ORCID Profile
0000-0001-6605-9556
Current Organisation
University of Veterinary Medicine Vienna
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Publisher: Public Library of Science (PLoS)
Date: 05-07-2012
Publisher: Informa UK Limited
Date: 07-2005
Publisher: Public Library of Science (PLoS)
Date: 05-02-2015
Publisher: Wiley
Date: 22-09-2010
DOI: 10.1111/J.1399-0039.2010.01566.X
Abstract: The membrane-attack complex (MAC) of complement pathway and perforin (PF) are important tools deployed by the immune system to target pathogens. Both perforin and the C9 component of the MAC contain a common 'MACPF' domain and form pores in the cell membrane as part of their function. The MAC targets gram-negative bacteria and certain pathogenic parasites, while perforin, released by natural killer cells or cytotoxic T lymphocytes (CTLs), targets virus-infected and transformed host cells (1). Remarkably, recent structural studies show that the MACPF domain is homologous to the pore-forming portion of bacterial cholesterol-dependent cytolysins these data have provided important insight into the mechanism of pore-forming MACPF proteins. In addition to their role in immunity, MACPF family members have been identified as animal venoms, factors required for pathogen migration across host cell membranes and factors that govern developmental processes such as embryonic patterning and neuronal guidance (2). While most MACPF proteins characterized to date either form pores or span lipid membranes, some do not (e.g. the C6 component of the MAC). A current challenge is thus to understand the role, pore forming or otherwise, of MACPF proteins in developmental biology. This review discusses structural and functional ersity of the mammalian MACPF proteins.
Publisher: Wiley
Date: 21-03-2011
DOI: 10.1111/J.1758-2229.2011.00246.X
Abstract: Pseudoalteromonas tunicata is a marine bacterium that was originally isolated from the surface of the tunicate Ciona intestinalis. Since C. intestinalis expresses extracellular matrix (ECM) and P. tunicata has a gene encoding a functional ECM-binding protein, we hypothesized that P. tunicata could adhere to this host via protein-ECM interactions and as a result change its membrane proteome. An in vitro adhesion assay was developed to show that P. tunicata adheres strongly to ECM. To further study the adhesion biology of P. tunicata, two-dimensional (2D) electrophoresis was used to explore the membrane-associated sub-proteome of P. tunicata during planktonic, adherent and non-adherent states. More than 30 proteins were resolved using blue native (BN)/SDS 2D PAGE, many of which were identified by mass spectrometry. BN/SDS PAGE also allowed the identification of several novel protein complexes, which indicate structural and functional relationships for these proteins and related proteins in several other organisms. A proteomic change associated with adhesion was identified by comparison of 2D gels from the three model states. Collectively, these studies explore the membrane proteome of P. tunicata during the transition from planktonic to ECM-adherent states.
Publisher: Elsevier BV
Date: 07-2010
DOI: 10.1016/J.VETMIC.2010.01.027
Abstract: Pasteurella multocida is a ubiquitous pathogen which causes a range of diseases in erse animal species. Components of the bacterial outer membrane, such as trans membrane proteins and lipoproteins, play key roles in the interaction of the pathogen with the host environment and in the host immune response to infection. In this review, we evaluate the current knowledge of P. multocida outer membrane proteins and their role in pathogenesis and immunity.
Publisher: American Society for Microbiology
Date: 11-2008
DOI: 10.1128/AAC.00245-08
Abstract: Two TolC homologs, PM0527 and PM1980, were identified for Pasteurella multocida . A pm0527 mutant displayed increased susceptibility to a range of chemicals, including rif in (512-fold) and acridine orange (128-fold). A pm1980 mutant showed increased susceptibility to rif in, ceftazidime, and vancomycin.
Publisher: American Chemical Society (ACS)
Date: 12-2017
Location: Australia
No related grants have been discovered for Tamas Hatfaludi.