Prof Peter Lund MA DPhil

Prof Peter Lund

School of Biosciences
Emeritus Professor of Molecular Microbiology

Contact details

Address
School of Biosciences
The University of Birmingham
Edgbaston
Birmingham
B15 2TT
United Kingdom

Peter Lund is a molecular microbiologist with particular research interests in how bacteria respond to different stresses in their environment.  These are studied with a range of genetic and biochemical tools including high throughput methods.  He is currently retired from teaching and administration but runs an active research programme funded by BBSRC, the Leverhulme Trust, and the Darwin Trust of Edinburgh, with several international collaborations, and he also leads a European COST Action.  He has worked in several other research fields in both academia and industry.  In addition, he has held positions on national advisory committees dealing with aspects of regulation of genetically-modified organisms.      

Qualifications

  • Emeritus Professor of Molecular Microbiology
  • DPhil in Microbial Genetics, University of Sussex, 1984
  • MA in Natural Sciences (Part II Genetics), University of Cambridge, 1979

Biography

Dr Lund graduated from Cambridge in Natural Sciences (specialising in Genetics), and subsequently worked both in academia and industry. His PhD research on analysis of bacteriophage Mu transposition was done at the University of Sussex, where he also worked as a post-doctoral research fellow.  He then moved to Bristol University, where he worked on the regulation of bacterial gene expression by mercuric ions, developing a model explaining how the MerR protein could work both as a repressor and an activator.  A subsequent move to California followed, to work in one of the first agri-biotechnology companies, Advanced Genetic Sciences. Here he worked on a range of projects including expression of chitinases and fish antifreeze proteins in plants.  This gave him an insight into the commercial application of molecular biology techniques, and developed his interest in the interface between science and society and the ways in which GM technologies are regulated.

He returned to the UK to a lectureship at the University of Birmingham in 1990 and worked here until 2020, apart from a spell as a visiting senior research fellow at the University of Melbourne, Australia.  His research interests in Birmingham have centred around stress responses in bacteria and archaea; in particular, the roles of molecular chaperones, and the impact of low pH on gene expression.  In addition he had responsibility for developing and managing several modules and degree programmes. 

His interests in regulation of GM technologies have led to membership of several national advisory committees for the FSA, HSE, and DEFRA.  He retired with an Emeritus Chair position at the end of 2020 but continues to run an active research laboratory and supervise several PhD students, as well as chairing a European COST Action and acting as cross-committee member on two GM regulatory committees.

Teaching

No current teaching responsibilities.  
Formerly programme leader for the MSc in Molecular Biotechnology, BSc in Bioinformatics, and MSci with Professional Placement.
Contributed to development and delivery of numerous modules in microbiology, genetics, biochemistry, and bioethics at all undergraduate and postgraduate taught levels. 

Postgraduate supervision

There are no vacancies for PhD students in the laboratory. 

Doctoral research

PhD title
An in vitro system for studying transposition of bacteriophage Mu.

Research

Current research:

  • The roles of chaperonins in Mycobacteria, using the zebrafish-M. marinum model (funded by BBSRC and the Darwin Trust of Edinburgh)
  • Use of transposon sequencing and laboratory evolution to study responses to low pH in laboratory and pathogenic strains of bacteria (funded by BBSRC and the Leverhulme Trust)

Previous areas of research interest include:

  • Modelling responses of gut bacteria and opportunistic pathogens to organic acids
  • Stress responses in foodborne pathogens
  • Systems biology analysis of bacterial responses to low pH
  • The regulation and functions of archaeal chaperonins
  • The roles of multiple chaperonins in root-nodulating bacteria
  • Regulation of expression of multiple chaperonin genes
  • Mechanisms and exploitation of disulphide bond catalysis in bacteria
  • Stress responses in Chlamydia
  • Expression of fish antifreeze genes in transgenic tomato plants
  • Expression of chitinase in plants as an antifungal strategy
  • Targeting plant genes by homologous recombination
  • Mechanisms of gene regulation of mercury resistance genes by the MerR protein
  • Functional dissection of the mer operon
  • In vitro and in vivo transposition of bacteriophage Mu

Other activities

  • Chair, European COST Action CA19113 (“Understanding and Exploiting the Responses of Micro-organisms to Low pH”)
  • Member, Advisory Committee on Releases to the Environment  (DEFRA)
  • Member, Scientific Advisory Committee on Genetic Manipulation (Health and Safety Executive) 
  • Former member, Advisory Committee on Novel Foods and Processes (Food Standards Agency)
  • Former member and non-executive director, the Food Ethics Council
  • Former consultant to a range of companies including GSK, Oxitech, Auspherix.
  • Former member. BBSRC research grants committee B
  • Member & former member of editorial board for various journals including Biochemical Journal, Microbiology, FEMS Microbiology Letters, Applied and Environmental Microbiology
  • Chair, European COST Action CA19113 (“Understanding and Exploiting the Responses of Micro-organisms to Low pH”)
  • Member, Advisory Committee on Releases to the Environment  (DEFRA)
  • Member, Scientific Advisory Committee on Genetic Manipulation (Health and Safety Executive)

 

  • Former member, Advisory Committee on Novel Foods and Processes (Food Standards Agency)
  • Former member and non-executive director, the Food Ethics Council
  • Former consultant to a range of companies including GSK, Oxitech, Auspherix.
  • Former member. BBSRC research grants committee B
Member or former member of editorial board for various 

Publications

  1. Mapping the Transcriptional and Fitness Landscapes of a Pathogenic E. coli Strain: The Effects of Organic Acid Stress under Aerobic and Anaerobic Conditions. Bushell F, Herbert JMJ, Sannasiddappa TH, Warren D, Turner AK, Falciani F, Lund PA. Genes (Basel). 2020;12(1):53. doi: 10.3390/genes12010053. PMID: 33396416
  2. Understanding How Microorganisms Respond to Acid pH Is Central to Their Control and Successful Exploitation. Lund PA, De Biase D, Liran O, Scheler O, Mira NP, Cetecioglu Z, Fernández EN, Bover-Cid S, Hall R, Sauer M, O'Byrne C. Front Microbiol. 2020;11:556140. doi:  10.3389/fmicb.2020.556140. eCollection 2020. PMID: 33117305
  3. A Bayesian non-parametric mixed-effects model of microbial growth curves. Tonner PD, Darnell CL, Bushell FML, Lund PA, Schmid AK, Schmidler SC. PLoS Comput Biol. 2020;16(10):e1008366. doi: 10.1371/journal.pcbi.1008366. eCollection 2020 Oct. PMID: 33104703
  4. Use of a model to understand the synergies underlying the antibacterial mechanism of H2O2-producing honeys. Masoura M, Passaretti P, Overton TW, Lund PA, Gkatzionis K. Sci Rep. 2020;10(1):17692. doi: 10.1038/s41598-020-74937-6. PMID: 33077785 
  5. Villapún VM, Qu B, Lund PA, Wei W, Dover LG, Thompson JR, Adesina JO, Hoerdemann C, Cox S, González S.  Optimizing the antimicrobial performance of metallic glass composites through surface texturing Materials Today Communications 101074 (2020)
  6. Bushell FML, Tonner PD, Jabbari S, Schmid AK, Lund PA. Synergistic Impacts of Organic Acids and pH on Growth of Pseudomonas aeruginosa: A Comparison of Parametric and Bayesian Non-parametric Methods to Model Growth. Front Microbiol. 2019 9 3196. doi: 10.3389/fmicb.2018.03196
  7. Jain N, Knowles TJ, Lund PA, Chaudhuri TK.  Minichaperone (GroEL191-345) mediated folding of MalZ proceeds by binding and release of native and functional intermediates. Biochim Biophys Acta. 2018 1866 941-951. doi: 10.1016/j.bbapap.2018.05.015.
  8. Goodall ECA, Robinson A, Johnston IG, Jabbari S, Turner KA, Cunningham AF, Lund PA, Cole JA, Henderson IR. The Essential Genome of Escherichia coli K-12. MBio 9 e02096-17 (2018)
  9. Iqbal M, Doherty N, Page AML, Qazi SNA, Ajmera I, Lund PA, Kypraios T, Scott DJ, Hill PJ, Stekel DJ. Reconstructing promoter activity from Lux bioluminescent reporters. PLoS Comput Biol 13: e1005731. (2017)
  10. Sannasiddappa TH, Lund PA, Clarke SR. In Vitro Antibacterial Activity of Unconjugated and Conjugated Bile Salts on Staphylococcus aureus. Front Microbiol. 8 : 1581 (2017)
  11. Sen H, Aggarwal N, Ishionwu C, Hussain N, Parmar C, Jamshad M, Bavro VN, Lund PA.  Structural and Functional Analysis of the Escherichia coli Acid-Sensing Histidine Kinase EvgS.J Bacteriol. 199 e00310-17 (2017)
  12. Shah R, Large AT, Ursinus A, Lin B, Gowrinathan P, Martin J, Lund PA. Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis. J Bacteriol 198: 2692-2670  (2016). 
  13. Halstead FD, Rauf M, Moiemen NS, Bamford A, Wearn CM, Fraise AP, Lund PA, Oppenheim BA, Webber MA. The Antibacterial Activity of Acetic Acid against Biofilm-Producing Pathogens of Relevance to Burns Patients. PLoS One. 10:e0136190 (2015)
  14. Lund PA, Tramonti A, de Biase D. Coping with low pH: molecular strategies in neutralophilic bacteria.  FEMS Micro Rev 38:1091-125 (2014)
  15. Johnson MD, Bell J, Clarke K, Chandler R, Pathak P, Xia Y, Marshall RL, Weinstock GM, Loman NJ, Winn PJ, Lund PA. Characterization of mutations in the PAS domain of the EvgS sensor kinase selected by laboratory evolution for acid resistance in Escherichia coli. Mol Microbiol 93: 911-27 (2014)
  16. Hu Y, Coates AR, Liu A, Lund PA, Henderson B. Identification of the monocyte activating motif in Mycobacterium tuberculosis chaperonin 60.1. Tuberculosis (Edinb) 93: 442-7 (2013)
  17. Browning DF, Wells TJ, França FL, Morris FC, Sevastsyanovich YR, Bryant JA, Johnson MD, Lund PA, Cunningham AF, Hobman JL, May RC, Webber MA, Henderson IR. Laboratory adapted Escherichia coli K-12 becomes a pathogen of Caenorhabditis elegans upon restoration of O antigen biosynthesis. Mol Microbiol 87: 939-50 (2013)
  18. Henderson B, Fares MA, Lund PA.  Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions. Biol Reviews  88: 955-87 (2013)
  19. Parnas A, Nisemblat S, Weiss C, Levy-Rimler G, Pri-Or A, Zor T, Lund PA, Bross P, Azem A. Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. PLoS One. 2012 7: e50318 (2012)
  20. Batt SM, Jabeen T, Bhowruth V, Quill L, Lund PA, Eggeling L, Alderwick LJ, Fütterer K, Besra GS. Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors. Proc Natl Acad Sci USA 109:11354-9 (2012)
  21. Fan MQ, Rao T, Zacco E, Ahmed MT, Shukla A, Ojha A, Freeke J, Robinson CV, Benesch JL, Lund PA.  The unusual mycobacterial chaperonins: evidence for in vivo oligomerisation and specialisation of function. Mol Microbiol 85: 934-44 (2012)
  22. Stincone A, Daudi N, Rahman AS, Antczak P, Henderson IR, Cole JA, Lund PA*, Falciani F*.  A systems biology approach sheds new light on Escherichia coli acid resistance.  Nucleic Acids Res 39: 7512-28 (2011) * joint senior authors
  23. Johnson MD, Burton NA, Gutiérrez B, Painter K, Lund PA.  RcsB is required for inducible acid resistance in Escherichia coli and acts at gadE-dependent and -independent promoters.  J Bacteriol 193: 3653-6 (2011)
  24. Rao T, Lund PA.  Differential expression of the multiple chaperonins of Mycobacterium smegmatis.  FEMS Micro Lett 310: 24-31. (2010)
  25. Burton NA, Johnson MD, Antczak P, Robinson A, Lund PA.  Novel aspects of the acid response network of E. coli K-12 are revealed by a study of transcriptional dynamics.  J Mol Biol 401: 726-42 (2010)
  26. Henderson B, Lund PA, Coates AR. Multiple moonlighting functions of mycobacterial molecular chaperones. Tuberculosis (Edinb) 90: 119-124 (2010)
  27. Kovács E, Sun Z, Liu H, Scott DJ, Karsisiotis AI, Clarke AR, Burston SG, Lund PA.  Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.  J Mol Biol 396: 1271-83 (2010)
  28. Holmes CW, Penn CW, Lund PA. The hrcA and hspR regulons of Campylobacter jejuni. Microbiology 156: 158-66 (2010)
  29. Liu H, Kovács E, and Lund PA. Characterisation of mutations in GroES that allow GroEL to function as a single ring.  FEBS Letters 583: 2365-71 (2009)
  30. Lund PA  Multiple chaperonins in bacteria – why so many?  FEMS Micro Rev 4: 785-800 (2009)
  31. Large AT and Lund PA. Archaeal chaperonins. Frontiers Biosci 14: 1304-24 (2009)
  32. Hu Y, Henderson B, Lund PA, Tormay P, Ahmed MT, Gurcha SS, Besra GS, Coates AR. A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection. Infect Immun 76: 1535-46 (2008)
  33. Large A, Stamme C, Lange C, Duan Z, Allers T, Soppa J, Lund PA. Characterization of a tightly controlled promoter of the halophilic archaeon Haloferax volcanii and its use in the analysis of the essential cct1 gene Mol Microbiol 66: 1092-106 (2007)
  34. Gould P, Burgar H, Lund PA. Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent. Cell Stress Chaps 12: 123-31 (2007)
  35. Perni S, Shama G, Hobman JL, Lund PA,  Kershaw CK, Hidalgo-Arroyo GA, Penn CW,  Deng XT, Walsh JL, Kong MG. Probing bactericidal mechanisms induced by cold atmospheric plasmas with Escherichia coli mutants. Applied Phys Lett 90: 073902 (2007)
  36. Gould P, Maguire M, Lund PA. Distinct mechanisms regulate expression of the two major groEL homologues in Rhizobium leguminosarum. Arch Microbiol 187: 1-14 (2007)
  37. Kapatai G, Large A, Benesch JL, Robinson CV, Carrascosa JL, Valpuesta JM, Gowrinathan P, Lund PA.  All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable. Mol Microbiol 61: 1583-97 (2006)
  38. Rodríguez-Quiñones F, Maguire M, Wallington EJ, Gould PS, Yerko V, Downie JA, and Lund PA.  Two of the three groEL homologues in Rhizobium leguminosarum are dispensable for normal growth.  Arch Microbiol 183: 253-65 (2005)
  39. George R, Kelly SM, Price NC, Erbse A, Fisher M, Lund PA. Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties. Biochem Biophys Res Commun 324: 822-8 (2004)
  40. Sun Z., Scott DJ, Lund PA.  Isolation and characterisation of mutants of GroEL that are fully functional as single rings  J Mol Biol 332: 715-28 (2003)
  41. Large AT, Kovacs E, Lund PA. Properties of the chaperonin complex from the halophilic archaeon Haloferax volcanii.FEBS Lett 532: 309-12 (2002)
  42. Lewthwaite J, George R, Lund PA, Poole S, Tormay P, Sharp L, Coates AR, Henderson B. Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is dependent on interaction with cell surface CD14. Cell Stress Chaperones 7: 130-136 (2002)
  43. Kuczynska-Wisnik D, Kedzierska S, Matuszewska E, Lund PA, Taylor A, Lipinska B, Laskowska E. The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock.  Microbiology 148:1757-65 (2002)
  44. Lund PA. Microbial Molecular Chaperones. Adv Microb Physiol 44: 93-140 (2001)
  45. Walters C, Clarke A, Cliff MJ, Lund PA, Harding SE.  Trp203 mutation in GroEL promotes a self-association reaction: a hydrodynamic study  Europ Biophys Jou 29: 420-28 (2000)
  46. Stafford SJ, Lund PA. Mutagenic studies on human protein disulfide isomerase by complementation of Escherichia coli dsbA and dsbC.FEBS Letters 466: 317-22 (2000)
  47. van der Vies S, Lund PA. Determination of chaperonin activity in vivo. Methods in Mol Biol. 140: 75-96. Ed: Schneider C. Pub: Humana Press (2000)
  48. Cliff MJ, Kad NM, Hay N, Lund PA, Webb MR, Burston SG, Clarke AR. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL J Mol Biol 293: 667-84 (1999)
  49. Erbse A, Yifrach O, Jones S,  Lund PA. Chaperone activity of a chimeric GroEL protein that can exist in a single or double ring form. J Biol Chem 274: 20351-357 (1999)
  50. Javed MU, Michelangeli F, Lund PA. GroEL protects the sarcoplasmic reticulum Ca(++)-dependent ATPase from inactivation in vitro. Biochem Mol Biol Int 47: 631-638 (1999)
  51. Stafford SJ, Humphreys DP, Lund PA. Mutations in dsbA and dsbB but not dsbC lead to enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+FEMS Micro Lett 174: 179-84 (1999)
  52. Jones S, Wallington E J, George R, Lund PA. An arginine residue (arg 101) which is conserved in many GroEL homologues is required for interactions between the two heptameric rings. J Mol Biol 282: 789-800 (1988)
  53. Chatelier J, Hill F, Lund PA, Fersht AR. In vivo activities of GroEL minichaperones. Proc Natl Acad Sci USA 95: 9861-66 (1998)
  54. Ivic A, Olden D, Wallington EJ, Lund PA. Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37ºC but not 43ºC.  Gene 194: 1-8 (1997)
  55. Gibbons DL, Hixson JD, Hay N, Lund PA , Gorovits B M, Ybarra J, Horowitz P M. Intrinsic fluorescence studies of the chaperonin GroEL containing single tyr/trp replacements reveal ligand induced conformational changes. J Biol Chem 271: 31989-95 (1996)
  56. Devitt A, Lund PA, Pearce JH. Induction of alpha/beta interferon and dependent nitric oxide synthesis during Chlamydia trachomatis infection of McCoy cells in the absence of exogenous cytokine.  Infec and Imm 64: 3951-56 (1996)
  57. Humphreys D P, Weir N, Lawson A, Mountain A, Lund PA. Coexpression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coliFEBS Letters 380: 194-97 (1996)
  58. Humphreys D P, Weir N, Mountain A, Lund PA. Human protein disulphide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coliJ Biol Chem 270: 28210-15 (1995)
  59. Everest P, Frankel G, Li J, Lund PA, Chatfield S, Dougan G. Expression of LacZ from htrA, nirB and groE promoters in a Salmonella vaccine strain: effects of growth in mammalian cells. FEMS Micro Letters 126: 97-102 (1995)
  60. Lund PA. The in vivo role of molecular chaperones Essays in Biochemistry 29: 113-122 Ed: Apps D Pub: Portland Press (1995)
  61. Wallington EJ, Lund PA Rhizobium leguminosarum possesses multiple chaperonin 60 (cpn60) genes. Microbiology 140: 113-22 (1994)
  62. Lund PA. The chaperonin cycle and protein folding. BioEssays 16: 229-31 (1994)
  63. Lund PA, Dunsmuir P. A plant signal sequence enhances the secretion of bacterial ChiA in transgenic plants. Plant Mol Biol 18: 47-53 (1992)
  64. Badcoe I G, Smith C J, Wood S, Halsall D, Holbrook J J, Lund PA, Clarke AR. The binding of a chaperonin to the folding intermediates of lactate dehydrogenase.  Biochemistry 30: 9195-20 (1991)
  65. Hightower R, Baden C, Penzes E, Lund PA, Dunsmuir P. Expression of antifreeze proteins in transgenic plants. Plant Mol Biol 17:1013-21 (1991)
  66. Lee K, Lund PA, Lowe K, Dunsmuir P. Homologous recombination with a plant gene following Agrobacterium-mediated transformation. Plant Cell 2: 415-25 (1990)
  67. Lund PA, Lee RY, Dunsmuir P. Bacterial chitinase is modified and secreted in transgenic tobacco. Plant Physiol 91: 130-35 (1989)
  68. Lund PA, Brown NL. Up-promoter mutations in the positively-regulated mer promoter of Tn501. Nucl Acids Res 17: 5517-27 (1989)
  69. Lund PA, Brown NL.  Regulation of transcription from the mer and merR promoters in the transposon Tn501. J Mol Biol 205: 343-53 (1989)
  70. Lund PA, and NL  Role of the merT and merP gene products of transposon Tn501 in the induction and expression of resistance to mercuric ions. Gene 52: 207-14 (1987)
  71. Lund PA, Ford SJ, and Brown NL. Transcriptional regulation of the mercury resistance genes of transposon Tn501. J Gen Micro 132: 465-80 (1986)
  72. Akroyd J, Barton B, Lund P, Maynard-Smith S, Sultana K and Symonds N. Mapping and properties of the gam and sot genes of phage Mu: their possible roles in recombination. Cold Spring Harbor Symp Quant Biol 49: 291-296 (1984)

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