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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Structure of Internalin InIK from the Human Pathogen Listeria monocytogenes

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Autor(es):
Neves, David [1] ; Job, Viviana [2, 3, 4] ; Dortet, Laurent [5, 6, 7] ; Cossart, Pascale [5, 6, 7] ; Dessen, Andrea [2, 3, 4, 1]
Número total de Autores: 5
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 7
Tipo de documento: Artigo Científico
Fonte: Journal of Molecular Biology; v. 425, n. 22, p. 4520-4529, NOV 15 2013.
Citações Web of Science: 10
Resumo

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)

Processo FAPESP: 11/52067-6 - Estruturação de complexos macromoleculares da parede bacteriana: biossíntese e virulência
Beneficiário:Andrea Dessen de Souza e Silva
Linha de fomento: Auxílio à Pesquisa - Programa SPEC