Adapted from:

Heger-Stevic et al. Displaying Whole-Chain Proteins on Hepatitis B Virus Capsid-Like Particles.  2018;1776:503-531. Cryo-EM derived reconstruction courtesy of Dr. Bettina Böttcher, University of Würzburg, Germany.

With SplitCore ARTES complements its VLP based vaccine development capabilities, adding an innovative capsid-like particle(cVLP) approach.

The Hepatitis B core protein is the capsid forming matrix with 90 – 120 dimer assembling into an icosahedral cVLP of 30 – 34 nm diameter. Foreign antigen proteins with closely located N- and C-termini or small peptides are successfully presented by insertion into the c/e1 loop of the core protein.

Proteins with extended structures and N- resp. C-termini apart from each other can now be presented on the surface of Hepatitis B core capsid-like VLP´s by splitting this protein within the c/e1 loop. These SplitCore cVLP´s present the foreign protein in a repetitive structure, allowing for induction of a B-cell specific immune response in addition to T-cell activation.

A SplitCore based Lyme disease vaccine candidate, presenting OspA, has been shown to be successful in inducing a protective immune response (Walker, A., Skamel, C. & Nassal M. SplitCore: An exceptionally versatile viral nanoparticle for native whole protein display regardless of 3D structure. Sci. Rep. 1, 5; DOI: 10.1038/srep00005 (2011)).

ARTES’ SplitCore Features:

  • produced in either bacteria or yeast
  • cVLP´s with or without nucleic acid binding domain
  • platform for presentation of large proteins, structurally complex proteins and dimeric proteins