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FIGURE 1 The comparison of amino acid sequences and mast cell- stimulating activities between the two most frequent allelic variants of SSL12. (a) Amino acid sequence alignment of SSL12N coded in <t>NCTC8325</t> and its allelic variant, SSL12M coded in MRSA252 strain. The alignment was obtained using fastp program in Genetyx version 12 (Software Development, Tokyo, Japan). Asterisks indicate identical residues; dots indicate similar residues, respectively. The regions corresponding to the N-terminal region, OB-fold, and β-grasp are indicated by the double-headed arrows. (b) The release of β-Hex from BMMCs treated with recombinant SSL12N and SSL12M. BMMCs differentiated from bone marrow cells of BALB/c mice were treated with indicated concentrations of SSL12N and SSL12M for 30 min, and then the activity of β-Hex in the supernatant was determined. The release of β-Hex was shown as % of total β-Hex content. The data shown were representative of three independent experiments, and the values are expressed as mean ± SD of triplicate wells. ***p <.001 and n.s., not significant compared with control
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FIGURE 1 The comparison of amino acid sequences and mast cell- stimulating activities between the two most frequent allelic variants of SSL12. (a) Amino acid sequence alignment of SSL12N coded in <t>NCTC8325</t> and its allelic variant, SSL12M coded in MRSA252 strain. The alignment was obtained using fastp program in Genetyx version 12 (Software Development, Tokyo, Japan). Asterisks indicate identical residues; dots indicate similar residues, respectively. The regions corresponding to the N-terminal region, OB-fold, and β-grasp are indicated by the double-headed arrows. (b) The release of β-Hex from BMMCs treated with recombinant SSL12N and SSL12M. BMMCs differentiated from bone marrow cells of BALB/c mice were treated with indicated concentrations of SSL12N and SSL12M for 30 min, and then the activity of β-Hex in the supernatant was determined. The release of β-Hex was shown as % of total β-Hex content. The data shown were representative of three independent experiments, and the values are expressed as mean ± SD of triplicate wells. ***p <.001 and n.s., not significant compared with control
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FIGURE 1 The comparison of amino acid sequences and mast cell- stimulating activities between the two most frequent allelic variants of SSL12. (a) Amino acid sequence alignment of SSL12N coded in <t>NCTC8325</t> and its allelic variant, SSL12M coded in MRSA252 strain. The alignment was obtained using fastp program in Genetyx version 12 (Software Development, Tokyo, Japan). Asterisks indicate identical residues; dots indicate similar residues, respectively. The regions corresponding to the N-terminal region, OB-fold, and β-grasp are indicated by the double-headed arrows. (b) The release of β-Hex from BMMCs treated with recombinant SSL12N and SSL12M. BMMCs differentiated from bone marrow cells of BALB/c mice were treated with indicated concentrations of SSL12N and SSL12M for 30 min, and then the activity of β-Hex in the supernatant was determined. The release of β-Hex was shown as % of total β-Hex content. The data shown were representative of three independent experiments, and the values are expressed as mean ± SD of triplicate wells. ***p <.001 and n.s., not significant compared with control
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FIGURE 1 The comparison of amino acid sequences and mast cell- stimulating activities between the two most frequent allelic variants of SSL12. (a) Amino acid sequence alignment of SSL12N coded in NCTC8325 and its allelic variant, SSL12M coded in MRSA252 strain. The alignment was obtained using fastp program in Genetyx version 12 (Software Development, Tokyo, Japan). Asterisks indicate identical residues; dots indicate similar residues, respectively. The regions corresponding to the N-terminal region, OB-fold, and β-grasp are indicated by the double-headed arrows. (b) The release of β-Hex from BMMCs treated with recombinant SSL12N and SSL12M. BMMCs differentiated from bone marrow cells of BALB/c mice were treated with indicated concentrations of SSL12N and SSL12M for 30 min, and then the activity of β-Hex in the supernatant was determined. The release of β-Hex was shown as % of total β-Hex content. The data shown were representative of three independent experiments, and the values are expressed as mean ± SD of triplicate wells. ***p <.001 and n.s., not significant compared with control

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Identification of responsible amino acid residues in staphylococcal superantigen-like 12 for the activation of mast cells.

doi: 10.1111/gtc.12973

Figure Lengend Snippet: FIGURE 1 The comparison of amino acid sequences and mast cell- stimulating activities between the two most frequent allelic variants of SSL12. (a) Amino acid sequence alignment of SSL12N coded in NCTC8325 and its allelic variant, SSL12M coded in MRSA252 strain. The alignment was obtained using fastp program in Genetyx version 12 (Software Development, Tokyo, Japan). Asterisks indicate identical residues; dots indicate similar residues, respectively. The regions corresponding to the N-terminal region, OB-fold, and β-grasp are indicated by the double-headed arrows. (b) The release of β-Hex from BMMCs treated with recombinant SSL12N and SSL12M. BMMCs differentiated from bone marrow cells of BALB/c mice were treated with indicated concentrations of SSL12N and SSL12M for 30 min, and then the activity of β-Hex in the supernatant was determined. The release of β-Hex was shown as % of total β-Hex content. The data shown were representative of three independent experiments, and the values are expressed as mean ± SD of triplicate wells. ***p <.001 and n.s., not significant compared with control

Article Snippet: The genes of SSL12 allelic variants were amplified from the genome of S. aureus NCTC8325 and MRSA252 (ATCC BAA-1720).

Techniques: Comparison, Sequencing, Variant Assay, Software, Recombinant, Activity Assay, Control