Structural studies of proteins related to the infection process by Enterococcus fe...
| Full text | |
| Author(s): |
Neves, David
[1]
;
Job, Viviana
[2, 3, 4]
;
Dortet, Laurent
[5, 6, 7]
;
Cossart, Pascale
[5, 6, 7]
;
Dessen, Andrea
[2, 3, 4, 1]
Total Authors: 5
|
| Affiliation: | [1] CNPEM, Brazilian Natl Lab Biosci LNBio, Sao Paulo - Brazil
[2] Univ Grenoble 1, Inst Biol Struct, Bacterial Pathogenesis Grp, F-38027 Grenoble - France
[3] Commissariat Energie Atom, Grenoble - France
[4] Ctr Natl Rech Sci, Grenoble - France
[5] Inst Pasteur, Unite Interact Bacteries Cellules, F-75015 Paris - France
[6] INSERM, F-75015 Paris - France
[7] INRA, USC2020, F-75015 Paris - France
Total Affiliations: 7
|
| Document type: | Journal article |
| Source: | Journal of Molecular Biology; v. 425, n. 22, p. 4520-4529, NOV 15 2013. |
| Web of Science Citations: | 10 |
| Abstract | |
Listeria monocytogenes is a human pathogen that employs a wide variety of virulence factors in order to adhere to, invade, and replicate within target cells. Internalins play key roles in processes ranging from adhesion to receptor recognition and are thus essential for infection. Recently, InIK, a surface-associated internalin, was shown to be involved in Listeria's ability to escape from autophagy by recruitment of the major vault protein (MVP) to the bacterial surface. Here, we report the structure of InIK, which harbors four domains arranged in the shape of a ``bent arm{''}. The structure supports a role for the ``elbow{''} of InIK in partner recognition, as well as of two Ig-like pedestals intercalated by hinge regions in the projection of InIK away from the surface of the bacterium. The unusual fold and flexibility of InIK could be essential for MVP binding and concealment from recognition by molecules involved in the autophagic process. (C) 2013 Elsevier Ltd. All rights reserved. (AU) | |
| FAPESP's process: | 11/52067-6 - Assembly and structure of macromolecular complexes involved in bacterial cell wall: biosynthesis and virulence |
| Grantee: | Andrea Dessen de Souza e Silva |
| Support type: | Research Projects - SPEC Program |