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Systematic and applied microbiology2002; 24(4); 486-489; doi: 10.1078/0723-2020-00062

Surface immunolocalisation of HPr in the equine pathogen Streptococcus equi.

Abstract: We have investigated the surface localisation of the phosphotransferase system protein HPr in the equine pathogen Streptococcus equi subsp. equi using immunogold localisation and transmission electron microscopy. Like the LppC acid phosphatase lipoprotein, a reference surface antigen, the S. equi HPR could be clearly detected on the surfaces of intact cells. This study is consistent with previous reports that some streptococcal HPr is cell surface associated and suggests that the extracytoplasmic mobilisation and transfer of phosphate groups by streptococci warrant further investigation.
Publication Date: 2002-03-06 PubMed ID: 11876354DOI: 10.1078/0723-2020-00062Google Scholar: Lookup
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  • Journal Article

Summary

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The research study discusses the investigation of the surface location of HPr protein in a horse pathogen Streptococcus equi subsp. equi using specific scientific techniques. Clear detection was observed, signaling the need for additional research into the streptococci mechanism of mobilizing and transferring phosphate groups.

Introduction

  • The study begins by examining the surface localization of HPr, a protein found in the phosphotransferase system of the Streptococcus equi subsp. equi bacterium, which causes diseases like strangles in horses.

Methodology

  • Utilizing advanced scientific techniques known as immunogold localisation and transmission electron microscopy, the research team was able to map out the location of the HPr protein.

Findings

  • The study found that the S. equi HPr protein was distinctly detectable on the surfaces of undamaged cells. This protein was observed to be located similarly to another surface antigen, the LppC acid phosphatase lipoprotein, a known reference point.

Interpretation and Future Outlook

  • The results of the study are consistent with previous investigations which suggested that some HPr in streptococci are associated with the cell surface.
  • Based on these findings, the study suggests that the process involved in the extracytoplasmic mobilisation and transfer of phosphate groups by streptococci could be an important point of further investigation.

Significance

  • The knowledge gained from this study could allow us to better understand the characteristics and behaviors of the Streptococcus equi subsp. equi bacterium, and potentially lay the groundwork for developing preventive measures or treatments for diseases that it causes.

Cite This Article

APA
Dixon S, Haswell M, Harrington D, Sutcliffe IC. (2002). Surface immunolocalisation of HPr in the equine pathogen Streptococcus equi. Syst Appl Microbiol, 24(4), 486-489. https://doi.org/10.1078/0723-2020-00062

Publication

ISSN: 0723-2020
NlmUniqueID: 8306133
Country: Germany
Language: English
Volume: 24
Issue: 4
Pages: 486-489

Researcher Affiliations

Dixon, S
  • School of Sciences, University of Sunderland, UK.
Haswell, M
    Harrington, D
      Sutcliffe, I C

        MeSH Terms

        • Bacterial Proteins / metabolism
        • Immunohistochemistry
        • Microscopy, Electron
        • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
        • Streptococcus equi / metabolism

        Citations

        This article has been cited 2 times.
        1. Hamilton A, Robinson C, Sutcliffe IC, Slater J, Maskell DJ, Davis-Poynter N, Smith K, Waller A, Harrington DJ. Mutation of the maturase lipoprotein attenuates the virulence of Streptococcus equi to a greater extent than does loss of general lipoprotein lipidation.. Infect Immun 2006 Dec;74(12):6907-19.
          doi: 10.1128/IAI.01116-06pubmed: 17015455google scholar: lookup
        2. Wilkins JC, Beighton D, Homer KA. Effect of acidic pH on expression of surface-associated proteins of Streptococcus oralis.. Appl Environ Microbiol 2003 Sep;69(9):5290-6.