title: Crystal Structure of an Invasivity-Associated Domain of SdrE in S. aureus.
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.
authors.affiliation: 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.|Department of Laboratory Medicine, People's Hospital of YuBei District, YuBei District, Chongqing, People's Republic of China.
authors.forename: Miao
authors.initials: M
authors.lastname: Luo
authors.affiliation: 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.
authors.forename: Xiang
authors.initials: X
authors.lastname: Zhang
authors.affiliation: Department of Laboratory Medicine, Chongqing Medical University, YixueYuanlu-1, Chongqing, People's Republic of China.
authors.forename: Shaocheng
authors.initials: S
authors.lastname: Zhang
authors.affiliation: 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.
authors.forename: Hongpeng
authors.initials: H
authors.lastname: Zhang
authors.affiliation: Department of Laboratory Medicine, Hospital of Zhejiang, Xihu District, Hangzhou, People's Republic of China.
authors.forename: Wei
authors.initials: W
authors.lastname: Yang
authors.affiliation: School of Life Science, the University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
authors.forename: Zhongliang
authors.initials: Z
authors.lastname: Zhu
authors.affiliation: 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.
authors.forename: Ke
authors.initials: K
authors.lastname: Chen
authors.affiliation: 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.
authors.forename: Lei
authors.initials: L
authors.lastname: Bai
authors.affiliation: 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.
authors.forename: Jie
authors.initials: J
authors.lastname: Wei
authors.affiliation: 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.
authors.forename: Ailong
authors.initials: A
authors.lastname: Huang
authors.affiliation: 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.|Department of Laboratory Medicine, Chongqing Medical University, YixueYuanlu-1, Chongqing, People's Republic of China.
authors.forename: Deqiang
authors.initials: D
authors.lastname: Wang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D001665:Binding Sites; D045744:Cell Line, Tumor; D003001:Cloning, Molecular; D050716:Complement C4b-Binding Protein / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D017242:Complement Factor H / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006367:HeLa Cells; D054884:Host-Pathogen Interactions; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry / Q000235:genetics; D008024:Ligands; D008958:Models, Molecular; D009154:Mutation; D010006:Osteoblasts / Q000276:immunology / Q000382:microbiology; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000472:pathogenicity
chemical_list: D001426:Bacterial Proteins; C055609:C4BPA protein, human; D050716:Complement C4b-Binding Protein; D007074:Immunoglobulin G; D008024:Ligands; D011994:Recombinant Proteins; C118507:SdrE protein, Staphylococcus aureus; D017242:Complement Factor H