Difference between revisions of "Part:BBa K133001"

Latest revision as of 04:31, 30 October 2008

CF-multiHP-RGD-Histop

Chimeric flagellin with added multiepitope at the C-terminal. Chimeric fusion protein retains the central, most antigenic segment of H. pylori (hypervariable region) flagellin FlaA, while replacing the N- and C-terminal segment by the FliC flagellin from E. coli, which is responsible for the activation of TLR5 (176 AA from the N-terminal and 99 AA from the C-terminal). Thus, combining the right parts of flagellin of E. coli with that of H. pylori enables activation of innate immunity - a characteristic that flagellin of H. pylori alone does not posess - while presenting the antigen of H. pylori for antibody production. We also designed a highly immunogenic fusion protein - multiepitope - which combines most immunogenic portions of three essensial H. pylori proteins: VacA, UreB, HpaA.

Since the protein was designed to be produced, we additionally added RGD-Hisstop tag (for the part description and implication follow: [1].

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NheI site found at 1207
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 764
Illegal BamHI site found at 1275
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 301
1000
INCOMPATIBLE WITH RFC[1000]
Illegal BsaI.rc site found at 2091

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K133001 short</partinfo>
-Chimeric flagellin with added multiepitope at the C-terminal. Chimeric fusion protein retains the central, most antigenic segment of H. pylori (hypervariable region) flagellin FlaA, while replacing the N- and C-terminal segment by the FliC flagellin from E. coli, which is responsible for the activation of TLR5 (176 AA from the N-terminal and 99 AA from the C-terminal). Thus, combining the right parts of flagellin of ''E. coli'' with that of ''H. pylori'' enables activation of innate immunity - a characteristic that flagellin of ''H. pylori'' alone does not posess - while presenting the antigen of ''H. pylori''  for antibody production. We also designed a highly immunogenic fusion protein - multiepitope - which combines most immunogenic portions of three essensial ''H. pylori'' proteins: VacA, UreB, HpaA.
+Chimeric flagellin with added multiepitope at the C-terminal. Chimeric fusion protein retains the central, most antigenic segment of <i>H. pylori</i> (hypervariable region) flagellin FlaA, while replacing the N- and C-terminal segment by the FliC flagellin from <i>E. coli</i>, which is responsible for the activation of TLR5 (176 AA from the N-terminal and 99 AA from the C-terminal). Thus, combining the right parts of flagellin of ''E. coli'' with that of ''H. pylori'' enables activation of innate immunity - a characteristic that flagellin of ''H. pylori'' alone does not posess - while presenting the antigen of ''H. pylori''  for antibody production. We also designed a highly immunogenic fusion protein - multiepitope - which combines most immunogenic portions of three essensial ''H. pylori'' proteins: VacA, UreB, HpaA.
 Since the protein was designed to be produced, we additionally added RGD-Hisstop tag (for the part description and implication follow: [https://parts.igem.org/wiki/index.php?title=Part:BBa_K133036].