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The Many Faces of IpaB

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Date 2016 Feb 24
PMID 26904511
Citations 12
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Abstract

The type III secretion system (T3SS) is Shigella's most important virulence factor. The T3SS apparatus (T3SA) is comprised of an envelope-spanning basal body and an external needle topped by a tip complex protein called IpaD. This nanomachine is used to deliver effector proteins into host cells to promote pathogen entry. A key component of the matured T3SS needle tip complex is the translocator protein IpaB. IpaB can exist in multiple states when prepared as a recombinant protein, however, it has also been described as having additional roles in Shigella pathogenesis. This mini-review will briefly describe some of the features of IpaB as a T3SS needle tip protein, as a pore-forming translocator protein and as an effector protein. Reflection on the potential importance of the different in vitro states of IpaB on its function and importance in serotype-independent vaccines is also provided.

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References
1.
Lafont F, Tran van Nhieu G, Hanada K, Sansonetti P, van der Goot F . Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interaction. EMBO J. 2002; 21(17):4449-57. PMC: 126195. DOI: 10.1093/emboj/cdf457. View

2.
Cordes F, Komoriya K, Larquet E, Yang S, Egelman E, Blocker A . Helical structure of the needle of the type III secretion system of Shigella flexneri. J Biol Chem. 2003; 278(19):17103-7. DOI: 10.1074/jbc.M300091200. View

3.
Hume P, McGhie E, Hayward R, Koronakis V . The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology. Mol Microbiol. 2003; 49(2):425-39. DOI: 10.1046/j.1365-2958.2003.03559.x. View

4.
Watarai M, Funato S, Sasakawa C . Interaction of Ipa proteins of Shigella flexneri with alpha5beta1 integrin promotes entry of the bacteria into mammalian cells. J Exp Med. 1996; 183(3):991-9. PMC: 2192368. DOI: 10.1084/jem.183.3.991. View

5.
Kubori T, Matsushima Y, Nakamura D, Uralil J, Lara-Tejero M, Sukhan A . Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science. 1998; 280(5363):602-5. DOI: 10.1126/science.280.5363.602. View