Crystal Structure of an Invasivity-Associated Domain of SdrE in S. aureus

Miao Luo; Xiang Zhang; Shaocheng Zhang; Hongpeng Zhang; Wei Yang; Zhongliang Zhu; Ke Chen; Lei Bai; Jie Wei; Ailong Huang; Deqiang Wang

doi:10.1371/journal.pone.0168814

Crystal Structure of an Invasivity-Associated Domain of SdrE in S. aureus

PLoS One. 2017 Jan 26;12(1):e0168814. doi: 10.1371/journal.pone.0168814. eCollection 2017.

Authors

Miao Luo^{1

2}, Xiang Zhang¹, Shaocheng Zhang³, Hongpeng Zhang¹, Wei Yang⁴, Zhongliang Zhu⁵, Ke Chen¹, Lei Bai¹, Jie Wei¹, Ailong Huang¹, Deqiang Wang^{1

3}

Affiliations

¹ Key Laboratory of Molecular Biology for Infectious Diseases (Ministry of Education), Institute for Viral Hepatitis, Department of Infectious Diseases, The Second Affiliated Hospital, Chongqing Medical University, Chongqing, PR China.
² Department of Laboratory Medicine, People's Hospital of YuBei District, YuBei District, Chongqing, People's Republic of China.
³ Department of Laboratory Medicine, Chongqing Medical University, YixueYuanlu-1, Chongqing, People's Republic of China.
⁴ Department of Laboratory Medicine, Hospital of Zhejiang, Xihu District, Hangzhou, People's Republic of China.
⁵ School of Life Science, the University of Science and Technology of China, Hefei, Anhui, People's Republic of China.

Abstract

The surface protein SdrE, a microbial surface components recognizing adhesive matrix molecule (MSCRAMM) family protein expressed on the surface of Staphylococcus aureus (S. aureus), can recognize human complement regulator Factor H and C4BP, thus making it a potentially promising vaccine candidate. In this study, SdrE278-591 was found to directly affect S. aureus host cell invasion. Additionally, the crystal structure of SdrE278-591 at a resolution of 1.25 Å was established, with the three-dimensional structure revealing N2-N3 domains which fold in a manner similar to an IgG fold. Furthermore, a putative ligand binding site located at a conserved charged groove formed by the interface between N2 and N3 domains was identified, with β2 suspected to occupy the ligand recognizing site and undergo a structural rearrangement to allow ligand binding. Overall, these findings have further contributed to the understanding of SdrE as a key factor for S. aureus invasivity and will enable a better understanding of bacterial infection processes.

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / immunology
Binding Sites
Cell Line, Tumor
Cloning, Molecular
Complement C4b-Binding Protein / chemistry*
Complement C4b-Binding Protein / genetics
Complement C4b-Binding Protein / immunology
Complement Factor H / chemistry*
Complement Factor H / genetics
Crystallography, X-Ray
Escherichia coli / genetics
Escherichia coli / metabolism
Gene Expression
HeLa Cells
Host-Pathogen Interactions
Humans
Immunoglobulin G / chemistry
Immunoglobulin G / genetics
Ligands
Models, Molecular
Mutation*
Osteoblasts / immunology
Osteoblasts / microbiology
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Folding
Protein Interaction Domains and Motifs
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / immunology
Staphylococcus aureus / chemistry*
Staphylococcus aureus / pathogenicity

Substances

Bacterial Proteins
C4BPA protein, human
Complement C4b-Binding Protein
Immunoglobulin G
Ligands
Recombinant Proteins
SdrE protein, Staphylococcus aureus
Complement Factor H

Grants and funding

This research was supported by a grant (2013ZX10002002-003-002) from the National Science and Technology Major Projects, a grant (81301395) from the Chinese National Natural Science Foundation and a grant (cstc2015jcyjA10003) from the Chongqing Natural Science Foundation.