Advanced search
Start date
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

tructural basis for effector recognition by an antibacterial type IV secretion syste

Full text
Show less -
Oka, Gabriel U. [1] ; Souza, Diorge P. [1, 2] ; Cenens, William [1] ; Matsuyama, Bruno Y. [1] ; Cardoso, Marcus V. C. [1, 3] ; Oliveira, Luciana C. [1, 4] ; Lima, Filipe da Silva [1, 5] ; Cuccovia, Iolanda M. [1] ; Guzzo, Cristiane R. [1, 6] ; Salinas, Roberto K. [1] ; Farah, Chuck S. [1]
Total Authors: 11
[1] Univ Sao Paulo, Inst Chem, Dept Biochem, BR-05508000 Sao Paulo, SP - Brazil
[2] MRC Lab Mol Biol, Div Cell Biol, Cambridge CB2 0QH - England
[3] Univ Fed Ouro Preto, Inst Exact & Biol Sci, Dept Chem, BR-35400000 Ouro Preto - Brazil
[4] Nmx Res & Solut Inc, Laval, PQ H7V 5B7 - Canada
[5] Univ Fed Pernambuco, Dept Fundamental Chem, Ctr Exact & Nat Sci, BR-50754056 Recife, PE - Brazil
[6] Univ Sao Paulo, Inst Biomed Sci, Dept Microbiol, BR-05508000 Sao Paulo, SP - Brazil
Total Affiliations: 6
Document type: Journal article
Web of Science Citations: 0

Many soil-, water-, and plant-associated bacterial species from the orders Xanthomonadales, Burkholderales, and Neisseriales carry a type IV secretion system (T4SS) specialized in translocating effector proteins into other gram-negative species, leading to target cell death. These effectors, known as X-Tfes, carry a carboxyl-terminal domain of similar to 120 residues, termed XVIPCD, characterized by several conserved motifs and a glutamine-rich tail. Previous studies showed that the XVIPCD is required for interaction with the T4SS coupling protein VirD4 and for T4SS-dependent translocation. However, the structural basis of the XVIPCD-VirD4 interaction is unknown. Here, we show that the XVIPCD interacts with the central all-alpha domain of VirD4 (VirD4(AAD)). We used solution NMR spectroscopy to solve the structure of the XVIPCD of X-Tfe(XAC2609) from Xanthomonas citri and to map its interaction surface with VirD4(AAD). Isothermal titration calorimetry and in vivo Xanthomonas citri versus Escherichia coli competition assays using wild-type and mutant X-Tfe(XAC2609) and X-Tfe(X4C3634) indicate that XVIPCD5 can be divided into two regions with distinct functions: the well-folded N-terminal region contains specific conserved motifs that are responsible for interactions with VirD4(AAD), while both N- and carboxyl-terminal regions are required for effective X-Tfe translocation into the target cell. The conformational stability of the N-terminal region is reduced at and below pH 7.0, a property that may facilitate X-Tfe unfolding and translocation through the more acidic environment of the periplasm. (AU)

FAPESP's process: 18/09277-9 - Investigation of the structural requirements for recognition of T4SS-related toxins by the coupling protein VirD4.
Grantee:Gabriel Umaji Oka
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 15/18237-2 - Genetic elucidation of the functional and regulatory mechanisms underlying the Type IV Secretion System in Xanthomonas citri and how it mediates contact dependent killing
Grantee:William Cenens
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 17/17303-7 - Structure and function of bacterial secretion systems
Grantee:Shaker Chuck Farah
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 16/00458-5 - Structural and functional characterization of Xanthomonas citri type IV secretion system.
Grantee:Bruno Yasui Matsuyama
Support Opportunities: Scholarships in Brazil - Post-Doctoral