Check Out These New AIPs, ASAP

As first described in 1970, quorum sensing was observed in the marine bacterium Aliivibrio fischeri.1 Quorum sensing, the process of cell to cell communication, is a crucial component of bacterial virulence. Bacteria use it to detect and regulate cell population densities. The requirements of bacteria to perform quorum sensing are three-fold: the ability to secrete a signaling molecule, followed by the ability to secrete an autoinducer, and finally, the capacity to regulate gene transcription. These abilities together allow bacteria to perform activities typically thought of in higher-level organisms, such as communication and organization.2

With the prevalence and virulence of Methicillin-resistant Staphylococcus aureus (MRSA), the promise of Autoinducing Peptides (AIPs) is in their ability to disrupt the second link required of this triumvirate. Approximately one in three people carry S. aureus bacteria in their nose, usually without any illness. The incidence of MRSA is less: about two in every 100 people carry it and most do not develop serious MRSA infections. However, it is a major problem in a hospital setting, often leading to sepsis, which is the body’s extreme response to an infection and often turns fatal.3  Misuse of antibiotics has made treatment of MRSA challenging, to say the least, and there is a hunt for antibiotic alternatives. With these issues in mind, we have just introduced three new AIPs, as modulators of accessory gene regulator (Agr) quorum sensing in Staphylococcus aureus.

Also of possible interest:

Aryl hydrocarbon receptor (AHR) interacting protein (AIP) may have a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, probably by influencing its receptivity for ligand and/or its nuclear targeting. AIP is a Cellular negative regulator of the hepatitis B virus (HBV) X protein. Furthermore, AIP is a ubiquitously expressed protein, which binds to HSP 90 and AHR through a highly conserved carboxy-terminal tetraticopeptide repeat domain.

AIP Human Recombinant is produced in E. coli, and is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-330 a.a.) and having a molecular mass of 39.8kDa. AIP is fused to a 20 amino acid His-tag at the N-terminus and purified by proprietary chromatographic techniques.

  • Aryl Hydrocarbon Receptor Interacting Protein Human Recombinant
    AH receptor-interacting protein, AIP, Aryl-hydrocarbon receptor-interacting protein, HBV X-associated protein 2, XAP-2, Immunophilin homolog ARA9, XAP2, ARA9, FKBP16, FKBP37, SMTPHN


1. Nealson, K.H.; Platt, T.; Hastings, J.W. (1970). "Cellular control of the synthesis and activity of the bacterial luminescent system". Journal of Bacteriology. 104 (1): 313–22. PMC 248216. PMID 5473898.