scholarly journals Contribution of Protein G–Related α2‐Macroglobulin–Binding Protein to Bacterial Virulence in a Mouse Skin Model of Group A Streptococcal Infection

2003 ◽  
Vol 187 (11) ◽  
pp. 1694-1703 ◽  
Author(s):  
Antonia W. Toppel ◽  
Magnus Rasmussen ◽  
Manfred Rohde ◽  
Eva Medina ◽  
Gursharan S. Chhatwal
Keyword(s):  
Streptococcal Infection ◽  
Binding Protein ◽  
Mouse Skin ◽  
Bacterial Virulence ◽  
Protein G ◽  
Skin Model ◽  
Α2 Macroglobulin ◽  
Group A

scholarly journals Binding of α2-macroglobulin to GRAB (Protein G-related α2-macroglobulin-binding protein), an important virulence factor of group A streptococci, is mediated by two charged motifs in the ΔA region

2004 ◽  
Vol 381 (3) ◽  
pp. 877-885 ◽  
Author(s):  
Antonia W. GODEHARDT ◽  
Sven HAMMERSCHMIDT ◽  
Ronald FRANK ◽  
Gursharan S. CHHATWAL
Keyword(s):  
Amino Acids ◽  
Synthetic Peptides ◽  
Binding Protein ◽  
Binding Activity ◽  
Protein G ◽  
Amino Acid Substitutions ◽  
Group A Streptococci ◽  
Α2 Macroglobulin ◽  
Arginine Residues ◽  
Group A

GRAB (Protein G-related α2M-binding protein) is a surface protein of group A streptococci and exhibits high affinity for α2-macroglobulin (α2M), a broad-range protease inhibitor. It is the sole α2M-binding protein of group A streptococci that has been shown to promote bacterial virulence in a mouse model of skin infection. The binding site for α2M was predicted to be in the N-terminal A domain of GRAB. In the present study, the α2M-binding domain was first narrowed down to 34 amino acids (amino acids 34–67) using variable truncated N-terminal GRAB fusion proteins. The sequence of the identified domain was used to design overlapping synthetic peptides of different sizes, which were then immobilized on a membrane and assayed for their α2M-binding activity. The peptide screening revealed two binding motifs of ten amino acids length, located in the ΔA (N-terminal part of the A domain) region (amino acids 34–67) with the sequences PRIIPNGGTL (amino acids 41–50) and NAPEKLALRN (amino acids 56–65) respectively. These motifs were used for systematic mutational analysis by generating synthetic peptides containing individual amino acid substitutions at every position of the mapped binding regions. The results indicated a critical role for the arginine residue at position 42 in the first binding domain and at position 64 in the second binding region. Validation of arginine residues as the critical amino acids for α2M binding was achieved by site-directed mutagenesis and binding assays. Competitive inhibition assays with GRAB containing amino acid substitutions R42G (Arg42→Gly), R64G and R42G/R64G indicated differential contribution of the arginine residues at positions 42 and 64 to α2M-binding activity and, thus, their involvement in GRAB-induced virulence.

Immune response to a laminin-binding protein (Lmb) in group A streptococcal infection

2005 ◽  
Vol 47 (2) ◽  
pp. 196-202 ◽  
Author(s):  
Rezwanul M. Wahid ◽  
Masao Yoshinaga ◽  
Junichiro Nishi ◽  
Nobuaki Maeno ◽  
Jav Sarantuya ◽  
...  
Keyword(s):  
Immune Response ◽  
Streptococcal Infection ◽  
Binding Protein ◽  
Group A ◽  
Laminin Binding Protein ◽  
Laminin Binding

scholarly journals LL-37-mediated activation of host receptors is critical for defense against group A streptococcal infection

Cell Reports ◽  
2021 ◽  
Vol 34 (9) ◽  
pp. 108766
Author(s):  
Debabrata Biswas ◽  
Poornima Ambalavanan ◽  
Miriam Ravins ◽  
Aparna Anand ◽  
Abhinay Sharma ◽  
...  
Keyword(s):  
Streptococcal Infection ◽  
Group A

Invasive group A streptococcal infection in pregnancy

2010 ◽  
Vol 60 (6) ◽  
pp. 417-424 ◽  
Author(s):  
Takahiro Yamada ◽  
Takashi Yamada ◽  
Mie K. Yamamura ◽  
Kenichi Katabami ◽  
Mineji Hayakawa ◽  
...  
Keyword(s):  
Streptococcal Infection ◽  
Invasive Group ◽  
Group A ◽  
In Pregnancy

scholarly journals Association between Resistance to Erythromycin and the Presence of the Fibronectin Binding Protein F1 Gene, prtF1, in Streptococcus pyogenes Isolates from German Pediatric Patients

2005 ◽  
Vol 49 (7) ◽  
pp. 2990-2993 ◽  
Author(s):  
Maria Haller ◽  
Kirsten Fluegge ◽  
Sandra Jasminder Arri ◽  
Brit Adams ◽  
Reinhard Berner
Keyword(s):  
Streptococcus Pyogenes ◽  
Pediatric Patients ◽  
Group A Streptococcus ◽  
Binding Protein ◽  
Macrolide Resistance ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding ◽  
Cell Invasiveness

ABSTRACT A total of 301 German pediatric group A streptococcus isolates were screened for the presence of macrolide resistance and the fibronectin binding protein F1 gene (prtF1) encoding an adhesin and cell invasiveness protein. The prtF1 gene was present significantly more often among macrolide-resistant isolates. The majority of these were not clonally related.

scholarly journals α2-Macroglobulin: a New Component in the Insulin-like Growth Factor/Insulin-like Growth Factor Binding Protein-1 Axis

2001 ◽  
Vol 276 (45) ◽  
pp. 41668-41674 ◽  
Author(s):  
Melissa Westwood ◽  
John D. Aplin ◽  
Ilse A. Collinge ◽  
Andrew Gill ◽  
Anne White ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Α2 Macroglobulin
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