Part:BBa_K4727112

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.