67 FR 48 pg. 11107 - Availability for Non-Exclusive, Exclusive, or Partially Exclusive Licensing of U.S. Patent Application Concerning Method for Detecting Clostridium Botulinum Neurotoxin Serotypes A, B, E and F in a Sample
Type: NOTICEVolume: 67Number: 48Page: 11107
FR document: [FR Doc. 02-5905 Filed 3-11-02; 8:45 am]
Agency: Defense Department
Sub Agency: Department of the Army
Official PDF Version: PDF Version
DEPARTMENT OF DEFENSE
Department of the Army
Availability for Non-Exclusive, Exclusive, or Partially Exclusive Licensing of U.S. Patent Application Concerning Method for Detecting Clostridium Botulinum Neurotoxin Serotypes A, B, E and F in a Sample
AGENCY:
Department of the Army, DoD.
ACTION:
Notice.
SUMMARY:
In accordance with 37 CFR 404.6, announcement is made of the availability for licensing of U.S. Patent Application No. 60/232,929 entitled "Method for Detecting Clostridium Botulinum Neurotoxin Serotypes A, B, E and F in a Sample" filed September 15, 2000. Foreign rights are also available (PCT/US01/28641). The United States Government as represented by the Secretary of the Army has rights in this invention.
ADDRESSES:
Commander, U.S. Army Medical Research and Materiel Command, ATTN: Command Judge Advocate, MCMR-JA, 504 Scott Street, Fort Detrick, Frederick, Maryland 21702-5012.
FOR FURTHER INFORMATION CONTACT:
For patent issues, Ms. Elizabeth Arwine, Patent Attorney, (301) 619-7808. For licensing issues, Dr. Paul Mele, Office of Research Technology Assessment, (301) 619-6664, both at telefax (301) 619-5034.
SUPPLEMENTARY INFORMATION:
The present invention relates to a simple, sensitive colorimetric capture ELISA for BoNTs with detection limits at or below 1 mouse unit. The assay is reproducible and accurate with negligible cross-reactivity between serotypes. The strength of the assay relies on its novel format and the unique preparation of the antibodies used in the assay. The antibodies are affinity-purified to the heavy chain C-fragment of the toxin. Others have used antibodies, which are not affinity purified or which are purified to the whole toxin molecule. We reasoned that since the C-terminal region of the heavy chain is where the binding domain is located, this portion of the molecule should not be covered by associated proteins, if the binding domain is located, this portion of the molecule should not be covered by associated proteins; if the binding domain was blocked, then the molecule would be precluded from binding to the cell surface and would not be toxic. Thus, the binding region "looks" the same in both the purified and complex forms. Antibodies to this region should recognize preparation of the antibodies is that they do not cross-react between serotypes, they recognize neutralizing epitopes, and they recognize purified and complex toxins equally.
Luz D. Ortiz,
Army Federal Register Liaison Officer.
[FR Doc. 02-5905 Filed 3-11-02; 8:45 am]
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