An approach to chimeric subunit immunogen provides efficient protection against toxicity, type III and type v secretion systems of Shigella

2021 ◽  
Vol 100 ◽  
pp. 108132
Author(s):  
Alireza Felegary ◽  
Shahram Nazarian ◽  
Emad Kordbacheh ◽  
Javad Fathi ◽  
Mohamad Ebrahim Minae
Author(s):  
Enguo Fan ◽  
Nandini Chauhan ◽  
D. B. R. K. Gupta Udatha ◽  
Jack C. Leo ◽  
Dirk Linke

2016 ◽  
Vol 4 (1) ◽  
Author(s):  
Enguo Fan ◽  
Nandini Chauhan ◽  
D. B. R. K. Gupta Udatha ◽  
Jack C. Leo ◽  
Dirk Linke

2012 ◽  
Vol 367 (1592) ◽  
pp. 1088-1101 ◽  
Author(s):  
Jack C. Leo ◽  
Iwan Grin ◽  
Dirk Linke

Autotransport in Gram-negative bacteria denotes the ability of surface-localized proteins to cross the outer membrane (OM) autonomously. Autotransporters perform this task with the help of a β-barrel transmembrane domain localized in the OM. Different classes of autotransporters have been investigated in detail in recent years; classical monomeric but also trimeric autotransporters comprise many important bacterial virulence factors. So do the two-partner secretion systems, which are a special case as the transported protein resides on a different polypeptide chain than the transporter. Despite the great interest in these proteins, the exact mechanism of the transport process remains elusive. Moreover, different periplasmic and OM factors have been identified that play a role in the translocation, making the term ‘autotransport’ debatable. In this review, we compile the wealth of details known on the mechanism of single autotransporters from different classes and organisms, and put them into a bigger perspective. We also discuss recently discovered or rediscovered classes of autotransporters.


2019 ◽  
Vol 10 ◽  
Author(s):  
Ina Meuskens ◽  
Athanasios Saragliadis ◽  
Jack C. Leo ◽  
Dirk Linke

2013 ◽  
Vol 394 (11) ◽  
pp. 1385-1398 ◽  
Author(s):  
Iris Gawarzewski ◽  
Sander H.J. Smits ◽  
Lutz Schmitt ◽  
Joachim Jose

Abstract Pathogenic gram-negative bacteria have evolved several secretion mechanisms to translocate adhesins, enzymes, toxins, and other virulence factors across the inner and outer membranes. Currently, eight different secretion systems, type I–type VIII (T1SS–T8SS) plus the chaperone-usher (CU) pathway, have been identified, which act in one-step or two-step mechanisms to traverse both membrane barriers. The type V secretion system (T5SS) is dependent first on the Sec translocon within the inner membrane. The periplasmic intermediates are then secreted through aqueous pores formed by β-barrels in the outer membrane. Until now, transport across the outer membrane has not been understood on a molecular level. With respect to special characteristics revealed by crystal structure analysis, bioinformatic and biochemical data, five subgroups of T5SS were defined. Here, we compare the transport moieties of members of four subgroups based on X-ray crystal structures. For the fifth subgroup, which was identified only recently, no structures have thus far been reported. We also discuss different models for the translocation process across the outer membrane with respect to recent findings.


2002 ◽  
Vol 184 (21) ◽  
pp. 5966-5970 ◽  
Author(s):  
Sarah E. Burr ◽  
Katja Stuber ◽  
Thomas Wahli ◽  
Joachim Frey

ABSTRACT Aeromonas salmonicida subsp. salmonicida, the etiological agent of furunculosis, is an important fish pathogen. We have screened this bacterium with a broad-host-range probe directed against yscV, the gene that encodes the archetype of a highly conserved family of inner membrane proteins found in every known type III secretion system. This has led to the identification of seven open reading frames that encode homologues to proteins functioning within the type III secretion systems of Yersinia species. Six of these proteins are encoded by genes comprising a virA operon. The A. salmonicida subsp. salmonicida yscV homologue, ascV, was inactivated by marker replacement mutagenesis and used to generate an isogenic ascV mutant. Comparison of the extracellular protein profiles from the ascV mutant and the wild-type strain indicates that A. salmonicida subsp. salmonicida secretes proteins via a type III secretion system. The recently identified ADP-ribosylating toxin AexT was identified as one such protein. Finally, we have compared the toxicities of the wild-type A. salmonicida subsp. salmonicida strain and the ascV mutant against RTG-2 rainbow trout gonad cells. While infection with the wild-type strain results in significant morphological changes, including cell rounding, infection with the ascV mutant has no toxic effect, indicating that the type III secretion system we have identified plays an important role in the virulence of this pathogen.


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