8082 Federal Register / Vol. 75, No. 35 / Tuesday, February 23, 2010 / Notices 

Mr. Lais is subject to debarment based 

on a finding, under section 306(a)(2)(B) 

of the act (21 U.S.C. 355a(a)(2)(B)), that 

he was convicted of a felony under 

Federal law for conduct relating to the 

regulation of a drug product. 

In the plea agreement entered on 

April 25, 2005, Mr. Lais expressly 

waived his right, if any, to contest any 

debarment that may be initiated by the 

Secretary of Health and Human Services 

under 21 U.S.C.335a. In accordance 

with section 306(c)(2)(B) of the act, Mr. 

Lais notified FDA of his acquiescence to 

debarment in a letter signed on October 

3, 2006. A person subject to debarment 

is entitled to an opportunity for an 

agency hearing on disputed issues of 

material fact under section 306(i) of the 

act, but by acquiescing to debarment Mr. 

Lais waived his opportunity for a 

hearing and to raise any contentions 

concerning his debarment. 

II. Findings and Order 

Therefore, the Acting Director, Office 

of Enforcement, Office of Regulatory 

Affairs, under section 306(a)(2)(B) of the 

act, under authority delegated to the 

Acting Director (Staff Manual Guide 

1410.35), finds that Patrick J. Lais has 

been convicted of a felony under 

Federal law for conduct relating to the 

regulation of a drug product under the 

act. 

As a result of the foregoing finding 

and based on his notification of 

acquiescence, Mr. Lais is permanently 

debarred from providing services in any 

capacity to a person with an approved 

or pending drug product application 

under sections 505, 512, or 802 of the 

act (21 U.S.C. 355, 360b, or 382), or 

under section 351 of the Public Health 

Service Act (42 U.S.C. 262), effective 

October 3, 2006, the date of notification 

of acquiescence (see sections 

306(c)(1)(B), (c)(2)(A)(ii), and 201(dd) of 

the act (21 U.S.C. 321(dd))). Any person 

with an approved or pending drug 

product application who knowingly 

employs or retains as a consultant or 

contractor, or otherwise uses the 

services of Patrick J. Lais, in any 

capacity during Mr. Lais’s debarment, 

will be subject to civil money penalties 

(section 307(a)(6) of the act (21 U.S.C. 

335b(a)(6))). If Mr. Lais provides 

services in any capacity to a person with 

an approved or pending drug product 

application during his period of 

debarment he will be subject to civil 

money penalties (section 307(a)(7) of the 

act). In addition, FDA will not accept or 

review any abbreviated new drug 

applications submitted by or with the 

assistance of Mr. Lais during his period 

of debarment (section 306(c)(1)(B) of the 

act). 

Any application by Mr. Lais for 

special termination of debarment under 

section 306(d)(4) of the act should be 

identified with Docket No. FDA–2009– 

N–0585 and sent to the Division of 

Dockets Management (see ADDRESSES). 

All such submissions are to be filed in 

four copies. The public availability of 

information in these submissions is 

governed by 21 CFR 10.20(j). 

Publicly available submissions may 

be seen in the Division of Dockets 

Management between 9 a.m. and 4 p.m., 

Monday through Friday. 

Dated: January 26, 2010. 

Brenda Holman, 

Acting Director, Office of Enforcement, Office 

of Regulatory Affairs. 

[FR Doc. 2010–3552 Filed 2–22–10; 8:45 am] 

BILLING CODE 4160–01–S 

DEPARTMENT OF HEALTH AND 

HUMAN SERVICES 

National Institutes of Health 

Government-Owned Inventions; 

Availability for Licensing 

AGENCY: National Institutes of Health, 

Public Health Service, HHS. 

ACTION: Notice. 

SUMMARY: The inventions listed below 

are owned by an agency of the U.S. 

Government and are available for 

licensing in the U.S. in accordance with 

35 U.S.C. 207 to achieve expeditious 

commercialization of results of 

federally-funded research and 

development. Foreign patent 

applications are filed on selected 

inventions to extend market coverage 

for companies and may also be available 

for licensing. 

ADDRESSES: Licensing information and 

copies of the U.S. patent applications 

listed below may be obtained by writing 

to the indicated licensing contact at the 

Office of Technology Transfer, National 

Institutes of Health, 6011 Executive 

Boulevard, Suite 325, Rockville, 

Maryland 20852–3804; telephone: 301/ 

496–7057; fax: 301/402–0220. A signed 

Confidential Disclosure Agreement will 

be required to receive copies of the 

patent applications. 

Automated Computer-Aided Polyp 

Detection for Computed Tomography 

Colonography (Virtual Colonoscopy) 

Description of Invention: This 

invention describes an automated 

method for colon registration from 

supine and prone scans that combines 

the use of Computed Tomographic 

Colonography (CTC) and Computer 

Aided Detection (CAD) software. 

Currently, in order to detect colonic 

polyps, patients are scanned twice— 

once in the supine, and again in the 

prone positions. This approach 

improves CTC sensitivity by reducing 

the extent of non-interpretable collapsed 

or fluid-filled segments. In order to 

assist radiologists in interpreting CTC 

data or evaluating colonic polyp 

candidates detected by CAD in both 

scans, it is important to provide not 

only the locations of suspicious polyps, 

but also the possible matched pairs 

(correspondences) of polyps in these 

scans. To achieve this, the two scans 

need to be aligned. In this invention, the 

colon registration problem is formulated 

as time series matching along the 

centerline of the colon. Anatomically 

salient points on the colon are initially 

distinguished as they can be viewed as 

landmarks along the central path of the 

colon. Correlation optimized warping is 

then applied to the segments defined by 

the anatomical landmarks to find better 

global registration based on the local 

correlation of segments. 

When CTC is performed in 

conjunction with CAD software, 

screening may become easier on 

patients, less time-consuming, and more 

accurate. The effectiveness of the 

method was verified in experiments in 

which the polyp location was used as a 

measure for the registration error. The 

algorithm was tested on a CTC dataset 

of 12 patients with 14 polyps. 

Experimental results showed that by 

using this method, the estimation error 

of polyp location could be reduced 

60.4% (from 47.2mm to18.7mm on 

average) compared to a traditional 

method based on dynamic time 

warping. 

Colon cancer is the second leading 

cause of cancer-related deaths in the 

United States, and the method used in 

this invention will aid in effective early 

detection of the disease, which will 

have a significant impact on its 

prognosis. 

Applications: Efficient and robust 

detection of colon cancer. 

Development Status: Early stage. 

Inventors: Ronald M. Summers et al. 

(NIHCC). 

Related Publication: Huang A, Roy D, 

Franaszek M, Summers RM. Teniae coli 

guided navigation and registration for 

virtual colonoscopy. Visualization, 

2005. VIS 05. IEEE, pp. 279–285, 23–28 

Oct 2005; doi 10.1109/ 

VISUAL.2005.1532806. 

Patent Status: U.S. Patent Application 

No. 61/220,481 filed June 25, 2009 (HHS 

Reference No. E–135–2009/0–US–01). 

Licensing Status: Available for 

licensing. 

mstockstill on DSKH9S0YB1PROD with NOTICES

Federal Register / Vol. 75, No. 35 / Tuesday, February 23, 2010 / Notices 8083 

Licensing Contact: Jeffrey A. James, 

Ph.D.; 301–435–5474; 

jeffreyja@mail.nih.gov. 

Alpha 1-3 NAcetylgalactosaminyltransferases With 

Altered Donor and Acceptor 

Specificities, Compositions, and 

Methods of Use: Development of 

Pharmaceutical Agents and Improved 

Vaccines 

Description of Invention: The present 

invention relates to the field of 

glycobiology, specifically to 

glycosyltransferases. The present 

invention provides structure-based 

design of novel glycosyltransferases and 

their biological applications. 

The structural information of 

glycosyltransferases has revealed that 

the specificity of the sugar donor in 

these enzymes is determined by a few 

residues in the sugar-nucleotide binding 

pocket of the enzyme, which is 

conserved among the family members 

from different species. This 

conservation has made it possible to 

reengineer the existing 

glycosyltransferases with broader sugar 

donor specificities. Mutation of these 

residues generates novel 

glycosyltransferases that can transfer a 

sugar residue with a chemically reactive 

functional group to Nacetylglucosarnine (GlcNAc), galactose 

(Gal) and xylose residues of 

glycoproteins, glycolipids and 

proteoglycans (glycoconjugates). Thus, 

there is potential to develop mutant 

glycosyltransferases to produce 

glycoconjugates carrying sugar moieties 

with reactive groups that can be used in 

the assembly of bio-nanoparticles to 

develop targeted-drug delivery systems 

or contrast agents for medical uses. 

Accordingly, methods to synthesize 

N-acetylglucosamine linkages have 

many applications in research and 

medicine, including in the development 

of pharmaceutical agents and improved 

vaccines that can be used to treat 

disease. 

This application claims compositions 

and methods based on the structurebased design of alpha 1–3 NAcetylgalactosaminyltransferase (alpha 

3 GalNAc-T) mutants from alpha l3galactosyltransferase (a3Gal-T) that can 

transfer 2′-modified galactose from the 

corresponding UDP-derivatives due to 

mutations that broaden the alpha 

3Gal-T donor specificity and make the 

enzyme alpha3 GalNAc-T. 

Applications: Development of 

pharmaceutical agents and improved 

vaccines. 

Development Status: Enzymes have 

been synthesized and preclinical studies 

have been performed. 

Inventors: Pradman Qasba, Boopathy 

Ramakrishnan, Elizabeth Boeggeman, 

Marta Pasek (NCI). 

Patent Status: PCT Application No. 

PCT/US2007/018678 filed August 22, 

2007, which published as WO 2009/ 

025646 on February 26, 2009 (HHS 

Reference No. E–279–2007/0–PCT–01). 

Licensing Status: Available for 

licensing. 

Licensing Contact: John Stansberry, 

PhD; 301–435–5236; 

stansbej@mail.nih.gov. 

Collaborative Research Opportunity: 

The National Cancer Institute’s 

Nanobiology Program is seeking 

statements of capability or interest from 

parties interested in collaborative 

research to further develop, evaluate, or 

commercialize structure-based design of 

novel glycosyltransferases. Please 

contact John D. Hewes, PhD at 301–435– 

3121 or hewesj@mail.nih.gov for more 

information. 

Beta 1,4–Galactosyltransferases With 

Altered Donor and Acceptor 

Specificities, Compositions and 

Methods of Use: Development of 

Pharmaceuticals and Improved 

Vaccines 

Description of Invention: The present 

invention relates to the field of 

glycobiology, specifically to 

glycosyltransferases. The present 

invention provides structure-based 

design of novel glycosyltransferases and 

their biological applications. 

The structural information of 

glycosyltransferases has revealed that 

the specificity of the sugar donor in 

these enzymes is determined by a few 

residues in the sugar-nucleotide binding 

pocket of the enzyme, which is 

conserved among the family members 

from different species. This 

conservation has made it possible to 

reengineer the existing 

glycosyltransferases with broader sugar 

donor specificities. Mutation of these 

residues generates novel 

glycosyltransferases that can transfer a 

sugar residue with a chemically reactive 

functional group to Nacetylglucosarnine (GlcNAc), galactose 

(Gal) and xylose residues of 

glycoproteins, glycolipids and 

proteoglycans (glycoconjugates). Thus, 

there is potential to develop mutant 

glycosyltransferases to produce 

glycoconjugates carrying sugar moieties 

with reactive groups that can be used in 

the assembly of bio-nanoparticles to 

develop targeted-drug delivery systems 

or contrast agents for medical uses. 

Accordingly, methods to synthesize 

N-acetylglucosamine linkages have 

many applications in research and 

medicine, including in the development 

of pharmaceutical agents and improved 

vaccines that can be used to treat 

disease. 

The invention claims beta (1,4)- 

galactosyltransferase I mutants having 

altered donor and acceptor and metal 

ion specificities, and methods of use 

thereof. In addition, the invention 

claims methods for synthesizing 

oligosaccharides using the beta (1,4)- 

galactosyltransferase I mutants and to 

using the beta (1,4)-galactosyltransferase 

I mutants to conjugate agents, such as 

therapeutic agents or diagnostic agents, 

to acceptor molecules. More 

specifically, the invention claims a 

double mutant beta 1, 4 

galactosyltransferase, human beta-1, 4- 

Tyr289Leu-Met344His-Gal-T1, 

constructed from the individual 

mutants, Tyr289Leu-Gal-T1 and 

Met344His-Gal-T1, that transfers 

modified galactose in the presence of 

magnesium ion, in contrast to the wildtype enzyme which requires manganese 

ion. 

Application: Development of 

pharmaceutical agents and improved 

vaccines. 

Development Status: Enzymes have 

been synthesized and preclinical studies 

have been performed. 

Inventors: Pradman Qasba, Boopathy 

Ramakrishnan, Elizabeth Boeggeman 

(NCI). 

Patent Status: PCT Application No. 

PCT/US2007/018656 filed August 22, 

2007, which published as WO 2009/ 

025645 on February 26, 2009 (HHS 

Reference No. E–280–2007/0–PCT–01). 

Licensing Status: Available for 

licensing. 

Licensing Contact: John Stansberry, 

PhD; 301–435–5236; 

stansbej@mail.nih.gov. 

Collaborative Research Opportunity: 

The National Cancer Institute’s 

Nanobiology Program is seeking 

statements of capability or interest from 

parties interested in collaborative 

research to further develop, evaluate, or 

commercialize glycosyltransferases. 

Please contact John D. Hewes, PhD at 

301–435–3121 or hewesj@mail.nih.gov 

for more information. 

Dated: February 4, 2010. 

Richard U. Rodriguez, 

Director, Division of Technology Development 

and Transfer, Office of Technology Transfer, 

National Institutes of Health. 

[FR Doc. 2010–3450 Filed 2–22–10; 8:45 am] 

BILLING CODE 4140–01–P 

mstockstill on DSKH9S0YB1PROD with NOTICES