Difference between revisions of "Part:BBa K257002"

Revision as of 15:20, 21 October 2009

ClyA_Fusion_C-Term

ClyA (or HlyE) is an alpha-PFT for Pore Forming Toxins. PFTs are potent virulence factors class starting in a soluble form to an outer membrane-integrated pore. They exhibit their toxic effect either by membrane permeability barrier destruction or by toxic components delivery through the pores which forming by several assembly 8 or 13 ClyA subunits.

ClyA can be used to co-localize fully functional heterologous proteins directly in bacterial OMVs

We can fuse GFP to the C or N term of Cly A, to track OMVs easily.
ClyA is capable of co-localizing a variety of structurally diverse fusion partners to the surface of E. coli and their released vesicles, but only when the periplasmic disulfide bond-forming machinery was present ,it’s makes OMVs an ideal structure to transport hydrophobic compounds like membrane proteins into the host.
Cly A confers vesicle binding to and invasion of host cells.1
ClyA was significantly enriched in OMVs relative to other lumenal and membrane bound OMV proteins.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 85
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K257002 short</partinfo>
-ClyA is a virulence factor
+ClyA (or HlyE) is an alpha-PFT for Pore Forming Toxins. PFTs are potent virulence factors class starting in a soluble form to an outer membrane-integrated pore. They exhibit their toxic effect either by membrane permeability barrier destruction or by toxic components delivery through the pores which forming by several assembly 8 or 13 ClyA subunits.
+#ClyA can be used to co-localize fully functional heterologous proteins directly in bacterial OMVs
+#We can fuse GFP to the C or N term of Cly A, to track OMVs easily.
+#ClyA is capable of co-localizing a variety of structurally diverse fusion partners to the surface of E. coli and their released vesicles, but only when the periplasmic disulfide bond-forming machinery was present ,it’s makes OMVs an ideal structure to transport hydrophobic compounds like membrane proteins into the host.
+#Cly A confers vesicle binding to and invasion of host cells.[[1]]
+#ClyA was significantly enriched in OMVs relative to other lumenal and membrane bound OMV proteins.
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