On the Lab. II building site

425 special CDSs in PCN033 (XLSX 29 kb

Additional file 6 of Genetic characterization of atypical porcine pestivirus from neonatal piglets with congenital tremor in Hubei province, China

Additional file 6: Sanger sequencing peak maps. The base quality values were shown in the Sanger sequencing peak maps

Additional file 3 of Genetic characterization of atypical porcine pestivirus from neonatal piglets with congenital tremor in Hubei province, China

Additional file 3: Table S1. Primers used for co-infection detection in this study

Additional file 5 of Genetic characterization of atypical porcine pestivirus from neonatal piglets with congenital tremor in Hubei province, China

Additional file 5: Table S3. Recombination events detection and analysis of all available APPV strains

Additional file 4 of Genetic characterization of atypical porcine pestivirus from neonatal piglets with congenital tremor in Hubei province, China

Additional file 4: Table S2. Primers used for APPV genome amplification in this study

Large-Scale Identification of Bacteria–Host Crosstalk by Affinity Chromatography: Capturing the Interactions of <i>Streptococcus suis</i> Proteins with Host Cells

Protein–protein interactions between bacteria and their hosts are responsible for all types of infection processes. The investigation of the bacteria–host crosstalk can provide a comprehensive understanding of the pathogenesis of bacterial disease. Despite scattered efforts in this field, a systematic identification of interactions between host and bacterial proteins remains unavailable. Here, we develop ACSP (affinity chromatography-based surface proteomics), which combines affinity chromatography and shotgun proteomics (LC–MS/MS), to investigate the interactions on a large-scale. Using ACSP, the potential surface interacting proteins (SIPs) of Streptococcus suis serotype 2 (SS2) were captured by the chromatographic resin, which was immobilized with the native surface molecules of Hep-2 cells. And then 40 potential SIPs were identified from the preys by LC–MS/MS, including 3 SIPs that have been previously reported in the literature. We selected 8 important SIPs and confirmed their ability to adhere to Hep-2 cells. Additionally, 3 newly identified SIPs, or their polyclonal antibodies, were found to significantly inhibit the adherence of SS2 to Hep-2 cells, indicating their essential role in the interaction between SS2 and Hep-2 cells. Using this example, we show that ACSP represents a new valuable tool for investigating the bacteria–host interactions

Large-Scale Identification of Bacteria–Host Crosstalk by Affinity Chromatography: Capturing the Interactions of <i>Streptococcus suis</i> Proteins with Host Cells

Protein–protein interactions between bacteria and their hosts are responsible for all types of infection processes. The investigation of the bacteria–host crosstalk can provide a comprehensive understanding of the pathogenesis of bacterial disease. Despite scattered efforts in this field, a systematic identification of interactions between host and bacterial proteins remains unavailable. Here, we develop ACSP (affinity chromatography-based surface proteomics), which combines affinity chromatography and shotgun proteomics (LC–MS/MS), to investigate the interactions on a large-scale. Using ACSP, the potential surface interacting proteins (SIPs) of Streptococcus suis serotype 2 (SS2) were captured by the chromatographic resin, which was immobilized with the native surface molecules of Hep-2 cells. And then 40 potential SIPs were identified from the preys by LC–MS/MS, including 3 SIPs that have been previously reported in the literature. We selected 8 important SIPs and confirmed their ability to adhere to Hep-2 cells. Additionally, 3 newly identified SIPs, or their polyclonal antibodies, were found to significantly inhibit the adherence of SS2 to Hep-2 cells, indicating their essential role in the interaction between SS2 and Hep-2 cells. Using this example, we show that ACSP represents a new valuable tool for investigating the bacteria–host interactions

Additional file 1: Table S1. of Isolation and full-genome sequencing of Seneca Valley virus in piglets from China, 2016

List of primers used in the study. (DOCX 19 kb

Additional file 1 of Egr-1 is a key regulator of the blood-brain barrier damage induced by meningitic Escherichia coli

Additional file 1

Large-Scale Identification of Bacteria–Host Crosstalk by Affinity Chromatography: Capturing the Interactions of <i>Streptococcus suis</i> Proteins with Host Cells

Protein–protein interactions between bacteria and their hosts are responsible for all types of infection processes. The investigation of the bacteria–host crosstalk can provide a comprehensive understanding of the pathogenesis of bacterial disease. Despite scattered efforts in this field, a systematic identification of interactions between host and bacterial proteins remains unavailable. Here, we develop ACSP (affinity chromatography-based surface proteomics), which combines affinity chromatography and shotgun proteomics (LC–MS/MS), to investigate the interactions on a large-scale. Using ACSP, the potential surface interacting proteins (SIPs) of Streptococcus suis serotype 2 (SS2) were captured by the chromatographic resin, which was immobilized with the native surface molecules of Hep-2 cells. And then 40 potential SIPs were identified from the preys by LC–MS/MS, including 3 SIPs that have been previously reported in the literature. We selected 8 important SIPs and confirmed their ability to adhere to Hep-2 cells. Additionally, 3 newly identified SIPs, or their polyclonal antibodies, were found to significantly inhibit the adherence of SS2 to Hep-2 cells, indicating their essential role in the interaction between SS2 and Hep-2 cells. Using this example, we show that ACSP represents a new valuable tool for investigating the bacteria–host interactions