Unfoldase-mediated protein translocation through an α-hemolysin nanopore [PDF]
Nature Biotechnology, 2013 Using nanopores to sequence biopolymers was proposed more than a decade ago. Recent advances in enzyme-based control of DNA translocation and in DNA nucleotide resolution using modified biological pores have satisfied two technical requirements of a functional nanopore DNA sequencing device. Nanopore sequencing of proteins was also envisioned. Although
Jeff Nivala, D. Marks, M. Akeson
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Hemolysin Co-regulated Family Proteins Hcp1 and Hcp2 Contribute to Edwardsiella ictaluri Pathogenesis [PDF]
Frontiers in Veterinary Science, 2021 Edwardsiella ictaluri is a Gram-negative facultative intracellular pathogen causing enteric septicemia of catfish (ESC), a devastating disease resulting in significant economic losses in the U.S. catfish industry. Bacterial secretion systems are involved
Safak Kalindamar +4 more
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Staphylococcus aureus alpha-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells. [PDF]
PLoS ONE, 2009 Community Acquired Methicillin Resistant Staphylococcus aureus (CA-MRSA) causes severe necrotizing infections of the skin, soft tissues, and lungs. Staphylococcal alpha-hemolysin is an essential virulence factor in mouse models of CA-MRSA necrotizing ...
Robin R Craven +7 more
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Microbial Cell Factories, 2012 Background Extracellular expression of proteins has an absolute advantage in a large-scale industrial production. In our previous study, Thermobifida fusca cutinase, an enzyme mainly utilized in textile industry, was expressed via type II secretory ...
Su Lingqia +5 more
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TolC, an Escherichia coli outer membrane protein required for hemolysin secretion. [PDF]
Proceedings of the National Academy of Sciences, 1990 Secretion of Escherichia coli alpha-hemolysin into the medium does not require the cleavage of an N-terminal signal peptide. The specific secretion apparatus was shown to consist of two proteins, HlyB and HlyD, both located in the inner membrane and encoded by genes contiguous to the hemolysin structural gene (hlyA).
C. Wandersman, P. Delepelaire
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Acylation of Escherichia coli Hemolysin: A Unique Protein Lipidation Mechanism Underlying Toxin Function [PDF]
Microbiology and Molecular Biology Reviews, 1998 SUMMARYThe pore-forming hemolysin (HlyA) of Escherichia coli represents a unique class of bacterial toxins that require a posttranslational modification for activity. The inactive protoxin pro-HlyA is activated intracellularly by amide linkage of fatty acids to two internal lysine residues 126 amino acids apart, directed by the cosynthesized HlyC ...
P. Stanley, V. Koronakis, C. Hughes
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Secretome analysis of Aspergillus fumigatus reveals Asp-hemolysin as a major secreted protein.
International Journal of Medical Microbiology, 2011 Surface-associated and secreted proteins represent primarily exposed components of Aspergillus fumigatus during host infection. Several secreted proteins are known to be involved in defense mechanisms or immune evasion, thus, probably contributing to pathogenicity.
Dirk Wartenberg +6 more
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Identification of two neutralizing human single-chain variable fragment antibodies targeting Staphylococcus aureus alpha-hemolysin [PDF]
Iranian Journal of Basic Medical Sciences, 2022 Objective(s): The inability of the host immune system to defeat Staphylococcus aureus is due to various secreted virulent factors such as leukocidins, superantigens, and hemolysins, which interrupt the function of immune components.
Somayeh Piri-Gavgani +5 more
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Use of black soldier fly (Hermetia illucens) prepupae amino acids as anti Aeromonas hydrophila enterotoxin in vivo [PDF]
Iraqi Journal of Veterinary Sciences, 2023 Aeromonas hydrophila is an opportunistic freshwater. These bacteria cause gastroenteritis and septicemia in animals and humans. Hemolysin and aerolysin, are important in the pathogenesis of A. hydrophila.
Dahliatul Qosimah +5 more
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The hemolysin A secretion system is a multi-engine pump containing three ABC transporters.
Cell, 2022 Type 1 secretion systems (T1SSs) are widespread in pathogenic Gram-negative bacteria, extruding protein substrates following synthesis of the entire polypeptide.
Hongtu Zhao, James Lee, Jue Chen
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