Author | Soares, Talyta do Nascimento | |
Author | Valadares, Verônica Silva | |
Author | Amorim, Gisele Cardoso | |
Author | Carvalho, Mayara de Mattos Lacerda de | |
Author | Pinho, Marcia Berrêdo | |
Author | Almeida, Fábio Ceneviva Lacerda | |
Author | Bisch, Paulo Mascarello | |
Author | Batista, Paulo Ricardo | |
Author | Lery, Letícia Miranda Santos | |
Access date | 2022-06-15T19:28:06Z | |
Available date | 2022-06-15T19:28:06Z | |
Document date | 2022 | |
Citation | SOARES, Talyta do Nascimento et al. The C-terminal extension of VgrG4 from Klebsiella pneumoniae remodels host cell microfilaments. Proteins, p. 1 - 14, 2022. | pt_BR |
ISSN | 1097-0134 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/53285 | |
Language | eng | pt_BR |
Publisher | Wiley | pt_BR |
Rights | open access | |
Subject in Portuguese | Interações bactéria-hospedeiro | pt_BR |
Subject in Portuguese | Citoesqueleto | pt_BR |
Subject in Portuguese | Interações proteína-proteína | pt_BR |
Subject in Portuguese | Proteômica | pt_BR |
Subject in Portuguese | T6SS | pt_BR |
Title | The C-terminal extension of VgrG4 from Klebsiella pneumoniae remodels host cell microfilaments | pt_BR |
Type | Article | |
DOI | 10.1002/prot.26344 | |
Abstract | Klebsiella pneumoniae is an opportunistic pathogen, which concerns public health systems
worldwide, as multiple antibiotic-resistant strains are frequent. One of its pathogenicity
factors is the Type VI Secretion System (T6SS), a macromolecular complex
assembled through the bacterial membranes. T6SS injects effector proteins inside
target cells. Such effectors confer competitive advantages or modulate the target cell
signaling and metabolism to favor bacterial infection. The VgrG protein is a T6SS core
component. It may present a variable C-terminal domain carrying an additional
effector function. Kp52.145 genome encodes three VgrG proteins, one of them with
a C-terminal extension (VgrG4-CTD). VgrG4-CTD is 138 amino acids long, does not
contain domains of known function, but is conserved in some Klebsiella, and non-
Klebsiella species. To get insights into its function, recombinant VgrG4-CTD was used
in pulldown experiments to capture ligands from macrophages and lung epithelial
cells. A total of 254 proteins were identified: most of them are ribosomal proteins.
Cytoskeleton-associated and proteins involved in the phagosome maturation pathway
were also identified. We further showed that VgrG4-CTD binds actin and
induces actin remodeling in macrophages. This study presents novel clues on the role
of K. pneumoniae T6SS in pathogenesis. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. NUMPEX-Bio. Duque de Caxias, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. NUMPEX-Bio. Duque de Caxias, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica. Centro Nacional de Ressonância Magnética Nuclear. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Física-Biológica. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Programa de Computação Científica. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Bacterium–host interactions | pt_BR |
Subject | Cytoskeleton | pt_BR |
Subject | Protein–protein interactions | pt_BR |
Subject | Proteomics | pt_BR |
Subject | T6SS | pt_BR |