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