Results 21 to 30 of about 1,369,932 (286)

Pore-Forming Toxins Trigger the Purge [PDF]

Cell Host & Microbe, 2016
The intestinal epithelium responds to pathogens by coordinating microbial elimination with tissue repair, both required to survive an infection. In this issue of Cell Host & Microbe, Lee et al. (2016) discover a rapid and evolutionarily conserved response to pore-forming toxins in the gut, involving cytoplasm ejection and enterocyte regrowth.
Alessandro, Bonfini, Nicolas, Buchon
openaire   +2 more sources

Structural and evolutionary properties of Brevibacillus laterosporus Mpp75Aa1.1, an ETX_MTX2 β-pore-forming protein.

, 2021
(A) Cartoon representation of the Mpp75Aa1.1 crystal structure. Domain I, the transmembrane pore-forming β-hairpin, and the carboxyl-terminal peptide, are colored in slate, green, and magenta, respectively.
Yong Yin (51909), Jun Zhang (48506), Yoonseong Park (231356), Stephen Duff (11547247), Eric Bretsnyder (11547253), Jason Milligan (9707545), Chunsheng Xia (4180507), Michael Aikins (3508022), Meiying Zheng (11547250), Artem Evdokimov (2106010), Jeffrey Haas (5215904), Timothy Rydel (3022389), Jeffrey Nageotte (11547256), Kara Giddings (11547259), Agoston Jerga (2987889), Jean-Louis Kouadio (9707548), Danqi Chen (1314816), William Moar (127463)   +17 more
core   +1 more source

Clostridium perfringensepsilon toxin H149A mutant as a platform for receptor binding studies [PDF]

, 2013
Clostridium perfringens epsilon toxin (Etx) is a pore-forming toxin responsible for a severe and rapidly fatal enterotoxemia of ruminants. The toxin is classified as a category B bioterrorism agent by the U.S.
Titball, R.W., Richard W. Titball, Bokori-Brown, M., Kokkinidou, M.C., Claire E. Naylor, Fernandes da Costa, S.P., Moss, David S., Monika Bokori‐Brown, Maria C. Kokkinidou, David S. Moss, Basak, Ajit K., Cole, Ambrose R., Sérgio Fernandes da Costa, Naylor, Claire E., Ambrose R. Cole, Christos G. Savva, Ajit K. Basak, Savva, Christos G.   +17 more
core   +1 more source

Enhanced SnapShot: Pore-Forming Toxins [PDF]

Cell, 2010
Enhanced SnapShots include features only possible online—animations, embedded captions, and dynamic visuals—all accessible by the click of a mouse. The goal of an Enhanced SnapShot is to provide everything currently available with the print SnapShot plus additional layers of information that are accessible through an easy to navigate interface.The ...
Mueller M, Ban N
openaire   +3 more sources

Dominant negative phenotype of Bacillus thuringiensis Cry1Ab, Cry11Aa and Cry4Ba mutants suggest hetero-oligomer formation among different Cry toxins. [PDF]

, 2011
Background - Bacillus thuringiensis Cry toxins are used worldwide in the control of different insect pests important in agriculture or in human health. The Cry proteins are pore-forming toxins that affect the midgut cell of target insects.
Leivi Portugal, Maagd, R.A., de, Daniela Carmona, Alejandra Bravo, Portugal, L., Bakker, P., Perez, C., Claudia Rodríguez-Almazán, Mario Soberón, Bravo, A., Rodriguez-Almazan, C., Carmona, D., Claudia Pérez, Soberon, M., Carlos Muñoz-Garay, Ruud A de Maagd, Munoz-Garay, C., Petra Bakker, Carmona Daniela, Portugal Leivi, Soberón Mario, de Maagd Ruud A., Ruud A. de Maagd, Pérez Claudia, Bakker Petra, Bravo Alejandra, Muñoz-Garay Carlos, Rodríguez-Almazán Claudia   +27 more
core   +1 more source

The Pore-forming Toxin Proaerolysin Is Activated by Furin [PDF]

Journal of Biological Chemistry, 1998
Aerolysin is secreted as an inactive dimeric precursor by the bacterium Aeromonas hydrophila. Proteolytic cleavage within a mobile loop near the C terminus of the protoxin is required for oligomerization and channel formation. This loop contains the sequence KVRRAR432, which should be recognized by mammalian proprotein convertases such as furin, PACE4,
Abrami, L., Fivaz, M., Decroly, E., Seidah, N. G., Jean, F., Thomas, G., Leppla, S. H., Buckley, J. T., van der Goot, F. G.   +8 more
openaire   +5 more sources

Bacterial pore-forming toxins

Microbiology, 2022
Pore-forming toxins (PFTs) are widely distributed in both Gram-negative and Gram-positive bacteria. PFTs can act as virulence factors that bacteria utilise in dissemination and host colonisation or, alternatively, they can be employed to compete with rival microbes in polymicrobial niches. PFTs transition from a soluble form to become membrane-embedded
Fatima R. Ulhuq, Giuseppina Mariano
openaire   +3 more sources

DEFENSE AND DEATH RESPONSES TO PORE FORMING TOXINS [PDF]

Biotechnology and Genetic Engineering Reviews, 2009
Pore forming toxins (PFT) are important virulence factors produced by bacteria to kill eukaryotic cells by forming holes in the cellular membrane. They represent a diverse group of proteins with a wide range of target cells. Although the amino acid sequence is not conserved among the different PFT, many of them share some aspects of their mechanism of ...
Angeles, Cancino-Rodezno, Helena, Porta, Mario, Soberon, Alejandra, Bravo   +3 more
openaire   +2 more sources

Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane

Nature Communications, 2021
The Vip3 family proteins from Bacillus thuringiensis are thought to exert their insecticidal activity through pore formation. Here authors present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms and show the activated ...
Matthew J. Byrne, Matthew G. Iadanza, Marcos Arribas Perez, Daniel P. Maskell, Rachel M. George, Emma L. Hesketh, Paul A. Beales, Marc D. Zack, Colin Berry, Rebecca F. Thompson   +9 more
doaj   +1 more source

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin [PDF]

, 2019
ABC toxins are pore-forming virulence factors produced by pathogenic bacteria. YenTcA is the pore-forming and membrane binding A subunit of the ABC toxin YenTc, produced by the insect pathogen Yersinia entomophaga.
Busby, Jason N., Piper, Sarah J, Lott, J. Shaun, Hurst, Mark RH, Schepers, Femke, Ve, Thomas, Landsberg, Michael J, Hurst, Mark R. H., Stahlberg, Henning, Hartley-Tassell, Lauren, Goldie, Kenneth N., Jones, Sandra A., Piper, Sarah J., Goldie, Kenneth N, Chassagnon, Irene, Busby, Jason N, Landsberg, Michael J., Box, Joseph K., Hankamer, Ben, Box, Joseph K, Scherer, Sebastian, Brillault, Lou, Lott, J Shaun, Dalziel, Julie E., Rothnagel, Rosalba, Jones, Sandra A, Croll, Tristan I., Croll, Tristan, Hurst, Mark R H, Dalziel, Julie E, Hartley-Tassell L, Stahlberg H, Jones SA, Chassagnon I, Hankamer B, Rothnagel R, Dalziel JE, Box JK, Schepers F, Piper SJ, Goldie KN, Croll TI, Scherer S, Brillault L, Ve T, Busby JN, Hurst MRH, Landsberg MJ, Lott JS   +48 more
core   +2 more sources