Structural basis for effector recognition by an antibacterial type IV secretion system-Reference-Cited by-同舟云学术

Structural basis for effector recognition by an antibacterial type IV secretion system

Published:2021-12-30 Issue:1 Volume:119 Page:
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proc. Natl. Acad. Sci. U.S.A.

Author:

Oka Gabriel U.¹,Souza Diorge P.¹^ORCID,Cenens William¹,Matsuyama Bruno Y.¹,Cardoso Marcus V. C.¹^ORCID,Oliveira Luciana C.¹^ORCID,da Silva Lima Filipe¹,Cuccovia Iolanda M.¹^ORCID,Guzzo Cristiane R.¹²,Salinas Roberto K.¹^ORCID,Farah Chuck S.¹^ORCID

Affiliation:

1. Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo 05508-000, SP, Brazil;

2. Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo 05508-000, SP, Brazil

Abstract

Significance Type IV secretion systems (T4SSs) have been studied for more than 70 y because of their roles in mediating horizontal DNA transfer, responsible for the spread of antibiotic resistance, and the injection of virulence factors into animal and plant hosts. Another important function is the contact-dependent injection of toxic effectors into competing bacteria of different species during bacterial warfare. The present study reveals how T4SSs use a specific domain of the VirD4 coupling protein to recruit antibacterial toxins for secretion by recognizing conserved carboxyl-terminal secretion signal domains. The molecular structure of the secretion signal domain described in this work will serve as a model for thousands of homologs encountered in several hundred distinct bacterial species.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Link

https://pnas.org/doi/pdf/10.1073/pnas.2112529119

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