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Christopher Penfold

Lecturer and Course Director for MSc in Molecular Medical Microbiology, Faculty of Medicine & Health Sciences

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Expertise Summary

Normal 0 false false false EN-GB X-NONE X-NONE MicrosoftInternetExplorer4 st1\:*{behavior:url(#ieooui) } /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-qformat:yes; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:11.0pt; font-family:"Calibri","sans-serif"; mso-ascii-font-family:Calibri; mso-ascii-theme-font:minor-latin; mso-fareast-font-family:"Times New Roman"; mso-fareast-theme-font:minor-fareast; mso-hansi-font-family:Calibri; mso-hansi-theme-font:minor-latin; mso-bidi-font-family:"Times New Roman"; mso-bidi-theme-font:minor-bidi;} Colicins are protein antibiotics produced by strains of Escherichia coli to kill non-producing strains of the same organims presumably as a method of competitive inhibition. Colicins molecules have three domains that are intrinsically linked to deliver the colicin from the outer membrane to the cytotoxic site of action; either the cytoplasmic membrane or the cytosol. The colicin system continues to generate exciting data about this amazing biological system that addresses several fundamental problems that are poorly understood at the molecular level: (1) Early steps in filamentous bacteriophage infection. Many phages share the same translocation machinery with colicins and possibly the same mechanism for traversing the OM; (2) Host protein function. The functions of host systems that are subverted by colicins such as the Tol-Pal complex remain unresolved even though they are important and ubiquitous in Gram-negative bacteria; (3) Protein recruitment by natively disordered regions (NDRs). NDRs are functionally important in proteins throughout the three kingdoms of life as well as being implicated in cancer, amyloid diseases and bacterial pathogenesis. We have discovered novel recruitment mechanisms used by enzymatic colicin NDRs to bind soluble and membrane-bound proteins in preparation for cellular import; (4) Protein translocation across membranes. How proteins are translocated across membrane barriers is a key issue in the biological and biomedical sciences. A quarter of the E. coli proteome is extracytoplasmic, targeted to a final destination by short, canonical N-terminal sequences that for the most part direct them either to the general secretory or Tat pathway machines. Nuclease colicins are also targeted but in the opposite direction, across both membrane barriers and by a mechanism that is insensitive to the structure of the imported enzyme.

Teaching Summary

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Research Summary

Bacteriocins are protein antibiotics produced by strains of bacteria that are active against related bacteria. We are particularly interested in a group of bacteriocins called colicins that are… read more

Recent Publications

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I teach on:

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  • MBD301: Introduction to Molecular Microbiology
  • MBD409: Microbial and Molecular techniques (practical sessions)
  • MBD403: Applied Molecular Microbiology
  • MBD402: Research Methods
  • MBD407: Scientififc review of writing

MSc Clinical Microbiology

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  • MO4MOL: Research Project

BMedsci

  • Clinical Laboratory Sciences

Current Research

Bacteriocins are protein antibiotics produced by strains of bacteria that are active against related bacteria. We are particularly interested in a group of bacteriocins called colicins that are produced by Escherichia coli and are active against other enterobacteriaceae. They are ~60 KDa proteins that consist of three functional domains that allow the colicin to bind to cell surface receptors, move through the cell envelope and then kill the bacterial cell by, for example, degrading the DNA. We are interested in how the DNase domain of colicin E9 is delivered into the cytoplasm of sensitive cells to exert its antibacterial effect. Antimicrobial peptides Antimicrobial peptides are low molecular weight polypeptides that have narrow spectrum activities. Lysostaphin, for example, is produced by Stapholococcus simulans against Staph. aureus and the clinically important MRSA. Lysostaphin has two domains; a targeting domain which binds to an unknown cell surface receptor of S. aureus and a cytotoxic domain which cleaves a pentaglycine cross bridge in the host cell wall. We are interested in conducting a structure/function study of both the targeting and endopeptidase domains of lysostaphin to determine whether it is possible to produce hybrid molecules with more broad spectrum activities.

School of Life Sciences

University of Nottingham
Medical School
Queen's Medical Centre
Nottingham NG7 2UH

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