Research Support, Non-U.S. Gov'ts
- The Identification of Six Novel Proteins with Fibronectin or Collagen Type І Binding Activity from Streptococcus suis Serotype 2
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Hui Zhang , Junxi Zheng , Li Yi , Yue Li , Zhe Ma , Hongjie Fan , Chengping Lu
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J. Microbiol. 2014;52(11):963-969. Published online October 31, 2014
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DOI: https://doi.org/10.1007/s12275-014-4311-x
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Abstract
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Streptococcus suis, a major swine pathogen, is an emerging zoonotic agent that causes meningitis and septic shock. Bacterial cell wall and secreted proteins are often involved in interactions with extracellular matrix proteins (ECMs), which play important roles in the initial steps of pathogenesis. In this study, 2D SDS-PAGE, western blotting-based binding affinity measurements, and microtiter plate binding assays were used to identify cell wall and secreted proteins from S. suis that interact with fibronectin and collagen type І. We identified six proteins from S. suis, including three proteins (translation elongation factor G, oligopeptide-binding protein
OppA precursor, and phosphoglycerate mutase) that show both fibronectin and collagen type І binding activity. To the best of our knowledge, these three newly identified proteins had no previously reported fibronectin or collagen type І binding activity. Overall, the aim in this study was to identify proteins with ECM binding activity from S. suis and it represents the first report of six new proteins from S. suis
that interact with fibronectin or collagen type І.
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Citations
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Yanyan Zhang, Rui Li, Qian Li, Yongwei Zhu, Xiaopei Yang, Di Zhao, Bingbing Zong
BMC Veterinary Research.2023;[Epub] CrossRef - Schistosoma mansoni phosphoglycerate mutase: a glycolytic ectoenzyme with thrombolytic potential
David B. Pirovich, Akram A. Da’dara, Patrick J. Skelly
Parasite.2022; 29: 41. CrossRef - Quantitative proteomic analysis reveals that serine/threonine kinase is involved in Streptococcus suis virulence and adaption to stress conditions
Haodan Zhu, Junming Zhou, Dandan Wang, Zhengyu Yu, Bin Li, Yanxiu Ni, Kongwang He
Archives of Microbiology.2021; 203(7): 4715. CrossRef - Identification of novel pig and human immunoglobulin G-binding proteins and characterization of the binding regions of enolase from Streptococcus suis serotype 2
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Quan Li, Yuhang Zhang, Du Dechao, Yu Yanfei, Wei Zhang
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B. Haas, D. Grenier
Médecine et Maladies Infectieuses.2018; 48(3): 159. CrossRef - Factor H specifically capture novel Factor H-binding proteins of Streptococcus suis and contribute to the virulence of the bacteria
Quan Li, Caifeng Ma, Yang Fu, Yanan He, Yanfei Yu, Dechao Du, Huochun Yao, Chengping Lu, Wei Zhang
Microbiological Research.2017; 196: 17. CrossRef - The surface-displayed chaperones GroEL and DnaK of Mycoplasma pneumoniae interact with human plasminogen and components of the extracellular matrix
Lisa Hagemann, Anne Gründel, Enno Jacobs, Roger Dumke
Pathogens and Disease.2017;[Epub] CrossRef - Initial steps of the pathogenesis of the infection caused byStreptococcus suis: fighting against nonspecific defenses
Mariela Segura, Cynthia Calzas, Daniel Grenier, Marcelo Gottschalk
FEBS Letters.2016; 590(21): 3772. CrossRef - Interactions of surface-displayed glycolytic enzymes of Mycoplasma pneumoniae with components of the human extracellular matrix
Anne Gründel, Enno Jacobs, Roger Dumke
International Journal of Medical Microbiology.2016; 306(8): 675. CrossRef - Identification of Novel Laminin- and Fibronectin-binding Proteins by Far-Western Blot: Capturing the Adhesins of Streptococcus suis Type 2
Quan Li, Hanze Liu, Dechao Du, Yanfei Yu, Caifeng Ma, Fangfang Jiao, Huochun Yao, Chengping Lu, Wei Zhang
Frontiers in Cellular and Infection Microbiology.2015;[Epub] CrossRef
- Characterization of Streptococcus pneumoniae N-Acetylglucosamine-6-Phosphate Deacetylase as a Novel Diagnostic Marker
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Chi-Won Choi , Hee-Young An , Yong Ju Lee , Yeol Gyun Lee , Sung Ho Yun , Edmond Changkyun Park , Yeonhee Hong , Gun-Hwa Kim , Jae-Eun Park , Sun Jong Baek , Hyun Sik Kim , Seung Il Kim
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J. Microbiol. 2013;51(5):659-664. Published online October 31, 2013
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DOI: https://doi.org/10.1007/s12275-013-3451-8
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Abstract
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The identification of novel diagnostic markers of pathogenic bacteria is essential for improving the accuracy of diagnoses and for developing targeted vaccines. Streptococcus pneumoniae is a significant human pathogenic bacterium that causes pneumonia. N-acetylglucosamine-6-phosphate deacetylase (NagA) was identified in a protein mixture secreted by S. pneumoniae and its strong immunogenicity was confirmed in an immuno-proteomic assay against the anti-serum of the secreted protein mixture. In this study, recombinant S. pneumoniae NagA protein was expressed and purified to analyze its protein characteristics, immunospecificity, and immunogenicity, thereby facilitating its evaluation as a novel diagnostic marker for S. pneumoniae. Mass spectrometry analysis showed that S. pneumoniae NagA contains four internal disulfide bonds and that it does not undergo posttranslational modification. S. pneumoniae NagA antibodies successfully detected NagA from different S. pneumoniae strains, whereas NagA from other pathogenic bacteria species was not detected. In addition, mice infected with S. pneumoniae generated NagA antibodies in an effective manner. These results suggest that NagA has potential as a novel diagnostic marker for S. pneumoniae because of its high immunogenicity and immunospecificity.
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