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Questions and Answers (3) View all
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Answer added in Bioinformatics and Computational Biology7 How can novel virulence factors be predicted in bacterial genomes? Are there any computational methods?By Ram · Indian Council of Medical ResearchRoland Arnold · University of TorontoHi, this is not a trivial problem, depends if you fish for known stuff (like transport systems) or unknown stuff (like effector proteins). For the lat... [more]Hi, this is not a trivial problem, depends if you fish for known stuff (like transport systems) or unknown stuff (like effector proteins). For the latter case, there are (at least for Type III secreted proteins) several prediction tools available. It also depends on the species of interest: in some bacteria, virulence factors are "organized" in pathogenicity islands which might be detectable.... Here some papers of interest: http://www.plospathogens.org/article/info%3Adoi%2F10.1371%2Fjournal.ppat.1000508 (prediction of type IV secreted virulence factors in Legionella http://www.plospathogens.org/article/info%3Adoi%2F10.1371%2Fjournal.ppat.1000376 http://www.plospathogens.org/article/info%3Adoi%2F10.1371%2Fjournal.ppat.1000375 http://www.biomedcentral.com/1471-2105/13/66/abstract some databases: http://biocomputer.bio.cuhk.edu.hk/T3DB/ http://www.effectors.org/ (prediction of TTSS secreted proteins and databases/online tools) hope this helps a little bit...Following
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Answer added in Bioinformatics and Computational Biology5 Where to look to find all (known) sequences binding to a specific protein?By Francesco Rao · Universität FreiburgRoland Arnold · University of TorontoHi: as Pawel said, STRING contains predicted guys as well. Perhaps you want to have a look here, they have verified binders to the PDZ domain: http://... [more]Hi: as Pawel said, STRING contains predicted guys as well. Perhaps you want to have a look here, they have verified binders to the PDZ domain: http://elm.eu.org/elms/browse_elms.html?q=pdz&submit=submit&reset_form=Reset Also have a look into the domino-database at http://mint.bio.uniroma2.it/domino/search/searchWelcome.do For PPI in general a comprehensive is iRefWeb. However, you will not know if these guys are mediated by the PDZ domain or not.Following
Publications (27) View all
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Article: Computational analysis of interactomes: Current and future perspectives for bioinformatics approaches to model the host-pathogen interaction space.
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ABSTRACT: Bacterial and viral pathogens affect their eukaryotic host partly by interacting with proteins of the host cell. Hence, to investigate infection from a systems' perspective we need to construct complete and accurate host-pathogen protein-protein interaction networks. Because of the paucity of available data and the cost associated with experimental approaches, any construction and analysis of such a network in the near future has to rely on computational predictions. Specifically, this challenge consists of a number of sub-problems: First, prediction of possible pathogen interactors (e.g. effector proteins) is necessary for bacteria and protozoa. Second, the prospective host binding partners have to be determined and finally, the impact on the host cell analyzed. This review gives an overview of current bioinformatics approaches to obtain and understand host-pathogen interactions. As an application example of the methods covered, we predict host-pathogen interactions of Salmonella and discuss the value of these predictions as a prospective for further research.Methods 06/2012; 57(4):508-18. · 4.01 Impact Factor -
SourceAvailable from: PubMed Central
Article: SIMAP--a comprehensive database of pre-calculated protein sequence similarities, domains, annotations and clusters.
Thomas Rattei, Patrick Tischler, Stefan Götz, Marc-André Jehl, Jonathan Hoser, Roland Arnold, Ana Conesa, Hans-Werner Mewes[show abstract] [hide abstract]
ABSTRACT: The prediction of protein function as well as the reconstruction of evolutionary genesis employing sequence comparison at large is still the most powerful tool in sequence analysis. Due to the exponential growth of the number of known protein sequences and the subsequent quadratic growth of the similarity matrix, the computation of the Similarity Matrix of Proteins (SIMAP) becomes a computational intensive task. The SIMAP database provides a comprehensive and up-to-date pre-calculation of the protein sequence similarity matrix, sequence-based features and sequence clusters. As of September 2009, SIMAP covers 48 million proteins and more than 23 million non-redundant sequences. Novel features of SIMAP include the expansion of the sequence space by including databases such as ENSEMBL as well as the integration of metagenomes based on their consistent processing and annotation. Furthermore, protein function predictions by Blast2GO are pre-calculated for all sequences in SIMAP and the data access and query functions have been improved. SIMAP assists biologists to query the up-to-date sequence space systematically and facilitates large-scale downstream projects in computational biology. Access to SIMAP is freely provided through the web portal for individuals (http://mips.gsf.de/simap/) and for programmatic access through DAS (http://webclu.bio.wzw.tum.de/das/) and Web-Service (http://mips.gsf.de/webservices/services/SimapService2.0?wsdl).Nucleic Acids Research 11/2009; 38(Database issue):D223-6. · 8.03 Impact Factor -
SourceAvailable from: Stefan Brandmaier
Article: Sequence-based prediction of type III secreted proteins.
Roland Arnold, Stefan Brandmaier, Frederick Kleine, Patrick Tischler, Eva Heinz, Sebastian Behrens, Antti Niinikoski, Hans-Werner Mewes, Matthias Horn, Thomas Rattei[show abstract] [hide abstract]
ABSTRACT: The type III secretion system (TTSS) is a key mechanism for host cell interaction used by a variety of bacterial pathogens and symbionts of plants and animals including humans. The TTSS represents a molecular syringe with which the bacteria deliver effector proteins directly into the host cell cytosol. Despite the importance of the TTSS for bacterial pathogenesis, recognition and targeting of type III secreted proteins has up until now been poorly understood. Several hypotheses are discussed, including an mRNA-based signal, a chaperon-mediated process, or an N-terminal signal peptide. In this study, we systematically analyzed the amino acid composition and secondary structure of N-termini of 100 experimentally verified effector proteins. Based on this, we developed a machine-learning approach for the prediction of TTSS effector proteins, taking into account N-terminal sequence features such as frequencies of amino acids, short peptides, or residues with certain physico-chemical properties. The resulting computational model revealed a strong type III secretion signal in the N-terminus that can be used to detect effectors with sensitivity of approximately 71% and selectivity of approximately 85%. This signal seems to be taxonomically universal and conserved among animal pathogens and plant symbionts, since we could successfully detect effector proteins if the respective group was excluded from training. The application of our prediction approach to 739 complete bacterial and archaeal genome sequences resulted in the identification of between 0% and 12% putative TTSS effector proteins. Comparison of effector proteins with orthologs that are not secreted by the TTSS showed no clear pattern of signal acquisition by fusion, suggesting convergent evolutionary processes shaping the type III secretion signal. The newly developed program EffectiveT3 (http://www.chlamydiaedb.org) is the first universal in silico prediction program for the identification of novel TTSS effectors. Our findings will facilitate further studies on and improve our understanding of type III secretion and its role in pathogen-host interactions.PLoS Pathogens 05/2009; 5(4):e1000376. · 9.13 Impact Factor -
SourceAvailable from: Ulrich Güldener
Article: PEDANT covers all complete RefSeq genomes.
Mathias C Walter, Thomas Rattei, Roland Arnold, Ulrich Güldener, Martin Münsterkötter, Karamfilka Nenova, Gabi Kastenmüller, Patrick Tischler, Andreas Wölling, Andreas Volz, Norbert Pongratz, Ralf Jost, Hans-Werner Mewes, Dmitrij Frishman[show abstract] [hide abstract]
ABSTRACT: The PEDANT genome database provides exhaustive annotation of nearly 3000 publicly available eukaryotic, eubacterial, archaeal and viral genomes with more than 4.5 million proteins by a broad set of bioinformatics algorithms. In particular, all completely sequenced genomes from the NCBI's Reference Sequence collection (RefSeq) are covered. The PEDANT processing pipeline has been sped up by an order of magnitude through the utilization of precalculated similarity information stored in the similarity matrix of proteins (SIMAP) database, making it possible to process newly sequenced genomes immediately as they become available. PEDANT is freely accessible to academic users at http://pedant.gsf.de. For programmatic access Web Services are available at http://pedant.gsf.de/webservices.jsp.Nucleic Acids Research 11/2008; 37(Database issue):D408-11. · 8.03 Impact Factor -
SourceAvailable from: Jan Krumsiek
Article: SIMAP--structuring the network of protein similarities.
Thomas Rattei, Patrick Tischler, Roland Arnold, Franz Hamberger, Jörg Krebs, Jan Krumsiek, Benedikt Wachinger, Volker Stümpflen, Werner Mewes[show abstract] [hide abstract]
ABSTRACT: Protein sequences are the most important source of evolutionary and functional information for new proteins. In order to facilitate the computationally intensive tasks of sequence analysis, the Similarity Matrix of Proteins (SIMAP) database aims to provide a comprehensive and up-to-date dataset of the pre-calculated sequence similarity matrix and sequence-based features like InterPro domains for all proteins contained in the major public sequence databases. As of September 2007, SIMAP covers approximately 17 million proteins and more than 6 million non-redundant sequences and provides a complete annotation based on InterPro 16. Novel features of SIMAP include a new, portlet-based web portal providing multiple, structured views on retrieved proteins and integration of protein clusters and a unique search method for similar domain architectures. Access to SIMAP is freely provided for academic use through the web portal for individuals at http://mips.gsf.de/simap/and through Web Services for programmatic access at http://mips.gsf.de/webservices/services/SimapService2.0?wsdl.Nucleic Acids Research 02/2008; 36(Database issue):D289-92. · 8.03 Impact Factor