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

Chen, Bin; Zhang, Anding; Xu, Zhongmin; Li, Ran; Chen, Huanchun; Jin, Meilin

doi:10.1021/pr200758q

Cited by 25 publications

(20 citation statements)

References 70 publications

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“…These were proposed as vaccine candidates especially as they are reasonably conserved among S. suis strains [93]. A combination of affinity chromatography and surface proteomics using LC-MS/MS [94] has identified 40 potential surface interacting proteins of S. suis although the majority of the identified proteins were intra-cellular rather than cell wall in origin and also showed that eight proteins further investigated were involved in the bacteria binding to Hep-2 cells.…”

Section: Bacterial Diseasesmentioning

confidence: 99%

The pig as an animal model for human pathologies: A proteomics perspective

Bassols

Costa

Eckersall

et al. 2014

Proteomics Clinical Apps

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Traditional biomedical models are easy to manage in experimental facilities and allow fast and affordable basic genetic studies related to human disorders, but in some cases they do not always represent the complexity of their physiology. Translational medicine demands selected models depending on the particularities of the human disease to be investigated, reproducing as closely as possible the evolution, clinical symptoms and molecular pathways, cells or tissues involved in the dysfunction. Thus, pig models offer an alternative because of their anatomical and physiological similarities to humans and the availability of genomic, transcriptomic and, progressively more, proteomic tools for analysis of this species. Furthermore, there is a wide range of natural, selected and transgenic porcine breeds. The present review provides a summary of the applications of the pig as a model for metabolic, cardiovascular, infectious diseases, xenotransplantation and neurological disorders and an overview of the possibilities that the diverse proteomic techniques offer to study these pathologies in depth.

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Section: Bacterial Diseasesmentioning

confidence: 99%

The pig as an animal model for human pathologies: A proteomics perspective

Bassols

Costa

Eckersall

et al. 2014

Proteomics Clinical Apps

226

158

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“…Recently high-throughput proteomic analysis has been applied for identification of relevant host–pathogen protein–protein interaction [ 22 , 23 ]. Moreover, affinity chromatography combined with shotgun proteomics analysis has been practiced for investigating the interactions between Streptococcus suis proteins and host cells [ 24 ].…”

Section: Introductionmentioning

confidence: 99%

Investigation of host–pathogen interaction between Burkholderia pseudomallei and autophagy-related protein LC3 using hydrophobic chromatography-based technique

et al. 2017

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Background Burkholderia pseudomallei is an intracellular bacteria causing Melioidosis, the disease widely disseminates in Southeast Asia and Northern Australia. B. pseudomallei has ability to invade various types of host cell and to interfere with host defense mechanisms, such as nitric oxide (NO). Due to the cross-talk among alternative killing mechanisms in host immune response against invading microbes, autophagy is the molecular mechanism belonging to intracellular elimination of eukaryotic cells that has been widely discussed. However, bacterial evasion strategy of B. pseudomallei and host-bacterial protein–protein interaction within autophagic machinery remain unknown.MethodsHere, we demonstrated the protein–protein interaction study between different strains of B. pseudomallei, including wild type PP844 and rpoS mutant, with autophagy-related protein LC3 that has been constructed, using the modified immunoaffinity hydrophobic chromatography based-technique. Liquid chromatography tandem-mass spectrometry (LC–MS/MS) analysis was utilized for identifying the eluted proteins obtained from the established column. In addition, the expression level of gene encoding candidate protein was predicted prior to verification using real-time quantitative reverse transcription PCR assay (RT-qPCR).ResultsLC3 recombinant proteins could be entrapped inside the column before encountering their bacterial interacting partners. Based on affinity interaction, the binding capacity of LC3 with antibody displayed over 50% readily for hydrophobically binding with bacterial proteins. Following protein identification, bacterial ATP-binding cassette (ABC) transporter periplasmic substrate-binding protein (BPSL2203) was identified as a candidate LC3-interacting protein, which was found only in B. pseudomallei wild type. Gene expression analysis and bioinformatics of BPSL2203 were validated the proteomic result which are suggesting the role of RpoS-dependent gene regulation.ConclusionsRemarkably, utilization of the modified immunoaffinity hydrophobic chromatography with LC–MS/MS is a convenient and reliable approach to a study in B. pseudomallei-LC3 protein–protein interaction.Electronic supplementary materialThe online version of this article (doi:10.1186/s13578-017-0172-4) contains supplementary material, which is available to authorized users.

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“…Suilysin, the extracellular protein factor, along with a muramidase-released protein have also been shown to be linked to, but not essential for, the full virulence of S. suis [21]. GapdH [22], Enolase [23], [24], Fibronectin/Fibrinogen-binding protein [25], HAM1 [26] and Adhesion [27], [28], [29], [30], [31], [32] have been shown to be involved in S. suis adherence and virulence. Serum opacity-like factor [33], D-Alanylation of Lipoteichoic Acid [34], Peptidoglycan GlcNAc deacetylase [35], IgA protease [36], [37], TroA [38], SodA [39], SsFHB [40] and Subtilisin-like serine protease [41], [42], [43] are also considered to be related to S. suis virulence.…”

Section: Introductionmentioning

confidence: 99%

HP0197 Contributes to CPS Synthesis and the Virulence of Streptococcus suis via CcpA

et al. 2012

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Streptococcus suis serotype 2 (SS2), a major swine pathogen and an emerging zoonotic agent, has greatly challenged global public health. The encoding proteins with unknown functions the bacterium encodes are an obstruction to studies of the pathogenesis. A novel surface protective antigen HP0197 is one of these proteins which have no sequence homology to any known protein. In the present study, the protein was determined to be involved in bacterial virulence through an evaluation of the isogenic mutant (Δhp0197) in both mice and pigs. The experimental infection also indicated that Δhp0197 could be cleared easily during infection, which could be attributed to the reduced thickness of the capsular polysaccharides (CPS) and the significantly reduced phagocytotic resistance. Microarrays-based comparative transcriptome analysis suggested that the suppressed expression of the operon responsible for CPS synthesis might be reversed by CcpA activity, which controlled global regulation of carbon catabolite through the binding of the CcpA and HPr-Ser-46-P to the catabolite-responsive elements (cre) of the target operons. The hypothesis was approved by the fact that the purified FLAG-tagged HPr from WT stain exhibited a higher binding activity to cre with CcpA compared to the Δhp0197 by the Electrophoretic Mobility Shift Assay, suggesting lower level of phosphorylation of the phosphocarrier protein HPr at residue Ser-46 (HPr-Ser-46P) in Δhp0197. These indicated that HP0197 could enhance CcpA activity to control the expression of genes involved in carbohydrate utilization and CPS synthesis, thus contributing to the virulence of S. suis.

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

Cited by 25 publications

References 70 publications

The pig as an animal model for human pathologies: A proteomics perspective

The pig as an animal model for human pathologies: A proteomics perspective

Investigation of host–pathogen interaction between Burkholderia pseudomallei and autophagy-related protein LC3 using hydrophobic chromatography-based technique

HP0197 Contributes to CPS Synthesis and the Virulence of Streptococcus suis via CcpA

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