From: Terry S. Singeltary Sr.
Sent: Saturday, October 05, 2013 11:33 AM
To: BSE-L BSE-L
Subject: Prospective Grant of Exclusive License: Use of
Quaking-Induced Conversion (QUIC) for Detection of Prions
[Federal Register Volume 78, Number 192 (Thursday, October 3, 2013)]
[Notices]
[Page 61375]
From the Federal Register Online via the Government Printing Office
[www.gpo.gov]
[FR Doc No: 2013-24141]
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DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Prospective Grant of Exclusive License: Use of Quaking-Induced Conversion
(QUIC) for Detection of Prions
AGENCY: National Institutes of Health, HHS.
ACTION: Notice.
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SUMMARY: This is notice, in accordance with 35 U.S.C. 209 and 37 CFR part
404, that the National Institutes of Health (NIH), Department of Health and
Human Services, is contemplating the grant of an exclusive license to practice
the inventions embodied in U.S. provisional Application 60/961,364 filed July
20, 2007 [E-109-2007/0-US-01], PCT/ US2008/070656, filed July 21, 2008;
[E-109-2007/1-PCT-01], EPC application No 08796382.3 filed July 21, 2008
[E-109-2007/1-EP-03], US Application No. 12/177,012, filed July 21, 2008 and
issued as US patent 8,216,788 on July 10, 2012 [E-109-2007/1-US-02], and US
Application No. 13/489,321, filed June 5, 2012 [E-109-2007/1-US-04]; Each
entitled ``Detection of Infectious Prion Protein by Seeded Conversion of
Recombinant Prion Protein'' By Byron Caughey et al. to Prionics AG having a
place of business at Wagistrasse 27a CH-8952 Schlieren-Zurich, Switzerland. The
patent rights in this invention have been assigned to the United States of
America.
DATES: Only written comments and/or application for a license that are
received by the NIH Office of Technology Transfer on or before November 4, 2013
will be considered.
ADDRESSES: Requests for a copy of the patent application, inquiries,
comments and other materials relating to the contemplated license should be
directed to: Tedd Fenn, Office of Technology Transfer, National Institutes of
Health, 6011 Executive Boulevard, Suite 325, Rockville, MD 20852-3804; Email:
Tedd.Fenn@mail.nih.gov; Telephone: 301-435-5031; Facsimile: 301-402-0220.
SUPPLEMENTARY INFORMATION:
The prospective worldwide exclusive license will be royalty bearing and
will comply with the terms and conditions of 35 U.S.C. 209 and 37 CFR part 404.
The prospective exclusive license may be granted unless, within thirty (30) days
from the date of this published Notice, NIH receives written evidence and
argument that establishes that the grant of the license would not be consistent
with the requirements of 35 U.S.C. 209 and 37 CFR part 404.
The invention relates to methods and compositions for the detection of
infectious proteins or prions and diagnosis of prion related diseases. Prion
diseases are neurodegenerative diseases of great public concern because humans
may be infected from hoofed animals used as food, food products such as milk, or
blood products. Currently available tests for disease-causing prions are either
incapable of detecting low concentrations of prions and must be used post-mortem
or are incapable of detecting low concentrations of prions economically or
accurately. This technology enables rapid and economical detection of sub-lethal
concentrations of prions by using recombinant, normal, prion protein (rPrP-sen)
as a marker or indicator of infectious prions in a sample. Specifically, prions
(contained in a sample) seed the polymerization of rPrP-sen, and polymerized
rPrP-sen is detected as an amplified indicator of prions in the sample. This
assay differs from the protein-misfolding cyclic amplification assay (PMCA)
because it enables the effective use of rPrP-sen and does not require multiple
amplification cycles unless a higher degree of sensitivity is required. It is
anticipated that this technology can be combined with additional prion-detection
technologies to further improve the sensitivity of the assay. In its current
embodiment, this assay has been used to detect prions in brain tissue or
cerebral spinal fluid (CSF) from humans (variant CJD), sheep (scrapie), and
hamsters (scrapie). The proposed field of exclusivity may be limited to
diagnostics requiring premarket approval by a U.S. or a foreign regulatory
agency.
Properly filed competing applications for a license filed in response to
this notice will be treated as objections to the contemplated license. Comments
and objections submitted in response to this notice will not be made available
for public inspection, and, to the extent permitted by law, will not be released
under the Freedom of Information Act, 5 U.S.C. 552.
Dated: September 27, 2013.
Richard U. Rodriguez, Director, Division of Technology Development &
Transfer, Office of Technology Transfer, National Institutes of Health. [FR Doc.
2013-24141 Filed 10-2-13; 8:45 am] BILLING CODE 4140-01-P
UNITED STATES DISTRICT COURT FOR THE DISTRICT OF COLUMBIA CREEKSTONE FARMS
PREMIUM BEEF, L.L.C., Plaintiff, v. U.S. DEPARTMENT OF AGRICULTURE, et al.,
Defendants. ::::::::::: Civil Action No. 06-0544 (JR)
snip...
JAMES ROBERTSON United States District Judge
The government's additional argument, that private testing 14 somehow would
interfere with USDA's surveillance program, is unexplained and therefore
rejected. Of greater concern is the possibility that private testing 15 could
produce a false positive result, which might trigger unnecessary public alarm.
USDA has asserted this possibility as a reason to avoid private testing. Indeed,
the Bio-Rad kits that Creekstone proposes using are used throughout the world,
including as part of the USDA's own surveillance testing. - 18 -
Invited.16: Studies of chronic wasting disease transmission in
cervid and non-cervid species
Edward A, Hoover,1 Candace K. Mathiason,1 Davin M. Henderson,1
Nicholas J. Haley,1 Davis M. Seelig,1 Nathaniel D. Denkers,1 Amy V. Nalls,1 Mark
D. Zabe,1 Glenn C. Telling,1 Fernando Goni2 and Thomas Wisniewski,2
1Prion Research Center; Colorado State University; Fort Collins, CO
USA; 2New York University School of Medicine; New York, NY USA
How and why some misfolded proteins become horizontally transmitted
agents and occasionally cross species barriers are issues fundamental to
understanding prion disease. Chronic wasting disease (CWD) of cervids is perhaps
a prototype of horizontal prion transmission, encompassing efficient mucosal
uptake, lymphoid amplification, neuroinvasion, peripheralization, and
dissemination via mucosal excretion. Efficient mucosal transmission of CWD in
deer has been demonstrated by oral, nasal, aerosol, and indirect contact
exposure. In addition, other studies (Mathiason CK, et al.) reported at the
symposium support a significant role for pre- and/or postnatal transmission of
CWD from doe to offspring. Accumulating, yet still incomplete, evidence also
suggests that the period of relatively covert CWD infection may be longer than
originally thought. Given the above, minimally invasive sensitive assays based
on body fluids from live animals would aid substantially in understanding the
biology of CWD. We have been applying seeded realtirne quaking-induced
amplification of recombinant PrP substrates (i.e., RT-QuIC methodology) to: (1)
investigate antemortem CWD detection, and (2) model PrP-based species barriers
and trans-species adaptation-topics we previously explored using sPMCA and in
vivo bioassays. At this symposium, we report sensitive and specific detection
CWD prions in saliva, urine, blood (Mathiason lab), and rectal and pharyngeal
lymph node samples (Haley NJ, et al.) from pre-symptomatic and symptomatic
experimentally and naturally exposed deer. Other ongoing studies are employing
RT-QuIC methodology to model amplification barriers among CWD, FSE, BSE, and CJD
prions using cervine, feline, bovine, human, and promiscuous rPrP substrates and
the above species prion seeds, cellular co-factors, and transgenic mice.
Finally, in collaboration with the Wisniewski laboratory, we are conducting of
experimental CWD vaccination studies in deer employing oral administration of an
attenuated Salmonella vector expressing cervid PrP epitopes.
=====
AD.06: Detecting prions in the brain and blood of TSE-infected deer
and hamsters
Alan Elder,1 Davin Henderson,1 Anca Selariu,1 Amy Nalls,1 Byron
Caughey,2 Richard Bessen,1 Jason Bartz3 and Candace Mathiason1
1Colorado State University; Fort Collins, CO USA; 2NIH Rocky
Mountain Laboratories; Hamilton, MT USA; 3Creighton University; Omaha, NE USA
While large quantities of protease resistant prion protein (PrPres)
can be demonstrated by western blot or IHC in lymphoid biopsies or post-mortem
brain tissues harvested from prion-infected animals, these conventional assays
are less reliable as means to detect the small quantities of prions thought to
be present in bodily fluids or associated with early and asymptomatic phases of
TSE disease. The Real Time-Quaking Induced Conversion (RT-QuIC) assay is capable
of detecting prions at concentrations below the level of sensitivity of
conventional assays and provides a real-time fluorescent readout negating the
use of proteases. We have made modifications to the RT-QuIC assay to utilize it
for the detection of PrPres in brain and blood harvested from various species
infected with prions. In this study, we analyzed CWD-infected deer and
CWD/TME-infected hamster whole blood to determine the effect of:
(1) various anticoagulants,
(2) freezing and
(3) NaPTA precipitation.
Brain tissue and blood collected from naive deer and hamsters
served as negative controls.
We were able to demonstrate amplifiable prions in
(1) brain and blood samples harvested from CWD/TME-infected
animals,
(2) heparinized blood,
(3) frozen vs. fresh blood and
(4) NaPTA treated samples.
The RT-QuIC assay is able to detect PrPres in various species of
animals and shows promise as an antemortem diagnostic tool for blood-borne TSEs.
=====
Oral.08: Mother to offspring transmission of chronic wasting
disease in Reeve's Muntjac deer
Amy Nalls,1 Erin McNulty,1 Jenny Powers,2 Davis Seelig,1 Clare
Hoover,1 Nicholas Haley,1 Jeanette Hayes-Klug,1 Kelly Anderson,1 Paula Stewart,3
Wilfred Goldmann,3 Edward A. Hoover1 and Candace K. Mathiason1
1Colorado State University; Fort Collins, CO USA; 2National Park
Service; Fort Collins, CO USA; 3The Roslin Institute and Royal School of
Veterinary Studies; Edinburgh, UK
To investigate the role mother to offspring transmission plays in
chronic wasting disease (CWD), we have developed a cervid model employing the
Reeve's muntjac deer (Muntiacus reevesi). Eight muntjac doe were orally
inoculated with CWD and tested PrPCWD lymphoid positive by 4 mo post infection.
Fourteen fawns were born to these eight CWD-infected doe-3 were born viable, 6
were born non-viable and 5 were harvested as fetuses from early or end-stage
CWD-infected doe. All three viable fawns have demonstrated CWD IHC lymphoid
biopsy positivity between 43 d post birth and 11 mo post birth. Two of these
three CWD positive viable offspring have developed clinical signs consistent
with TSE disease (28-33 mo post birth). Moreover, CWD prions have been detected
by sPMCA in 11 of 16 tissues harvested from 6 full-term non-viable fawns and in
7 of 11 fetal tissues harvested in utero from the second and third trimester
fetuses. Additional tissues and pregnancy related fluids from doe and offspring
are being analyzed for CWD prions. In summary, using the muntjac deer model we
have demonstrated CWD clinical disease in offspring born to CWD-infected doe,
and in utero transmission of CWD from mother to offspring. These studies provide
basis to further investigate the mechanisms of maternal transfer of prions.
=====
AD.63: Susceptibility of domestic cats to chronic wasting disease
Amy V.Nalls,1 Candace Mathiason,1 Davis Seelig,2 Susan Kraft,1
Kevin Carnes,1 Kelly Anderson,1 Jeanette Hayes-Klug1 and Edward A. Hoover1
1Colorado State University; Fort Collins, CO USA; 2University of
Minnesota; Saint Paul, MN USA
Domestic and nondomestic cats have been shown to be susceptible to
feline spongiform encephalopathy (FSE), almost certainly caused by consumption
of bovine spongiform encephalopathy (BSE)-contaminated meat. Because domestic
and free-ranging nondomestic felids scavenge cervid carcasses, including those
in areas affected by chronic wasting disease (CWD), we evaluated the
susceptibility of the domestic cat (Felis catus) to CWD infection
experimentally. Cohorts of 5 cats each were inoculated either intracerebrally
(IC) or orally (PO) with CWD-infected deer brain. At 40 and 42 mo
post-inoculation, two IC-inoculated cats developed signs consistent with prion
disease, including a stilted gait, weight loss, anorexia, polydipsia, patterned
motor behaviors, head and tail tremors, and ataxia, and progressed to terminal
disease within 5 mo. Brains from these two cats were pooled and inoculated into
cohorts of cats by IC, PO, and intraperitoneal and subcutaneous (IP/SC) routes.
Upon subpassage, feline-adapted CWD (FelCWD) was transmitted to all
IC-inoculated cats with a decreased incubation period of 23 to 27 mo. FelCWD was
detected in the brains of all the symptomatic cats by western blotting and
immunohistochemistry and abnormalities were seen in magnetic resonance imaging,
including multifocal T2 fluid attenuated inversion recovery (FLAIR) signal
hyper-intensities, ventricular size increases, prominent sulci, and white matter
tract cavitation. Currently, 3 of 4 IP/SQ and 2 of 4 PO inoculared cats have
developed abnormal behavior patterns consistent with the early stage of feline
CWD. These results demonstrate that CWD can be transmitted and adapted to the
domestic cat, thus raising the issue of potential cervid-to- feline transmission
in nature.
Sunday, August 25, 2013
Prion2013 Chronic Wasting Disease CWD risk factors, humans, domestic cats,
blood, and mother to offspring transmission
Thursday, June 07, 2012
RT-QuIC analysis of cerebrospinal fluid in sporadic Creutzfeldt-Jakob
disease
Friday, August 29, 2008
CREEKSTONE VS USDA COURT OF APPEALS, BUSH SAYS, NO WAY, NO HOW
- BSE TESTING CREEKSTONE VS
USDA
- BSE TESTING CREEKSTONE VS USDA (7872 lines)
From: Terry S. Singeltary Sr. <[log in to unmask]>
Date: Sat, 11 Nov 2006 10:23:42 –0600
- BSE TESTING CREEKSTONE VS USDA (7872 lines)
- BSE TESTING CREEKSTONE VS USDA
DECLARATION OF PAUL W. BROWN, M.D.
- BSE TESTING CREEKSTONE VS USDA DECLARATION OF PAUL W.
BROWN, M.D. (7319 lines)
From: Terry S. Singeltary Sr. <[log in to unmask]>
Date: Sat, 11 Nov 2006 10:24:12 -0600 - Re: BSE TESTING CREEKSTONE VS USDA DECLARATION OF PAUL W.
BROWN, M.D. (7629 lines)
From: Terry S. Singeltary Sr. <[log in to unmask]>
Date: Mon, 20 Nov 2006 12:07:39 –0600
- BSE TESTING CREEKSTONE VS USDA DECLARATION OF PAUL W.
BROWN, M.D. (7319 lines)
- BSE TESTING CREEKSTONE VS USDA WILD
OATS FILES FRIEND OF COURT BRIEFING
- BSE TESTING CREEKSTONE VS USDA WILD OATS FILES FRIEND OF
COURT BRIEFING (1295 lines)
From: Terry S. Singeltary Sr. <[log in to unmask]>
Date: Sat, 11 Nov 2006 10:25:13 -0600
- BSE TESTING CREEKSTONE VS USDA WILD OATS FILES FRIEND OF
COURT BRIEFING (1295 lines)
BSE BASE MAD COW TESTING TEXAS, USA, AND CANADA
Bovine Spongiform Encephalopathy; MRR
Tuesday, September 24, 2013
NORDION (US), INC., AND BIOAXONE BIOSCIENCES, INC., Settles $90M Mad Cow
TSE prion Contamination Suit Cethrin(R)
Case 0:12-cv-60739-RNS Document 1 Entered on FLSD Docket 04/26/2012 Page 1
of 15
Wednesday, September 25, 2013
Inspections, Compliance, Enforcement, and Criminal Investigations BSE TSE
PRION 2013
Monday, September 2, 2013
PRION2013 AD.22: Bovine spongiform encephalopathy, chronic wasting disease
and scrapie (TSE surveillance) programs in Alberta, Canada
Tuesday, July 2, 2013
APHIS USDA Administrator Message to Stakeholders: Agency Vision and Goals
Eliminating ALL remaining BSE barriers to export market
Tuesday, May 21, 2013
Canada, USA, Bad feed, mad cows: Why we know three BSE cases had a common
origin and why the SSS policy is in full force $$$
Monday, August 26, 2013
***The Presence of Disease-Associated Prion Protein in Skeletal Muscle of
Cattle Infected with Classical Bovine Spongiform Encephalopathy
Monday, September 02, 2013
Atypical BSE: role of the E211K prion polymorphism
Research Project: TRANSMISSION, DIFFERENTIATION, AND PATHOBIOLOGY OF
TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES
Location: Virus and Prion Research Unit
Sunday, September 1, 2013
Evaluation of the Zoonotic Potential of Transmissible Mink Encephalopathy
We previously described the biochemical similarities between PrPres derived
from L-BSE infected macaque and cortical MM2 sporadic CJD: those observations
suggest a link between these two uncommon prion phenotypes in a primate model
(it is to note that such a link has not been observed in other models less
relevant from the human situation as hamsters or transgenic mice overexpressing
ovine PrP [28]). We speculate that a group of related animal prion strains
(L-BSE, c-BSE and TME) would have a zoonotic potential and lead to prion
diseases in humans with a type 2 PrPres molecular signature (and more
specifically type 2B for vCJD)
snip...
Together with previous experiments performed in ovinized and bovinized
transgenic mice and hamsters [8,9] indicating similarities between TME and
L-BSE, the data support the hypothesis that L-BSE could be the origin of the TME
outbreaks in North America and Europe during the mid-1900s.
Sunday, August 11, 2013
Creutzfeldt-Jakob Disease CJD cases rising North America updated report
August 2013
Creutzfeldt-Jakob Disease CJD cases rising North America with Canada seeing
an extreme increase of 48% between 2008 and 2010
Friday, August 16, 2013
Creutzfeldt-Jakob disease (CJD) biannual update August 2013 U.K. and
Contaminated blood products induce a highly atypical prion disease devoid of
PrPres in primates
Thursday, September 26, 2013
Minimise transmission risk of CJD and vCJD in healthcare settings Guidance
TSS
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