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Image of Figure 14.4
Figure 14.4

β-Hairpin structure of BLIP residues 46 to 51. The image was generated using Swiss-PdbViewer and rendered with POV-Ray using Protein Data Bank coordinates 1BTL.

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14
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Image of Figure 14.5
Figure 14.5

BLIP residues critical for binding to TEM-1 β-lactamase. BLIP is shown in spacefill format. The residues determined to be in the hot spot based on loss of binding affinity after substitution with alanine are shown in black. The residue Tyr50 is labeled in light gray because the Tyr50Ala mutation increases the binding affinity of BLIP for TEM-1 β-lactamase. The image was generated using Molscript with Protein Data Bank coordinates 1JTG.

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14
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References

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1. Albeck, S., and, G. Schreiber. 1999. Biophysical characterization of the interaction of the β-lactamase TEM-1 with its protein inhibitor BLIP. Biochemistry 38:1121.
2. Albeck, S.,, R. Unger, and, G. Schreiber. 2000. Evaluation of direct and cooperative contributions towards the strength of buried hydrogen bonds and salt bridges. J. Mol. Biol. 298:503520.
3. Bogan, A. A., and, K. S. Thorn. 1998. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280:19.
4. Cunningham, B., and, J. A. Wells. 1989. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244:10811085.
5. Doran, J. L.,, B. K. Leskiw,, S. Aippersbach, and, S. E. Jensen. 1990. Isolation and characterization of a beta-lactamase-inhibitory protein from Streptomyces clavuligerus and cloning and analysis of the corresponding gene. J. Bacteriol. 172:49094918.
6. Hu, Z.,, B. Ma,, H. Wolfson, and, R. Nussinov. 2000. Conservation of polar residues as hot spots at protein interfaces. Proteins 39:331342.
7. Huang, W.,, Z. Zhang, and, T. Palzkill. 2000. Design of potent β-lactamase inhibitors by phage display of β-lactamase inhibitory protein. J. Biol. Chem. 275:1496414968.
8. Jelsch, C.,, L. Mourey,, J. M. Masson, and, J. P. Samama. 1993. Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 A resolution. Proteins 16:364383.
9. Kang, S. G.,, H. U. Park,, H. S. Lee,, H. T. Kim, and, K. J. Lee. 2000. New beta -lactamase inhibitory protein (BLIP-I) from Streptomyces exfoliatus SMF19 and its roles on the morphological differentiation. J. Biol. Chem. 275:1685116856.
10. Kim, M., and, K. J. Lee. 1994. Characteristics of β-lactamase-inhibiting proteins from Streptomyces exfoliatus SMF19. Appl. Environ. Microbiol. 60:10291032.
11. Lim, D.,, H. U. Park,, L. De Castro,, S. G. Kang,, H. S. Lee,, S. Jensen,, K. J. Lee, and, N. C. Strynadka. 2001. Crystal structure and kinetic analysis of β-lactamase inhibitor protein-II in complex with TEM-1 β-lactamase. Nat. Struct. Biol. 8:848852.
12. Matagne, A.,, J. Lamotte-Brasseur, and, J. M. Frere. 1998. Catalytic properties of class A β-lactamases: efficiency and diversity. Biochem. J. 330:581598.
13. Petrosino, J.,, G. Rudgers,, H. Gilbert, and, T. Palzkill. 1999. Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of β-lactamases. J. Biol. Chem. 274:23942400.
14. Rudgers, G. W.,, W. Huang, and, T. Palzkill. 2001. Binding properties of a peptide derived from β-lactamase inhibitory protein. Antimicrob. Agents Chemother. 45:32793286.
15. Rudgers, G. W., and, T. Palzkill. 1999. Identification of residues in β-lactamase critical for binding β-lactamase inhibitory protein. J. Biol. Chem. 274:69636971.
16. Rudgers, G. W., and, T. Palzkill. 2001. Protein minimization by random fragmentation and selection. Protein Eng. 14:487492.
17. Samanen, J.,, F. Ali,, T. Romoff,, R. Calvo,, E. Sorenson,, J. Vasko,, B. Storer,, D. Berry,, D. M. Bennett,, M. Strohsacker, et al. 1991. Development of a small RGD peptide fibrinogen receptor antagonist with potent anti-aggregatory activity in vitro. J. Med. Chem. 34:31143125.
18. Schreiber, G., and, A. R. Fersht. 1995. Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248:478486.
19. Selzer, T.,, S. Albeck, and, G. Schreiber. 2000. Rational design of faster associating and tighter binding protein complexes. Nat. Struct. Biol. 7:537541.
20. Strynadka, N. C.,, S. E. Jensen,, P. M. Alzari, and, M. N. James. 1996. A potent new mode of β-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex. Nat. Struct. Biol. 3:290297.
21. Thai, W.,, A. S. Paradkar, and, S. E. Jensen. 2001. Construction and analysis of β-lactamase-inhibitory protein (BLIP) non-producer mutants of Streptomyces clavuligerus. Microbiology 147:325335.
22. Zhang, Z., and, T. Palzkill. 2003. Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 β-lactamase with β-lactamase inhibitory protein. J. Biol. Chem. 278:4570645712.
23. Zhang, Z., and, T. Palzkill. 2004. Dissecting the protein-protein interface between β-lactamase inhibitory protein and class A β-lactamases. J. Biol. Chem. 279:4286042866.

Tables

Generic image for table
Table 14.1

Inhibition of class A β-lactamases by BLIP

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14
Generic image for table
Table 14.2

Role of interface residues in BLIP for binding to class A β-lactamases

Citation: Zhang Z, Palzkill T. 2007. β-Lactamase Inhibitory Proteins, p 227-234. In Bonomo R, Tolmasky M (ed), Enzyme-Mediated Resistance to Antibiotics. ASM Press, Washington, DC. doi: 10.1128/9781555815615.ch14

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