Difference between revisions of "Part:BBa K4727109"

 
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This guide DNA has been designed to work with dCas9 to target AMR related genes in Acinetobacter baumannii
 
This guide DNA has been designed to work with dCas9 to target AMR related genes in Acinetobacter baumannii
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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_K4727109 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4727109 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.
  
  

Latest revision as of 08:14, 23 September 2023


sgDNA OmpA 157 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.