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A Proline-Rich Region with a Highly Periodic Sequence in Streptococcal beta Protein Adopts the Polyproline II Structure and Is Exposed on the Bacterial Surface.

Areschoug, Thomas LU ; Linse, Sara LU ; Stålhammar-Carlemalm, Margaretha LU ; Hedén, Lars-Olof LU and Lindahl, Gunnar LU (2002) In Journal of Bacteriology 184(22). p.6376-6383
Abstract
Proline-rich regions have been identified in many surface proteins of pathogenic streptococci and staphylococci. These regions have been suggested to be located in cell wall-spanning domains and/or to be required for surface expression of the protein. Because little is known about these regions, which are found in extensively studied and biologically important surface proteins, we characterized the proline-rich region in one such protein, the beta protein of group B streptococci. The proline-rich region in beta, designated the XPZ region, has a proline at every third position, and the sequence is highly periodic in other respects. Immunochemical analysis showed that the XPZ region was not associated with the cell wall but was exposed on... (More)
Proline-rich regions have been identified in many surface proteins of pathogenic streptococci and staphylococci. These regions have been suggested to be located in cell wall-spanning domains and/or to be required for surface expression of the protein. Because little is known about these regions, which are found in extensively studied and biologically important surface proteins, we characterized the proline-rich region in one such protein, the beta protein of group B streptococci. The proline-rich region in beta, designated the XPZ region, has a proline at every third position, and the sequence is highly periodic in other respects. Immunochemical analysis showed that the XPZ region was not associated with the cell wall but was exposed on the bacterial surface. Moreover, characterization of a beta mutant lacking the XPZ region demonstrated that this region was not required for surface expression of the beta protein. Comparison of the XPZ region in different beta proteins showed that it varied in size but always retained the typical sequence periodicity. Circular dichroism spectroscopy indicated that the XPZ region had the structure of a polyproline II helix, an extended and solvent-exposed structure with exactly three residues per turn. Because of the three-residue sequence periodicity in the XPZ region, it is expected to be amphipathic and to have distinct nonpolar and polar surfaces. This study identified a proline-rich structure with unique properties that is exposed on the surface of an important human pathogen. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
volume
184
issue
22
pages
6376 - 6383
publisher
American Society for Microbiology
external identifiers
  • wos:000178916700032
  • pmid:12399508
  • scopus:0036842995
ISSN
0021-9193
DOI
10.1128/JB.184.22.6376-6393.2002
language
English
LU publication?
yes
id
17cf78ba-3f74-4811-bd86-36c2b60a2639 (old id 110498)
date added to LUP
2007-06-29 08:38:29
date last changed
2017-04-23 03:25:09
@article{17cf78ba-3f74-4811-bd86-36c2b60a2639,
  abstract     = {Proline-rich regions have been identified in many surface proteins of pathogenic streptococci and staphylococci. These regions have been suggested to be located in cell wall-spanning domains and/or to be required for surface expression of the protein. Because little is known about these regions, which are found in extensively studied and biologically important surface proteins, we characterized the proline-rich region in one such protein, the beta protein of group B streptococci. The proline-rich region in beta, designated the XPZ region, has a proline at every third position, and the sequence is highly periodic in other respects. Immunochemical analysis showed that the XPZ region was not associated with the cell wall but was exposed on the bacterial surface. Moreover, characterization of a beta mutant lacking the XPZ region demonstrated that this region was not required for surface expression of the beta protein. Comparison of the XPZ region in different beta proteins showed that it varied in size but always retained the typical sequence periodicity. Circular dichroism spectroscopy indicated that the XPZ region had the structure of a polyproline II helix, an extended and solvent-exposed structure with exactly three residues per turn. Because of the three-residue sequence periodicity in the XPZ region, it is expected to be amphipathic and to have distinct nonpolar and polar surfaces. This study identified a proline-rich structure with unique properties that is exposed on the surface of an important human pathogen.},
  author       = {Areschoug, Thomas and Linse, Sara and Stålhammar-Carlemalm, Margaretha and Hedén, Lars-Olof and Lindahl, Gunnar},
  issn         = {0021-9193},
  language     = {eng},
  number       = {22},
  pages        = {6376--6383},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {A Proline-Rich Region with a Highly Periodic Sequence in Streptococcal beta Protein Adopts the Polyproline II Structure and Is Exposed on the Bacterial Surface.},
  url          = {http://dx.doi.org/10.1128/JB.184.22.6376-6393.2002},
  volume       = {184},
  year         = {2002},
}