The Structural Basis for a Transition State That Regulates Pore Formation in a Bacterial Toxin

Autor: Kristin R. Wade, Sara L. Lawrence, Allison J. Farrand, Eileen M. Hotze, Michael J. Kuiper, Michael A. Gorman, Michelle P. Christie, Santosh Panjikar, Craig J. Morton, Michael W. Parker, Rodney K. Tweten

Publikováno v: mBio, Vol 10, Iss 2 (2019)

ABSTRACT The cholesterol-dependent cytolysin (CDC) genes are present in bacterial species that span terrestrial, vertebrate, and invertebrate niches, which suggests that they have evolved to function under widely different environmental conditions. U

Externí odkaz: https://doaj.org/article/7bf35b5ddc6847bfb07b9a7eda692855

Circulating hyaluronan as a marker of endothelial glycocalyx damage in dogs with myxomatous mitral valve disease and dogs in a hypercoagulable state

Autor: Sara J. Lawrence-Mills, Melanie J. Hezzell, Sophie E. Adamantos, Iris Chan, Kieran Borgeat, Jessie Rose Payne, Simon Satchell, Gavin I. Welsh, Rebecca R. Foster, Natalie Finch

Publikováno v: Lawrence-Mills, S, Hezzell, M J, Adamantos, S E, Chan, I, Borgeat, K, Payne, J R, Satchell, S C, Welsh, G I, Foster, R R & Finch, N C 2022, ' Circulating hyaluronan as a marker of endothelial glycocalyx damage in dogs with myxomatous mitral valve disease and dogs in a hypercoagulable state ', Veterinary Journal, vol. 285, 105845 . https://doi.org/10.1016/j.tvjl.2022.105845

The endothelial glycocalyx (eGlx) lines the luminal surface of endothelial cells, maintaining vascular health. Glycocalyx damage is pathophysiologically important in many diseases across species however few studies have investigated its breakdown in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d82f253e02295c1e1a479b6bebaab13f
https://doi.org/10.1016/j.tvjl.2022.105845

Two-component pore formation by the novel CDCL proteins ALY short and ALY long from Elizabethkingia anophelis

Autor: Bronte A. Johnstone, Sara L. Lawrence, Craig J. Morton, Jordan C. Evans, Michelle P. Christie, Rodney K. Tweten, Michael W. Parker

Publikováno v: Acta Crystallographica Section A Foundations and Advances. 77:C482-C482

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::aebf7163b44927d1c3e3f00dfd46ea40
https://doi.org/10.1107/s0108767321092047

Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation

Autor: Sara L. Lawrence, Michael W. Parker, Rodney K. Tweten, Terrence D. Mulhern, Susanne C. Feil, Craig J. Morton, Kristin R. Wade, Allison J. Farrand, Michael A. Gorman

Publikováno v: Scientific Reports

Pore-forming proteins are weapons often used by bacterial pathogens to breach the membrane barrier of target cells. Despite their critical role in infection important structural aspects of the mechanism of how these proteins assemble into pores remai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::253a34a0bd8739a79afec423e416a94c
https://pubmed.ncbi.nlm.nih.gov/26403197

Manipulating the Lewis antigen specificity of the cholesterol-dependent cytolysin lectinolysin

Autor: Sara L. Lawrence, Rodney K. Tweten, Susanne C. Feil, Terrence D. Mulhern, Michael J. Kuiper, Michael W. Parker, Jessica K. Holien, Larissa Doughty, Olan Dolezal

Publikováno v: Frontiers in Immunology, Vol 3 (2012)
Frontiers in Immunology

The cholesterol-dependent cytolysins (CDCs) attack cells by punching large holes in their membranes. Lectinolysin from Streptococcus mitis is unique among CDCs due to the presence of an N-terminal lectin domain that enhances the pore-forming activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33d3cdc9ccf6045a380f92509b69eaba
https://doi.org/10.3389/fimmu.2012.00330