Literature DB >> 11158359

Streptococcus pyogenes sclB encodes a putative hypervariable surface protein with a collagen-like repetitive structure.

Adrian M Whatmore1.   

Abstract

Streptococcus pyogenes is the causative agent in a wide range of diseases of humans of varying severity. During a study scanning the genome sequence of a serotype M1 invasive isolate SF370 for novel surface proteins, an ORF, designated sclB, was identified. The putative protein encoded by sclB contains both a signal peptide and classic Gram-positive wall-associated sequences. Comparison of the sequences of this ORF with those from a number of unrelated isolates demonstrated that sclB encodes a putative surface protein with a variable N-terminal sequence followed by a variable length tract of collagen-like GXY(n) repeats. A further feature of sclB is the presence of CAAAA repeat tracts immediately downstream of the putative start codon. The number of these pentameric repeats varies from 4 to 15 between strains and variation in repeat number results in the predicted SclB protein being either in or out of frame relative to the start codon. These observations suggest that expression of this protein may be regulated at the translational level as a result of gain or loss of CAAAA repeats. While the function of SclB remains to be elucidated, an sclB-specific transcript was detected by RT-PCR during in vitro culture. Finally, it is shown that a second gene, sclA, potentially encoding a protein with a similar extensive collagen-like structure and variable N-terminal sequence, is present in all isolates of S. pyogenes tested to date. Thus S. pyogenes harbours a novel family of structurally related and surface-exposed proteins of potential importance in the pathogenic process.

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Year:  2001        PMID: 11158359     DOI: 10.1099/00221287-147-2-419

Source DB:  PubMed          Journal:  Microbiology (Reading)        ISSN: 1350-0872            Impact factor:   2.777


  36 in total

1.  Mimivirus collagen is modified by bifunctional lysyl hydroxylase and glycosyltransferase enzyme.

Authors:  Kelvin B Luther; Andreas J Hülsmeier; Belinda Schegg; Stefan A Deuber; Didier Raoult; Thierry Hennet
Journal:  J Biol Chem       Date:  2011-11-01       Impact factor: 5.157

2.  Noncollagenous region of the streptococcal collagen-like protein is a trimerization domain that supports refolding of adjacent homologous and heterologous collagenous domains.

Authors:  Zhuoxin Yu; Oleg Mirochnitchenko; Chunying Xu; Ayumi Yoshizumi; Barbara Brodsky; Masayori Inouye
Journal:  Protein Sci       Date:  2010-04       Impact factor: 6.725

3.  The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group A Streptococcus shows significant similarity to immunomodulatory HIV protein gp41.

Authors:  Flavia Squeglia; Beth Bachert; Alfonso De Simone; Slawomir Lukomski; Rita Berisio
Journal:  J Biol Chem       Date:  2013-12-19       Impact factor: 5.157

4.  The Scl1 of M41-type group A Streptococcus binds the high-density lipoprotein.

Authors:  Yumin Gao; Chunwei Liang; Ruidong Zhao; Slawomir Lukomski; Runlin Han
Journal:  FEMS Microbiol Lett       Date:  2010-05-14       Impact factor: 2.742

5.  Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs.

Authors:  Timothy C Barnett; June R Scott
Journal:  J Bacteriol       Date:  2002-04       Impact factor: 3.490

6.  Identification of isolates of Streptococcus canis infecting humans.

Authors:  A M Whatmore; K H Engler; G Gudmundsdottir; A Efstratiou
Journal:  J Clin Microbiol       Date:  2001-11       Impact factor: 5.948

7.  Scl1, the multifunctional adhesin of group A Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells.

Authors:  Clayton C Caswell; Heaven Oliver-Kozup; Runlin Han; Ewa Lukomska; Slawomir Lukomski
Journal:  FEMS Microbiol Lett       Date:  2009-11-23       Impact factor: 2.742

8.  Identification of the first prokaryotic collagen sequence motif that mediates binding to human collagen receptors, integrins alpha2beta1 and alpha11beta1.

Authors:  Clayton C Caswell; Malgorzata Barczyk; Douglas R Keene; Ewa Lukomska; Donald E Gullberg; Slawomir Lukomski
Journal:  J Biol Chem       Date:  2008-11-05       Impact factor: 5.157

9.  A Streptococcus pyogenes derived collagen-like protein as a non-cytotoxic and non-immunogenic cross-linkable biomaterial.

Authors:  Yong Y Peng; Ayumi Yoshizumi; Stephen J Danon; Veronica Glattauer; Olga Prokopenko; Oleg Mirochnitchenko; Zhuoxin Yu; Masayori Inouye; Jerome A Werkmeister; Barbara Brodsky; John A M Ramshaw
Journal:  Biomaterials       Date:  2010-01-06       Impact factor: 12.479

10.  The group A streptococcal collagen-like protein-1, Scl1, mediates biofilm formation by targeting the extra domain A-containing variant of cellular fibronectin expressed in wounded tissue.

Authors:  Heaven Oliver-Kozup; Karen H Martin; Diane Schwegler-Berry; Brett J Green; Courtney Betts; Arti V Shinde; Livingston Van De Water; Slawomir Lukomski
Journal:  Mol Microbiol       Date:  2012-12-26       Impact factor: 3.501

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