H. pylori - Ace Infectious
Drug Development Targeting the cag Pathogenicity Island of H. pylori
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Drug Development Targeting the cag Pathogenicity Island of H. pylori

Ace Infectious provides drug development services targeting the pathogenesis of H. pylori in order to develop drugs to alleviate human diseases caused by H. pylori. Since the cag pathogenicity island (cagPAI) is an important genomic DNA fragment of highly virulent H. pylori, we provide drug development services targeting the proteins encoded by cagPAI.

cagPAI

Highly virulent H. pylori carries a genomic fragment of approximately 40 kb in size and it is flanked by 31 pb direct repeats. This genomic fragment is termed cagPAI. The cagPAI contains 27 - 31 genes and most of them encode proteins to formate the type IV secretion system (T4SS) of H. pylori. In addition, the cagPAI encodes an important virulence factor of H. pylori, CagA. H. pylori inject CagA into gastric cells through the T4SS which causing various gastric diseases.

H. pylori type IV secretion system structure modelFig. 1 H. pylori type IV secretion system structure model (Cristancho Liévano et al., 2018).

Services for cagPAI's drug development

Based on the pathogenic effect of cagPAI on H. pylori virulence, we provide drug development services targeting the proteins encoded by cagPAI to block the damage of H. pylori CagA protein to gastric cells.

Drug development targeting virulence factor CagA

We provide small molecule drug development services for CagA to help develop drugs that alleviate a variety of conditions caused by CagA, such as gastritis, atrophic gastritis and localized intestinal metaplasia. The N-terminal of H. pylori CagA consists of three subdomains (domains I, II, and III). We provide drug discovery services targeting domain I to help develop drugs that block the CagA-ASPP2 interaction. We also offer to develop drugs targeting domain III to disrupt the CagA structure. Then, the N-terminal region of CagA binds to integrin β1 which affect the entry of CagA into host cells. We offer peptide drug development targeting the binding site of CagA to integrin β1.

Drug development targeting energetic components of T4SS

CagE, Cagα, and Cagβ are energetic components of T4SS. We provide drug development services for CagE, Cagα, and Cagβ. And we provide inhibitor development services targeting the NTPase property of CagE and Cagα. Then, we provide to develop small molecule drug based on the structure of Cagβ or targeting the site where Cagβ interacts with CagE.

Drug development targeting adhesin CagL

CagL is located at the top of the T4SS. Based on the fact that it establishes a direct link between H. pylori and the host cell by binding to the cell membrane integrin α5β1, we offer small molecule drug and neutralizing antibody drug development services targeting this binding site (arginine-glycine-aspartate motif) to help truncate the connection with α5β1.

Contact us

Ace Infectious provides drug development services targeting the proteins encoded by cagPAI, including virulence factor (CagA), energetic components (CagE, Cagα, and Cagβ), and adhesin (CagL). If you have other drug development need for cagPAI-related proteins, we'd happy to provide services too. Please contact us  for professional services.

References

  1. Cristancho Liévano, F.; et al. cag pathogenicity island of Helicobacter pylori and its association to preneoplastic lesions and gastric cancer. Revista UDCA Actualidad & Divulgación Científica. 2018, 21(2): 309-18.
  2. Hatakeyama, M. Malignant Helicobacter pylori-associated diseases: Gastric cancer and MALT lymphoma. Helicobacter pylori in Human Diseases. 2019, 11: 135-49.

※ All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.