{"entity": "researcher", "timestamp": "2026-07-19T18:59:56.822Z", "family": "Heidler", "given": "Thomas V", "initials": "TV", "orcid": "0000-0002-5997-3945", "affiliations": ["Department of Chemistry, Ume\u00e5 Centre for Microbial Research (UCMR), Ume\u00e5 University, 90187, Ume\u00e5, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/54d1a40e92fc4128ab2477ccc717e7d8.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/54d1a40e92fc4128ab2477ccc717e7d8"}}, "publications": [{"entity": "publication", "iuid": "fdb4d8f046da44318cf95213df74e7b7", "links": {"self": {"href": "https://publications.scilifelab.se/publication/fdb4d8f046da44318cf95213df74e7b7.json"}, "display": {"href": "https://publications.scilifelab.se/publication/fdb4d8f046da44318cf95213df74e7b7"}}, "title": "A tripartite cytolytic toxin formed by Vibrio cholerae proteins with flagellum-facilitated secretion.", "authors": [{"family": "Nadeem", "given": "Aftab", "initials": "A", "orcid": "0000-0002-1439-6216", "researcher": {"href": "https://publications.scilifelab.se/researcher/a672dd942f9b4ba0880210a8c7358227.json"}}, {"family": "Nagampalli", "given": "Raghavendra", "initials": "R"}, {"family": "Toh", "given": "Eric", "initials": "E", "orcid": "0000-0002-0103-0696", "researcher": {"href": "https://publications.scilifelab.se/researcher/70008894b990416fab9d4eb4627a3bc0.json"}}, {"family": "Alam", "given": "Athar", "initials": "A", "orcid": "0000-0001-8773-7598", "researcher": {"href": "https://publications.scilifelab.se/researcher/9d1da5164b7644b897ef05c40cec4606.json"}}, {"family": "Myint", "given": "Si Lhyam", "initials": "SL", "orcid": "0000-0001-5384-3691", "researcher": {"href": "https://publications.scilifelab.se/researcher/ec5ca92bae3a4dfab72f4a44d29f5a18.json"}}, {"family": "Heidler", "given": "Thomas V", "initials": "TV", "orcid": "0000-0002-5997-3945", "researcher": {"href": "https://publications.scilifelab.se/researcher/54d1a40e92fc4128ab2477ccc717e7d8.json"}}, {"family": "Dongre", "given": "Mitesh", "initials": "M"}, {"family": "Zlatkov", "given": "Nikola", "initials": "N", "orcid": "0000-0003-3318-9084", "researcher": {"href": "https://publications.scilifelab.se/researcher/c76ab107ec0e421b8b3d51f1807a0b9c.json"}}, {"family": "Pace", "given": "Hudson", "initials": "H"}, {"family": "Bano", "given": "Fouzia", "initials": "F", "orcid": "0000-0003-0634-7091", "researcher": {"href": "https://publications.scilifelab.se/researcher/af79c94518a4488ea0bd314793eb808c.json"}}, {"family": "Sj\u00f6stedt", "given": "Anders", "initials": "A", "orcid": "0000-0002-0768-8405", "researcher": {"href": "https://publications.scilifelab.se/researcher/52b15132704f48609be086c9d256cb14.json"}}, {"family": "Bally", "given": "Marta", "initials": "M", "orcid": "0000-0002-5865-8302", "researcher": {"href": "https://publications.scilifelab.se/researcher/923521b36e7746a3979801d0502eb6a9.json"}}, {"family": "Uhlin", "given": "Bernt Eric", "initials": "BE", "orcid": "0000-0002-2991-8072", "researcher": {"href": "https://publications.scilifelab.se/researcher/9faa19d33fd84728bb6df987ba16475f.json"}}, {"family": "Wai", "given": "Sun Nyunt", "initials": "SN", "orcid": "0000-0003-4793-4671", "researcher": {"href": "https://publications.scilifelab.se/researcher/261986c5cf8f48878b74c4f60cc7af69.json"}}, {"family": "Persson", "given": "Karina", "initials": "K", "orcid": "0000-0003-0807-0348", "researcher": {"href": "https://publications.scilifelab.se/researcher/75b999cf004141468eefb2504b7c5b99.json"}}], "type": "journal article", "published": "2021-11-23", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "118", "issue": "47", "issn-l": "0027-8424"}, "abstract": "The protein MakA was discovered as a motility-associated secreted toxin from Vibrio cholerae Here, we show that MakA is part of a gene cluster encoding four additional proteins: MakB, MakC, MakD, and MakE. MakA, MakB, and MakE were readily detected in culture supernatants of wild-type V. cholerae, whereas secretion was very much reduced from a flagellum-deficient mutant. Crystal structures of MakA, MakB, and MakE revealed a structural relationship to a superfamily of bacterial pore-forming toxins. Expression of MakA/B/E in Escherichia coli resulted in toxicity toward Caenorhabditis elegans used as a predatory model organism. None of these Mak proteins alone or in pairwise combinations were cytolytic, but an equimolar mixture of MakA, MakB, and MakE acted as a tripartite cytolytic toxin in vitro, causing lysis of erythrocytes and cytotoxicity on cultured human colon carcinoma cells. Formation of oligomeric complexes on liposomes was observed by electron microscopy. Oligomer interaction with membranes was initiated by MakA membrane binding followed by MakB and MakE joining the assembly of a pore structure. A predicted membrane insertion domain of MakA was shown by site-directed mutagenesis to be essential for toxicity toward C. elegans Bioinformatic analyses revealed that the makCDBAE gene cluster is present as a genomic island in the vast majority of sequenced genomes of V. cholerae and the fish pathogen Vibrio anguillarum We suggest that the hitherto-unrecognized cytolytic MakA/B/E toxin can contribute to Vibrionaceae fitness and virulence potential in different host environments and organisms.", "doi": "10.1073/pnas.2111418118", "pmid": "34799450", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "2111418118"}, {"db": "pmc", "key": "PMC8617504"}], "notes": [], "created": "2022-04-01T16:02:49.616Z", "modified": "2022-04-01T16:02:49.767Z"}, {"entity": "publication", "iuid": "af9a1d63cb8445088a21a8b5498b3f5a", "links": {"self": {"href": "https://publications.scilifelab.se/publication/af9a1d63cb8445088a21a8b5498b3f5a.json"}, "display": {"href": "https://publications.scilifelab.se/publication/af9a1d63cb8445088a21a8b5498b3f5a"}}, "title": "Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide.", "authors": [{"family": "Heidler", "given": "Thomas V", "initials": "TV", "orcid": "0000-0002-5997-3945", "researcher": {"href": "https://publications.scilifelab.se/researcher/54d1a40e92fc4128ab2477ccc717e7d8.json"}}, {"family": "Ernits", "given": "Karin", "initials": "K"}, {"family": "Ziolkowska", "given": "Agnieszka", "initials": "A"}, {"family": "Claesson", "given": "Rolf", "initials": "R"}, {"family": "Persson", "given": "Karina", "initials": "K", "orcid": "0000-0003-0807-0348", "researcher": {"href": "https://publications.scilifelab.se/researcher/75b999cf004141468eefb2504b7c5b99.json"}}], "type": "journal article", "published": "2021-01-25", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "4", "issue": "1", "pages": "106", "issn-l": "2399-3642"}, "abstract": "The Gram-negative bacterium Porphyromonas gingivalis is a secondary colonizer of the oral biofilm and is involved in the onset and progression of periodontitis. Its fimbriae, of type-V, are important for attachment to other microorganisms in the biofilm and for adhesion to host cells. The fimbriae are assembled from five proteins encoded by the mfa1 operon, of which Mfa5 is one of the ancillary tip proteins. Here we report the X-ray structure of the N-terminal half of Mfa5, which reveals a von Willebrand factor domain and two IgG-like domains. One of the IgG-like domains is stabilized by an intramolecular isopeptide bond, which is the first such bond observed in a Gram-negative bacterium. These features make Mfa5 structurally more related to streptococcal adhesins than to the other P. gingivalis Mfa proteins. The structure reported here indicates that horizontal gene transfer has occurred among the bacteria within the oral biofilm.", "doi": "10.1038/s42003-020-01621-w", "pmid": "33495563", "labels": {"Cryo-EM": "Collaborative"}, "xrefs": [{"db": "pii", "key": "10.1038/s42003-020-01621-w"}, {"db": "pmc", "key": "PMC7835359"}], "notes": [], "created": "2021-12-13T21:53:45.043Z", "modified": "2021-12-13T21:53:45.135Z"}]}