Structural Characterization of TssL from Acinetobacter baumannii: a Key Component of the Type VI Secretion System

Author:

Ruiz Federico M.1ORCID,Lopez Juvenal2,Ferrara C. Gastón34,Santillana Elena1,Espinosa Yanis R.5,Feldman Mario F.2,Romero Antonio1

Affiliation:

1. Chemical and Physical Biology, Centro de Investigaciones Biológicas Margarita Salas, Madrid, Spain

2. Department of Molecular Microbiology, Washington University School of Medicine in St. Louis, St. Louis, Missouri, USA

3. School of Engineering and Agronomy, National University Arturo Jauretche, Florencio Varela, Argentina

4. Institute of Physics of Liquids and Biological Systems (IFLYSIB), CONICET-National University of La Plata, La Plata, Argentina

5. Grupo de Bioquímica Teórica, Universidad Industrial de Santander, Bucaramanga, Colombia

Abstract

Several Acinetobacter species carry one functional type VI secretion system (T6SS). The T6SS is encoded in a single locus containing 16 conserved genes, most of which code for proteins essential to T6SS activity. One of these key components is TssL, a cytoplasmic protein bound to the inner membrane. Despite its importance and its particular characteristics, the structure of T6SS in A. baumannii remains understudied. Here, we present structural, in silico , and in vivo studies of TssL, highlighting the importance of two well-conserved residues and improving our understanding of this secretion system in this bacterium.

Funder

HHS | National Institutes of Health

Ministerio de Economía y Competitividad

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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