{"entity": "researcher", "timestamp": "2026-04-20T22:46:31.574Z", "family": "Berntsson", "given": "Ronnie", "initials": "R", "orcid": "0000-0001-6848-322X", "affiliations": ["Department of Medical Biochemistry and Biophysics, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden.", "Wallenberg Centre for Molecular Medicine, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf"}}, "publications": [{"entity": "publication", "iuid": "35169fcfafb34d33808c4bcb778a2f58", "links": {"self": {"href": "https://publications.scilifelab.se/publication/35169fcfafb34d33808c4bcb778a2f58.json"}, "display": {"href": "https://publications.scilifelab.se/publication/35169fcfafb34d33808c4bcb778a2f58"}}, "title": "Systematic screens for fertility genes essential for malaria parasite transmission reveal conserved aspects of sex in a divergent eukaryote.", "authors": [{"family": "Sayers", "given": "Claire", "initials": "C"}, {"family": "Pandey", "given": "Vikash", "initials": "V"}, {"family": "Balakrishnan", "given": "Arjun", "initials": "A"}, {"family": "Michie", "given": "Katharine", "initials": "K"}, {"family": "Svedberg", "given": "Dennis", "initials": "D", "orcid": "0000-0001-5799-4075", "researcher": {"href": "https://publications.scilifelab.se/researcher/a9273749dce544ee85e251fab9edbb70.json"}}, {"family": "Hunziker", "given": "Mirjam", "initials": "M", "orcid": "0000-0002-2912-4993", "researcher": {"href": "https://publications.scilifelab.se/researcher/8f021733485045d8ad5ba2eb9c206525.json"}}, {"family": "Pardo", "given": "Mercedes", "initials": "M"}, {"family": "Choudhary", "given": "Jyoti", "initials": "J"}, {"family": "Berntsson", "given": "Ronnie", "initials": "R", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}}, {"family": "Billker", "given": "Oliver", "initials": "O", "orcid": "0000-0003-1716-168X", "researcher": {"href": "https://publications.scilifelab.se/researcher/baa3de453a8047688800db0d5a14e291.json"}}], "type": "journal article", "published": "2024-11-20", "journal": {"title": "Cell Syst", "issn": "2639-5460", "volume": "15", "issue": "11", "pages": "1075-1091.e6", "issn-l": "2405-4712"}, "abstract": "Sexual reproduction in malaria parasites is essential for their transmission to mosquitoes and offers a divergent eukaryote model to understand the evolution of sex. Through a panel of genetic screens in Plasmodium berghei, we identify 348 sex and transmission-related genes and define roles for unstudied genes as putative targets for transmission-blocking interventions. The functional data provide a deeper understanding of female metabolic reprogramming, meiosis, and the axoneme. We identify a complex of a SUN domain protein (SUN1) and a putative allantoicase (ALLC1) that is essential for male fertility by linking the microtubule organizing center to the nuclear envelope and enabling mitotic spindle formation during male gametogenesis. Both proteins have orthologs in mouse testis, and the data raise the possibility of an ancient role for atypical SUN domain proteins in coupling the nucleus and axoneme. Altogether, our data provide an unbiased picture of the molecular processes that underpin malaria parasite transmission. A record of this paper's transparent peer review process is included in the supplemental information.", "doi": "10.1016/j.cels.2024.10.008", "pmid": "39541984", "labels": {"NGI Stockholm (Genomics Production)": "Service", "National Genomics Infrastructure": "Service", "NGI Short read": "Service"}, "xrefs": [{"db": "pii", "key": "S2405-4712(24)00305-3"}], "notes": [], "created": "2025-01-02T10:30:05.533Z", "modified": "2025-04-07T07:30:42.201Z"}, {"entity": "publication", "iuid": "685690b58b1342119be3d7e107297ff7", "links": {"self": {"href": "https://publications.scilifelab.se/publication/685690b58b1342119be3d7e107297ff7.json"}, "display": {"href": "https://publications.scilifelab.se/publication/685690b58b1342119be3d7e107297ff7"}}, "title": "PrgE: an OB-fold protein from plasmid pCF10 with striking differences to prototypical bacterial SSBs.", "authors": [{"family": "Breidenstein", "given": "Annika", "initials": "A", "orcid": "0000-0002-6664-5165", "researcher": {"href": "https://publications.scilifelab.se/researcher/2dc11c4f051c428cbd040961715fb55e.json"}}, {"family": "Lamy", "given": "Ana\u00efs", "initials": "A", "orcid": "0000-0001-9757-100X", "researcher": {"href": "https://publications.scilifelab.se/researcher/3886e3714e8142778455c4b96e1a2983.json"}}, {"family": "Bader", "given": "Cyrielle Pj", "initials": "CP", "orcid": "0009-0001-0517-315X", "researcher": {"href": "https://publications.scilifelab.se/researcher/0d7b27a34f5841c59015f74acbfac461.json"}}, {"family": "Sun", "given": "Wei-Sheng", "initials": "WS", "orcid": "0000-0001-9738-8862", "researcher": {"href": "https://publications.scilifelab.se/researcher/55f91ceeaf1f4546b875d4f703c9a193.json"}}, {"family": "Wanrooij", "given": "Paulina H", "initials": "PH", "orcid": "0000-0002-8607-7564", "researcher": {"href": "https://publications.scilifelab.se/researcher/ac6d0c050c9d47698f5123b935c4068b.json"}}, {"family": "Berntsson", "given": "Ronnie P-A", "initials": "RP", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}}], "type": "journal article", "published": "2024-08-00", "journal": {"title": "Life Sci. Alliance", "issn": "2575-1077", "volume": "7", "issue": "8", "issn-l": "2575-1077"}, "abstract": "A major pathway for horizontal gene transfer is the transmission of DNA from donor to recipient cells via plasmid-encoded type IV secretion systems (T4SSs). Many conjugative plasmids encode for a single-stranded DNA-binding protein (SSB) together with their T4SS. Some of these SSBs have been suggested to aid in establishing the plasmid in the recipient cell, but for many, their function remains unclear. Here, we characterize PrgE, a proposed SSB from the Enterococcus faecalis plasmid pCF10. We show that PrgE is not essential for conjugation. Structurally, it has the characteristic OB-fold of SSBs, but it has very unusual DNA-binding properties. Our DNA-bound structure shows that PrgE binds ssDNA like beads on a string supported by its N-terminal tail. In vitro studies highlight the plasticity of PrgE oligomerization and confirm the importance of the N-terminus. Unlike other SSBs, PrgE binds both double- and single-stranded DNA equally well. This shows that PrgE has a quaternary assembly and DNA-binding properties that are very different from the prototypical bacterial SSB, but also different from eukaryotic SSBs.", "doi": "10.26508/lsa.202402693", "pmid": "38811160", "labels": {"Chemical Biology Consortium Sweden": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11137577"}, {"db": "pii", "key": "7/8/e202402693"}, {"db": "PDB", "key": "1EYG"}, {"db": "PDB", "key": "7R7J"}, {"db": "PDB", "key": "6I52"}, {"db": "PDB", "key": "5ODL"}, {"db": "PDB", "key": "8S4S"}, {"db": "PDB", "key": "8S4T"}], "notes": [], "created": "2024-12-02T15:35:42.899Z", "modified": "2025-10-17T13:04:27.340Z"}, {"entity": "publication", "iuid": "359058c44374439ab404fed28c025b0c", "links": {"self": {"href": "https://publications.scilifelab.se/publication/359058c44374439ab404fed28c025b0c.json"}, "display": {"href": "https://publications.scilifelab.se/publication/359058c44374439ab404fed28c025b0c"}}, "title": "Structural foundation for the role of enterococcal PrgB in conjugation, biofilm formation, and virulence.", "authors": [{"family": "Sun", "given": "Wei-Sheng", "initials": "WS", "orcid": "0000-0001-9738-8862", "researcher": {"href": "https://publications.scilifelab.se/researcher/55f91ceeaf1f4546b875d4f703c9a193.json"}}, {"family": "Lassinantti", "given": "Lena", "initials": "L", "orcid": "0000-0001-5470-591X", "researcher": {"href": "https://publications.scilifelab.se/researcher/4b18812736ac43ec827360b50724e736.json"}}, {"family": "J\u00e4rv\u00e5", "given": "Michael", "initials": "M"}, {"family": "Schmitt", "given": "Andreas", "initials": "A"}, {"family": "Ter Beek", "given": "Josy", "initials": "J", "orcid": "0000-0003-4165-9277", "researcher": {"href": "https://publications.scilifelab.se/researcher/d8db9baa8a5b423f88b3213190e292b8.json"}}, {"family": "Berntsson", "given": "Ronnie P-A", "initials": "RP", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}}], "type": "journal article", "published": "2023-10-20", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "12", "issn-l": "2050-084X"}, "abstract": "Type 4 Secretion Systems are a main driver for the spread of antibiotic resistance genes and virulence factors in bacteria. In Gram-positives, these secretion systems often rely on surface adhesins to enhance cellular aggregation and mating-pair formation. One of the best studied adhesins is PrgB from the conjugative plasmid pCF10 of Enterococcus faecalis, which has been shown to play major roles in conjugation, biofilm formation, and importantly also in bacterial virulence. Since prgB orthologs exist on a large number of conjugative plasmids in various different species, this makes PrgB a model protein for this widespread virulence factor. After characterizing the polymer adhesin domain of PrgB previously, we here report the structure for almost the entire remainder of PrgB, which reveals that PrgB contains four immunoglobulin (Ig)-like domains. Based on this new insight, we re-evaluate previously studied variants and present new in vivo data where specific domains or conserved residues have been removed. For the first time, we can show a decoupling of cellular aggregation from biofilm formation and conjugation in prgB mutant phenotypes. Based on the presented data, we propose a new functional model to explain how PrgB mediates its different functions. We hypothesize that the Ig-like domains act as a rigid stalk that presents the polymer adhesin domain at the right distance from the cell wall.", "doi": "10.7554/eLife.84427", "pmid": "37860966", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10588982"}, {"db": "pii", "key": "84427"}], "notes": [], "created": "2024-01-15T14:41:17.162Z", "modified": "2024-01-15T14:41:17.504Z"}, {"entity": "publication", "iuid": "0fa6a6d0d98e4cdc824c41a447297873", "links": {"self": {"href": "https://publications.scilifelab.se/publication/0fa6a6d0d98e4cdc824c41a447297873.json"}, "display": {"href": "https://publications.scilifelab.se/publication/0fa6a6d0d98e4cdc824c41a447297873"}}, "title": "Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.", "authors": [{"family": "Verma", "given": "Apoorv", "initials": "A", "orcid": "0000-0002-8726-0870", "researcher": {"href": "https://publications.scilifelab.se/researcher/570887d2afe6478da2130ad606cf94e9.json"}}, {"family": "\u00c5berg-Zingmark", "given": "Emma", "initials": "E", "orcid": "0000-0002-5052-5214", "researcher": {"href": "https://publications.scilifelab.se/researcher/82284b92733343d7ba9c03be8bc85fca.json"}}, {"family": "Sparrman", "given": "Tobias", "initials": "T", "orcid": "0000-0002-4442-6367", "researcher": {"href": "https://publications.scilifelab.se/researcher/f0d27dbd2f014795b1f7aa164d34bada.json"}}, {"family": "Mushtaq", "given": "Ameeq Ul", "initials": "AU", "orcid": "0000-0002-5636-2567", "researcher": {"href": "https://publications.scilifelab.se/researcher/d8b77280f8a9463a9af768275bc80ae9.json"}}, {"family": "Rogne", "given": "Per", "initials": "P", "orcid": "0000-0002-3687-9200", "researcher": {"href": "https://publications.scilifelab.se/researcher/31042ecc88a94cd6b97cef0508da93fd.json"}}, {"family": "Grundstr\u00f6m", "given": "Christin", "initials": "C"}, {"family": "Berntsson", "given": "Ronnie", "initials": "R", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}}, {"family": "Sauer", "given": "Uwe H", "initials": "UH", "orcid": "0000-0002-3420-439X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5d011e944ae54d47aed374d548007812.json"}}, {"family": "Backman", "given": "Lars", "initials": "L", "orcid": "0000-0003-3044-1256", "researcher": {"href": "https://publications.scilifelab.se/researcher/99a60ee46b814b5a822c9c93e46ffe42.json"}}, {"family": "Nam", "given": "Kwangho", "initials": "K", "orcid": "0000-0003-0723-7839", "researcher": {"href": "https://publications.scilifelab.se/researcher/29b33d801f244b6aac48a9d626962770.json"}}, {"family": "Sauer-Eriksson", "given": "Elisabeth", "initials": "E", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2022-11-04", "journal": {"title": "Sci Adv", "issn": "2375-2548", "volume": "8", "issue": "44", "pages": "eabm4089", "issn-l": "2375-2548"}, "abstract": "Enzymatic catalysis is critically dependent on selectivity, active site architecture, and dynamics. To contribute insights into the interplay of these properties, we established an approach with NMR, crystallography, and MD simulations focused on the ubiquitous phosphotransferase adenylate kinase (AK) isolated from <i>Odinarchaeota<\/i> (OdinAK). <i>Odinarchaeota<\/i> belongs to the Asgard archaeal phylum that is believed to be the closest known ancestor to eukaryotes. We show that OdinAK is a hyperthermophilic trimer that, contrary to other AK family members, can use all NTPs for its phosphorylation reaction. Crystallographic structures of OdinAK-NTP complexes revealed a universal NTP-binding motif, while <sup>19<\/sup>F NMR experiments uncovered a conserved and rate-limiting dynamic signature. As a consequence of trimerization, the active site of OdinAK was found to be lacking a critical catalytic residue and is therefore considered to be \"atypical.\" On the basis of discovered relationships with human monomeric homologs, our findings are discussed in terms of evolution of enzymatic substrate specificity and cold adaptation.", "doi": "10.1126/sciadv.abm4089", "pmid": "36332013", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC9635829"}], "notes": [], "created": "2022-11-28T13:05:26.193Z", "modified": "2025-10-17T13:03:54.457Z"}, {"entity": "publication", "iuid": "f228f506357b46fd84627f3218873390", "links": {"self": {"href": "https://publications.scilifelab.se/publication/f228f506357b46fd84627f3218873390.json"}, "display": {"href": "https://publications.scilifelab.se/publication/f228f506357b46fd84627f3218873390"}}, "title": "PrgB promotes aggregation, biofilm formation, and conjugation through DNA binding and compaction.", "authors": [{"family": "Schmitt", "given": "Andreas", "initials": "A"}, {"family": "Jiang", "given": "Kai", "initials": "K"}, {"family": "Camacho", "given": "Martha I", "initials": "MI"}, {"family": "Jonna", "given": "Venkateswara Rao", "initials": "VR"}, {"family": "Hofer", "given": "Anders", "initials": "A"}, {"family": "Westerlund", "given": "Fredrik", "initials": "F", "orcid": "0000-0002-4767-4868", "researcher": {"href": "https://publications.scilifelab.se/researcher/7afbab9c0cc94ff8bda3b2116039ad8d.json"}}, {"family": "Christie", "given": "Peter J", "initials": "PJ", "orcid": "0000-0002-9799-7067", "researcher": {"href": "https://publications.scilifelab.se/researcher/c37f5eb88e284b76b2855bbcc0bfb611.json"}}, {"family": "Berntsson", "given": "Ronnie P-A", "initials": "RP", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}}], "type": "journal article", "published": "2018-08-00", "journal": {"title": "Mol. Microbiol.", "issn": "1365-2958", "volume": "109", "issue": "3", "pages": "291-305", "issn-l": "0950-382X"}, "abstract": "Gram-positive bacteria deploy type IV secretion systems (T4SSs) to facilitate horizontal gene transfer. The T4SSs of Gram-positive bacteria rely on surface adhesins as opposed to conjugative pili to facilitate mating. Enterococcus faecalis PrgB is a surface adhesin that promotes mating pair formation and robust biofilm development in an extracellular DNA (eDNA) dependent manner. Here, we report the structure of the adhesin domain of PrgB. The adhesin domain binds and compacts DNA in vitro. In vivo PrgB deleted of its adhesin domain does not support cellular aggregation, biofilm development and conjugative DNA transfer. PrgB also binds lipoteichoic acid (LTA), which competes with DNA binding. We propose that PrgB binding and compaction of eDNA facilitates cell aggregation and plays an important role in establishment of early biofilms in mono- or polyspecies settings. Within these biofilms, PrgB mediates formation and stabilization of direct cell-cell contacts through alternative binding of cell-bound LTA, which in turn promotes establishment of productive mating junctions and efficient intra- or inter-species T4SS-mediated gene transfer.", "doi": "10.1111/mmi.13980", "pmid": "29723434", "labels": {"Protein Science Facility (PSF)": "Service"}, "xrefs": [{"db": "mid", "key": "NIHMS964932"}, {"db": "pmc", "key": "PMC6158044"}], "notes": [], "created": "2024-04-03T14:42:05.730Z", "modified": "2024-04-03T14:42:05.945Z"}]}