Ronnie Berntsson - Assistant Professor
Structural biology of type 4 secretion systems
We utilize structural biology and biochemistry/biophysics to study Type 4 Secretion Systems (T4SS), mainly from gram-positive bacteria. T4SSs transfer large defined pieces of DNA between cells, and as such are a major contributor to the horizontal gene transfer of both antibiotic resistance and virulence factors between bacteria. This can occur also between different species of bacteria. In the Berntsson lab we focus on gram-positive T4SSs, as gram-positive bacteria are responsible for the majority of the nosocomial (hospital) infections today, and as such lead to both prolonged hospitalization time and increased costs for the healthcare system. More basic knowledge is needed of these systems, both to actually understand how they work and for future development of novel antibiotics.
Cellular adhesion processes in G+ T4SSs
The adhesion process is crucial during cellular mating. A stable and direct contact needs to be made and kept stable during the entire mating process. Adhesion proteins that are part of gram-positive T4SSs bind to specific parts of the recipient cell. We study this process using both in vitro and in vivo methods to understand how the process occurs and how it is regulated, as well as studying the structure of these proteins using protein crystallography.
DNA processing in G+ T4SSs
The energetic components of the gram-positive T4SSs are responsible both for processing the substrate DNA as well as for providing the energy for the transport of the substrate over the membrane. We study the DNA interaction using various in vitro techniques in order to better understand how the proteins interact both with the DNA as well as with each other.
Dr. Andreas Schmitt, postdoctoral fellow
Dr. Saima Rehman, postdoctoral fellow
Lena Lassinantti, PhD Student
We are currently looking for 1-2 master students who wish to perform their master project studying gram-positive T4SSs. For more information, please contact Dr. Ronnie Berntsson.
Dunny, G and Berntsson, RP-A (2016). Enterococcal sex pheromones: evolutionary pathways to complex, two-signal systems. Journal of Bacteriology 198: 1556-1562
Berntsson RP-A1, Odegrip R1, Sehlen W, Skaar K, Svensson LM, Massad T, Högbom M, Haggård-Ljungquist E, Stenmark P (2014). Structural insight into DNA binding and oligomerization of the multifunctional Cox protein of bacteriophage P2. Nucleic Acids Res 42: 2725-2735
Gad H, Koolmeister T, Jacques S, Jemth A, Eshtad S, Desroses M, Svensson LM, Schultz N, Lundbäck T, Jacques-Cordonnier M, Gokturk C, Saleh A, Baranczewski P, Svensson R, Berntsson RP-A, Gustafsson R, Ström C, Johansson F, Jeppsson F, Gustafsson A, Loseva O, Sanjiv K, Johansson L, Höglund A, Evers B, Hagenkort A, Sigmundsson K, Hammarström L, Axelsson H, Haraldsson M, Häggblad M, Strömberg K, Martens U, Lundin C, Lundgren B, Granelli I, Jenmalm-Jensen A, Artursson P, Warpman-Berglund U, Stenmark P, Scobie M, Helleday T. (2014) Targeting MTH1 nucleotide triphosphatase prevents sanitation of oxidised dNTP pools and kills cancer cells. Nature 508: 215-221
Kmiec B, Teixeira PF, Berntsson RP-A, Murcha M, Branca R, Radomiljac J, Regberg J, Langel U, Lehtiö J, Whelan J, Stenmark P, Glaser E (2013) Peptide degradation by a novel dually localized organellar oligopeptidase. Proc Natl Acad Sci U S A. 110: 3761-3769
Berntsson RP-A, Peng L, Svensson LM, Dong M, Stenmark P (2013) Crystal structures of botulinum neurotoxin DC in complex with its protein receptors synaptotagmin I and II. Structure 21: 1602-1611
Berntsson RP-A, Peng L, Dong M, Stenmark P (2013) Structure of dual receptor binding to Botulinum neurotoxin B. Nat Commun. doi: 10.1038/ncomms3058
Berntsson RP-A, Schuurman-Wolters GK, Dunny G, Slotboom D-J, Poolman B (2012) Structure and mode of peptide binding of pheromone receptor PrgZ. J Biol Chem. 287: 37165-37170.
Klepsch MM, Kovermann M, Löw C, Balbach J, Permentier HP, Fusetti F, Gier de JW, Slotboom D-J, Berntsson RP-A (2011) Escherichia coli Peptide Binding Protein OppA Has a Preference for Positively Charged Peptides. J Mol Biol 414: 75–85.
Erkens GB, Berntsson RP-A, Fulyani F, Majsnerowska M, Vujičić-Žagar A, Beek ter J, Poolman B, Slotboom D-J (2011) The structural basis of modularity in ECF-type ABC transporters. Nat Struct Mol Biol 18: 755–760.
Berntsson RP-A, Doeven MK, Fusetti F, Duurkens RH, Sengupta D, Marrink S-J, Thunnissen A-MWH, Poolman B, Slotboom D-J (2009) The structural basis for peptide selection by the transport receptor OppA. EMBO J 28: 1332–1340.