Difference between revisions of "Part:BBa K4727112"

 
 
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<partinfo>BBa_K4727112 short</partinfo>
 
<partinfo>BBa_K4727112 short</partinfo>
  
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This guide DNA has been designed to work with dCas9 to target AMR related genes in
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This guide DNA has been designed to work with dCas9 to target AMR related genes in <i>Acinetobacter baumannii </i>
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OmpA is a porin protein. Its N-terminal domain is an antiparallel β-barrel structure made up of eight transmembrane strands in the outer membrane, and these strands are connected by four loops. The globular C-terminal domain consists of three short turns in the periplasmic domain. OmpA is the most studied virulence factor in Acinetobacter baumannii among the outer membrane proteins (OMPs), and it plays a key role in regulating adhesion, aggressiveness, biofilm production, and the host's immune response [1]. Our interest focuses on its role in biofilm formation, which was confirmed in [2] through mutagenic experiments, also conducted on our strain.
  
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K4727112 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4727112 SequenceAndFeatures</partinfo>
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===References===
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[1] Gaddy, Jennifer A., Andrew P. Tomaras, e Luis A. Actis. «The Acinetobacter Baumannii 19606 OmpA Protein Plays a Role in Biofilm Formation on Abiotic Surfaces and in the Interaction of This Pathogen with Eukaryotic Cells». Infection and Immunity 77, fasc. 8 (agosto 2009): 3150–60. https://doi.org/10.1128/IAI.00096-09.
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[2] Nie, Dan, Yue Hu, Zhou Chen, Mingkai Li, Zheng Hou, Xiaoxing Luo, Xinggang Mao, e Xiaoyan Xue. «Outer Membrane Protein A (OmpA) as a Potential Therapeutic Target for Acinetobacter Baumannii Infection». Journal of Biomedical Science 27, fasc. 1 (dicembre 2020): 26. https://doi.org/10.1186/s12929-020-0617-7.
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Latest revision as of 12:09, 27 September 2023


sgDNA OmpA 211 for A. baumannii

This guide DNA has been designed to work with dCas9 to target AMR related genes in Acinetobacter baumannii

OmpA is a porin protein. Its N-terminal domain is an antiparallel β-barrel structure made up of eight transmembrane strands in the outer membrane, and these strands are connected by four loops. The globular C-terminal domain consists of three short turns in the periplasmic domain. OmpA is the most studied virulence factor in Acinetobacter baumannii among the outer membrane proteins (OMPs), and it plays a key role in regulating adhesion, aggressiveness, biofilm production, and the host's immune response [1]. Our interest focuses on its role in biofilm formation, which was confirmed in [2] through mutagenic experiments, also conducted on our strain.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References

[1] Gaddy, Jennifer A., Andrew P. Tomaras, e Luis A. Actis. «The Acinetobacter Baumannii 19606 OmpA Protein Plays a Role in Biofilm Formation on Abiotic Surfaces and in the Interaction of This Pathogen with Eukaryotic Cells». Infection and Immunity 77, fasc. 8 (agosto 2009): 3150–60. https://doi.org/10.1128/IAI.00096-09.

[2] Nie, Dan, Yue Hu, Zhou Chen, Mingkai Li, Zheng Hou, Xiaoxing Luo, Xinggang Mao, e Xiaoyan Xue. «Outer Membrane Protein A (OmpA) as a Potential Therapeutic Target for Acinetobacter Baumannii Infection». Journal of Biomedical Science 27, fasc. 1 (dicembre 2020): 26. https://doi.org/10.1186/s12929-020-0617-7.