Posters AACR 2017:
- The oncolytic peptide LTX-315 enhances T cell clonality and induces synergy with chemotherapy
- A phase I, dose escalation study of LTX-315 as monotherapy or in combination with either ipilimumab or pembrolizumab, in patients with transdermally accessible tumors (NCTO 1986426)
- Mode of action study on LTX-315-induced cell death
- Induction of immunogenic cell death and tumor regression in murine animal models by a novel cytolytic compound, LTX-401
The oncolytic compound LTX-401 targets the Golgi apparatus
H Zhou, A Sauvat, LC Gomes-da-Silva, S Durand, S Forveille, K Iribarren, T Yamazaki, S Souquere, L Bezu, K Müller, M Leduc, P Liu, L Zhao, A Marabelle, L Zitvogel, Ø Rekdal, O Kepp and G Kroemer
Cell Death and Differentiation (2016), 1-11
The Cytolytic Amphipathic β(2,2)-Amino Acid LTX-401 Induces DAMP Release in Melanoma Cells and Causes Complete Regression of B16 Melanoma
LM Eike, B Mauseth, KA Camilio, Ø Rekdal, B Sveinbjørnsson
PLOS ONE/ February 16, 2016
Poster CIMT 2016 (and BIO 2016):
The oncolytic peptide LTX-315 enhances T cell clonality and induces synergy with CTLA-4 blockade
The oncolytic peptide LTX-315 overcomes resistance of cancers to immunotherapy with CTLA4 checkpoint blockade
T Yamazaki, JM Pitt, M Vétizou, A Marabelle, C Flores, Ø Rekdal, G Kroemer and L Zitvogel
Cell Death and Differentiation (2016), 1-12
Posters AACR 2016:
- Enhanced antitumor activity achieved by combining the oncolytic peptide LTX-315 with anti-PD-L1 antibody
- LTX-315, an oncolytic peptide, increases anticancer immunity mediated by CTLA4 blockade in an interleukin-2 receptor beta-chain-dependent manner
- The amphiphatic ß(2,2)-amino acid LTX-401 induces complete regression of experimental hepatocellular carcinoma
- The oncolytic peptide LTX-315 enhances tumor-specific immune responses and tumor regression in murine 4T1 breast cancer when combined with doxorubicin
Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide
Bengt Erik Haug, Ketil André Camilio, Liv Tone Eliassen, Wenche Stensen, John Sigurd Svendsen, Kristel Berg, Bjarte Mortensen, Guillaume Serin, Jean-Francois Mirjolet, Francis Bichat and Øystein Rekdal
Journal of Medicinal Chemistry 2016
The oncolytic peptide LTX-315 triggers immunogenic cell death
H Zhou, S Forveille, A Sauvat, T Yamazaki, L Senovilla, Y Ma, P Liu, H Yang, L Bezu, K Müller, L Zitvogel, Ø Rekdal, O Kepp and G Kroemer
Citation: Cell Death and Disease (2016) 7
The oncolytic peptide LTX-315 induces cell death and DAMP release by mitochondria distortion in human melanoma cells
Liv-Marie Eike, Nannan Yang, Øystein Rekdal and Baldur Sveinbjørnsson
Oncotarget, October 13, 2015
Poster (528) ECC2015:
Intra-tumoural treatment with LTX-315, an oncolytic peptide immunotherapy, in patients with advanced metastatic disease induces infiltration of CD8 effectors T-cells and regression in some injected tumors
The oncolytic peptide LTX-315 kills cancer cells through Bax/Bak-regulated mitochondrial membrane permeabilization
Heng Zhou, Sabrina Forveille, Allan Sauvat, Valentina Sica, Valentina Izzo, Sylvère Durand, Kevin Müller, Peng Liu, Laurence Zitvogel, Øystein Rekdal, Oliver Kepp and Guido Kroemer
Oncotarget, September 10, 2015
Poster Melanoma conference Island 2015:
LTX-315 (OncoporeTM) as an oncolytic peptide immunotherapy for the treatment of melanoma
Poster (24/13) AACR 2015:
Anticancer effects obtained against A20 lymphomas following treatment with LTX-315 (Oncopore™) in combination with low-dose cyclophosphamide
Poster (P264) SITC 2014:
Complete and specific regression of disseminated tumors in a novel rat mesenchymal three-tumor model after intralesional treatment with the nonapeptide LTX-315 (OncoporeTM)
LTX-315 (OncoporeTM)_A short synthetic anticancer peptide and novel immunotherapeutic agent
K. A. Camilio, Ø. Rekdal, B. Sveinbjörnsson
OncoImmunology 3, e29181; June 201 4; 2014 Landes Bioscience
Poster (3067) ASCO 2014:
A Phase I study with LTX-315 - an immunogenic cell death inducer - in patients with transdermally accessible tumors
Poster CIMT 2014:
LTX-315 treatment induces complete and specific regression of dissaminated tumors in a novel mesenchymal three tumor mode
Complete regression and systemic protective immune reponses obtained in B16 melanomas after treatment with LTX-315
K. A. Camilio, G. Berge, C. S. Ravuri, Ø. Rekdal, B. Sveinbjörnsson
Cancer Immunology, Immunotherapy: Volume 63, Issue 6 (2014), Page 601-613
Oral presentation at AASLD, the liver meeting 2013:
A novel immunotherapeutic treatment for experimental hepatocellular carcinoma (HCC) using the host-defense derived peptide LTX-315.
PD. Line et al
Intratumoral injection of LTX-315 includes immunogenic cell death, complete regression and long-term protective immune responses.
Complete regression and long-term specific protective immune responses obtained in rodent tumor models after intratumoral treatment with LTX-315.
Long-term protection against B16F1 melanoma upon vaccination with tumor cell lysate combined with LTX-315 as a novel adjuvant.
Complete regression of solid B16F1melanoma tumors obtained by intratumoral injection of LTX-315 (Oncopore®).
Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity.
Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.
J Biol Chem. 2012 Jan 2;287(1):233-44. Epub 2011 Nov 4.
Small lytic peptides escape the inhibitory effect of heparan sulfate on the surface of cancer cells.
Fadnes B, Uhlin-Hansen L, Lindin I, Rekdal Ø.
BMC Cancer. 2011 Mar 31;11:116
Therapeutic vaccination against a murine lymphoma by intratumoral injection of a cationic anticancer peptide.
Berge G, Eliassen LT, Camilio KA, Bartnes K, Sveinbjørnsson B & Rekdal Ø.
Cancer Immunol Immunother 59: 1285-94, 2010.
The anticancer activity of lytic peptides is inhibited by heparan sulfate on the surface of the tumor cells.
Fadnes B, Rekdal Ø & Uhlin-Hansen L.
BMC Cancer 9: 183, 2009.
The antimicrobial peptide, Lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo.
L. T. Eliassen, G. Berge, A. Leknessund, M. Wikman, I. Lindin, C. Løkke, F.Ponthan, J. I. Johnsen, B. Sveinbjørnsson, P Kogner, T. Flægstad and Ø. Rekdal.
Int. J of Cancer. 119. 493-500. (2006).
The effects of shortening lactoferrin derived peptides against tumor cells, bacteria and normal human cells.
N. Yang, M.B. Strøm, S.M. Mekonnen, J.S. Svendsen and Ø. Rekdal.
J. Peptide Sci. 10 (2004) 37.
Enhanced antitumor activity of 15-residue bovine lactoferricin derivatives containing bulky aromatic amino acids ad lipophilic N-terminal modifications.
L.T. Eliassen, B.E. Haug, G. Berge and Ø. Rekdal.
J. Peptide Sci . 9 (2003) 510-517
Antitumor activity and specificity as a function of substitutions in the lipophilic sector of helical lactoferrin-derived peptides.
N. Yang, T. Lejon and Ø. Rekdal.
J. Peptide Sci. 9 (2003) 300.
Enhanced antitumor activity and selectivity of lactoferrin derived peptides.
N. Yang, W. Stensen, J. S. Svendsen and Ø.Rekdal,
J. Peptide Res. 60 (2002) 187.
Evidence for a Direct Antitumor Mechanism of Action of Bovine Lactoferricin.
L.T. Eliassen, G. Berge, B. Sveinbjørnsson, J.S. Svendsen, L.H. Vorland and Ø. Rekdal
Anticancer Res. 22 (2002) 2703.