Advaxis, Incorporated


Based in North Brunswick, New Jersey, Advaxis is developing proprietary Listeria monocytogenes (Lm) cancer vaccines based on technology developed by Dr. Yvonne Paterson, professor of microbiology at the University of Pennsylvania and chairperson of Advaxis’ scientific advisory board. Advaxis is developing attenuated live Lm vaccines that deliver engineered tumor antigens, which stimulate multiple simultaneous immunological mechanisms to fight cancer.

Saturday, January 23, 2010

USPTO issues new patent for Advaxis' intellectual property portfolio

22. January 2010

The U.S. Patent and Trademark Office (USPTO) issued today patent 7,635,479, "Compositions and Methods for Enhancing the Immunogenicity of Antigens,” by Dr. Yvonne Paterson, et al, which is assigned to the Trustees of the University of Pennsylvania and licensed to Advaxis, Incorporated

“As we develop the intellectual property portfolio associated with our technology, this patent integrates nicely with our LLO- and ActA-antigen patents”

Research, originating in the laboratory of Dr. Yvonne Paterson and continued at Advaxis and elsewhere, has shown that the unique protein pattern called PEST (Proline, Glutamic Acid , Serine, Threonine) is associated with therapeutic efficacy in live Listeria monocytogenes (Lm)vaccines that are engineered to secrete antigen-adjuvant fusion proteins when either LLO (listeriolysin O) or ActA are used as the adjuvant.

“As we develop the intellectual property portfolio associated with our technology, this patent integrates nicely with our LLO- and ActA-antigen patents,” said Executive VP of Science and Operations Dr. John Rothman. “Our portfolio includes patents for three different attenuated vaccine strains of Listeria and two different families of fusion proteins.”

The Company’s flagship Lm strain is currently in clinical testing for human papilloma virus (HPV)-induced disease, including cancer of the cervix.

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Excerpt about PEST from Advaxis.........

("LLO"), a protein that generates a hole in the membrane of the phagolysosome and allows the bacteria to escape into the relatively safe cytoplasm. Once in the cytoplasm, however, LLO still retains some activity and is also capable of creating a hole in the cell membrane. This would destroy the host cell, and spill the bacteria back out into the intercellular space where it would be exposed to more immune cell attacks and destruction. To prevent this, a sequence of approximately 30 amino acids is present in the LLO protein, called the PEST sequence (for the predominant amino acids it contains). This PEST sequence is recognized by the host cells and targets the LLO protein for rapid digestion, thus giving LLO a very short life span.