Literature DB >> 15694862

Bacterial interactions with the eukaryotic secretory pathway.

Suzana P Salcedo1, David W Holden.   

Abstract

Pathogenic bacteria exploit a wide variety of host cellular processes to adhere to, invade, replicate within and damage host cells. One such process is the eukaryotic secretory pathway, in which proteins and lipids are modified and transported from the endoplasmic reticulum through the Golgi network to the plasma membrane and other cellular destinations. Certain bacteria secrete toxins that utilise this transport pathway to reach their cellular targets. Some intracellular pathogens, including Legionella, Brucella and Chlamydia, engage other steps of the pathway to establish intracellular replicative organelles. Recent work has implicated specific virulence proteins of enterohaemorrhagic Escherichia coli and Salmonella enterica in secretory pathway interactions.

Entities:  

Mesh:

Substances:

Year:  2005        PMID: 15694862     DOI: 10.1016/j.mib.2004.12.007

Source DB:  PubMed          Journal:  Curr Opin Microbiol        ISSN: 1369-5274            Impact factor:   7.934


  23 in total

1.  Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA.

Authors:  Yongqun Zhu; Liyan Hu; Yan Zhou; Qing Yao; Liping Liu; Feng Shao
Journal:  Proc Natl Acad Sci U S A       Date:  2010-02-22       Impact factor: 11.205

Review 2.  Make it or take it: fatty acid metabolism of apicomplexan parasites.

Authors:  Jolly Mazumdar; Boris Striepen
Journal:  Eukaryot Cell       Date:  2007-08-22

3.  Loss of a membrane trafficking protein αSNAP induces non-canonical autophagy in human epithelia.

Authors:  Nayden G Naydenov; Gianni Harris; Victor Morales; Andrei I Ivanov
Journal:  Cell Cycle       Date:  2012-11-27       Impact factor: 4.534

Review 4.  The current Salmonella-host interactome.

Authors:  Sylvia Schleker; Jingchun Sun; Balachandran Raghavan; Matthew Srnec; Nicole Müller; Mary Koepfinger; Leelavati Murthy; Zhongming Zhao; Judith Klein-Seetharaman
Journal:  Proteomics Clin Appl       Date:  2011-12-27       Impact factor: 3.494

5.  Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A.

Authors:  Yury Belyi; Ricarda Niggeweg; Bastian Opitz; Martin Vogelsgesang; Stefan Hippenstiel; Matthias Wilm; Klaus Aktories
Journal:  Proc Natl Acad Sci U S A       Date:  2006-10-26       Impact factor: 11.205

6.  Salmonella acquires lysosome-associated membrane protein 1 (LAMP1) on phagosomes from Golgi via SipC protein-mediated recruitment of host Syntaxin6.

Authors:  Richa Madan; Ruchir Rastogi; Seetharaman Parashuraman; Amitabha Mukhopadhyay
Journal:  J Biol Chem       Date:  2011-12-21       Impact factor: 5.157

7.  Quantitative Yeast Genetic Interaction Profiling of Bacterial Effector Proteins Uncovers a Role for the Human Retromer in Salmonella Infection.

Authors:  Kristin L Patrick; Jason A Wojcechowskyj; Samantha L Bell; Morgan N Riba; Tao Jing; Sara Talmage; Pengbiao Xu; Ana L Cabello; Jiewei Xu; Michael Shales; David Jimenez-Morales; Thomas A Ficht; Paul de Figueiredo; James E Samuel; Pingwei Li; Nevan J Krogan; Robert O Watson
Journal:  Cell Syst       Date:  2018-08-01       Impact factor: 10.304

Review 8.  Salmonella pathogenicity and host adaptation in chicken-associated serovars.

Authors:  Steven L Foley; Timothy J Johnson; Steven C Ricke; Rajesh Nayak; Jessica Danzeisen
Journal:  Microbiol Mol Biol Rev       Date:  2013-12       Impact factor: 11.056

9.  Pathogenic Bacterial Proteins and their Anti-Inflammatory Effects in the Eukaryotic Host.

Authors:  Jun Sun
Journal:  Antiinflamm Antiallergy Agents Med Chem       Date:  2009-09-01

10.  Contribution of phosphatidylserine to membrane surface charge and protein targeting during phagosome maturation.

Authors:  Tony Yeung; Bryan Heit; Jean-Francois Dubuisson; Gregory D Fairn; Basil Chiu; Robert Inman; Andras Kapus; Michele Swanson; Sergio Grinstein
Journal:  J Cell Biol       Date:  2009-06-01       Impact factor: 10.539

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.