The C-terminal portion of the fibrinogen-binding protein of Streptococcus equi subsp. equi contains extensive alpha-helical coiled-coil structure and contributes to thermal stability.
Abstract: The major cell wall-associated protein of the equine pathogen Streptococcus equi subsp. equi is a fibrinogen-binding protein (FgBP) which binds horse fibrinogen and equine IgG-Fc avidly through residues located in the N-terminal half and central regions of the molecule, respectively. The molecule is a major virulence factor for the organism and displays protective potential. In the present study, we use circular dichroism spectroscopy to investigate the secondary structure of the protein and show through the analysis of a panel of recombinant FgBP truncates that the C-terminal portion of FgBP contains an extensive alpha-helical coiled-coil structure that contributes to the thermal stability of the molecule.
Publication Date: 2002-01-12 PubMed ID: 11786261DOI: 10.1111/j.1574-6968.2002.tb10990.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The researchers of this study are examining the structure and function of the fibrinogen-binding protein (FgBP) in the bacterium, Streptococcus equi, a pathogen in horses. They are specifically focusing on the alpha-helical coiled-coil structure in the latter part of this protein, and how it contributes to its capacity to resist changes in temperature.
Study Background
- The protein under assessment in this research is the fibrinogen-binding protein (FgBP) found majorly in the bacterium Streptococcus equi.
- This bacterium, also known as an equine pathogen, affects horses primarily.
- FgBP is capable of attaching to horse fibrinogen and equine IgG-Fc, contributing significantly to the virulence of the bacterium.
- Researchers are particularly interested in this protein due to its thermal stability and potential to provide protection against the adverse effects of the bacterium.
Research Structure and Methods
- The methodology employed in this study involved the use of circular dichroism spectroscopy, a technique used to study the secondary structure of proteins.
- Additionally, a series of recombinant FgBP truncates were analyzed in this study.
- Recombinant FgBP truncates are proteins that are cut short or ‘truncated’ and recreated or ‘recombined’ in environments outside of a living organism.
Findings of the Study
- The study findings reveal the existence of an alpha-helical coiled-coil structure in the C-terminal (end) portion of FgBP.
- This structure was found to significantly contribute to the thermal stability of the protein molecule.
- This implies that the protein can withstand changes in the surrounding temperature due to the robust nature of the structure.
- The study deepens the understanding of the operation of FgBP in Streptococcus equi and its resilience to thermal variations, which could help devise appropriate prevention or intervention techniques against this bacterial pathogen.
Cite This Article
APA
Meehan M, Kelly SM, Price NC, Owen P.
(2002).
The C-terminal portion of the fibrinogen-binding protein of Streptococcus equi subsp. equi contains extensive alpha-helical coiled-coil structure and contributes to thermal stability.
FEMS Microbiol Lett, 206(1), 81-86.
https://doi.org/10.1111/j.1574-6968.2002.tb10990.x Publication
Researcher Affiliations
- Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin, Ireland.
MeSH Terms
- Animals
- Bacterial Proteins
- Carrier Proteins / chemistry
- Carrier Proteins / genetics
- Carrier Proteins / metabolism
- Circular Dichroism
- Protein Structure, Secondary / genetics
- Recombinant Proteins / chemistry
- Recombinant Proteins / genetics
- Recombinant Proteins / metabolism
- Streptococcus equi / chemistry
- Streptococcus equi / genetics
- Streptococcus equi / metabolism
Citations
This article has been cited 3 times.- Conners R, Hill DJ, Borodina E, Agnew C, Daniell SJ, Burton NM, Sessions RB, Clarke AR, Catto LE, Lammie D, Wess T, Brady RL, Virji M. The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil. EMBO J 2008 Jun 18;27(12):1779-89.
- Lewis MJ, Meehan M, Owen P, Woof JM. A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system. J Biol Chem 2008 Jun 20;283(25):17615-23.
- Barocchi MA, Masignani V, Rappuoli R. Opinion: Cell entry machines: a common theme in nature?. Nat Rev Microbiol 2005 Apr;3(4):349-58.
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