Showing papers on "Pore forming protein published in 2007"
TL;DR: The OmpA outer membrane protein of Escherichia coli and other enterobacteria is a multifaceted protein that can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages.
Abstract: The OmpA outer membrane protein of Escherichia coli and other enterobacteria is a multifaceted protein. This protein is expressed to very high levels and ompA is tightly regulated at the posttranscriptional level. It can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages. Many of these properties are due to four short protein loops that emanate from the protein to the outside of the cell. Herein it is described how the structure of this protein relates to its many functions.
369 citations
TL;DR: Crystal structures of PFO are presented that reveal a detailed molecular pathway that may be the basis for the allosteric transition that occurs on initial membrane binding leading to the exposure of membrane-spanning regions in a domain distant from the initial site of interaction.
85 citations
TL;DR: Results indicate that pore forming proteins (PFP) and amyloid oligomers share structural homology and suggest that PFPs and ameloid oligomeric pores and perforin share the same mechanism of membrane permeabilization.
Abstract: Degenerative diseases such as Alzheimer's, Parkinson's, and Huntington's diseases are believed to be causally related to the accumulation of amyloid oligomers that exhibit a common structure and may be toxic by a common mechanism involving permeabilization of membranes. We discovered that amyloid oligomers and the pore-forming bacterial toxin, alpha-hemolysin (alpha HL), as well as human perforin from cytotoxic T lymphocytes, share a structural and functional homology at the level of their common reactivity with a conformation-dependent antibody that is specific for amyloid oligomers, A11. The alpha HL oligomeric pores and partially folded alpha HL protomer, but not the monomer alpha HL precursor reacts with A11 antibody. A11 antibody inhibits the hemolytic activity of alpha HL, indicating that the structural homology is functionally significant. Perforin oligomers were also recognized by A11. Amyloidogenic properties of alpha HL and perforin were confirmed spectroscopically and morphologically. These results indicate that pore forming proteins (PFP) and amyloid oligomers share structural homology and suggest that PFPs and amyloid oligomers share the same mechanism of membrane permeabilization.
77 citations
TL;DR: It is shown that CLIC2 forms pH-dependent chloride channels in vitro with higher channel activity at low pH levels and that the channels are subject to redox regulation.
68 citations
TL;DR: The transmembrane protein TatA is the pore forming unit of the twin-arginine translocase (Tat), which has the unique ability of transporting folded proteins across the cell membrane, to obtain insight in the translocation mechanism.
42 citations
TL;DR: This study presents a first characterisation of YtfM by comparison to YaeT concerning structural, biochemical and electrophysiological properties and reveals that ytfM is a non-essential gene and lack of the protein had no effect on outer membrane composition and integrity.
Abstract: Omp85 proteins form a ubiquitous protein family, members of which are found in all Gram-negative bacteria. Omp85 of Neisseria meningitidis and YaeT of Escherichia coli are shown to be essential for outer membrane biogenesis. Interestingly, there exists a homologue to YaeT in E. coli and many proteobacteria, denoted YtfM, the function of which has not been described yet. Like YaeT, YtfM is predicted to consist of an amino-terminal periplasmic domain and a membrane-located carboxy-terminal domain. In this study, we present a first characterisation of YtfM by comparison to YaeT concerning structural, biochemical and electrophysiological properties. Furthermore, a knockout strain revealed that ytfM is a non-essential gene and lack of the protein had no effect on outer membrane composition and integrity. The only observable phenotype was strongly reduced growth, indicating an important role of YtfM in vivo.
23 citations
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TL;DR: Perforin-2 (P2) molecule is a pore forming protein The 5' untranslated region of the perforin2 protein controls translational activity Compositions include the Perforin protein and the 5' bounding box region as discussed by the authors.
Abstract: Perforin-2 (P2) molecule is a pore forming protein The 5 ' untranslated region of the perforin-2 protein controls translational activity Compositions include the perforin protein and the 5' untranslated region Methods of use include high-throughput screening assays for identification of therapeutic compounds in treatment of diseases
4 citations