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Calhoun "Reb" Thomas is the B-Tech Update columnist for The SciTech Lawyer. He can be reached at CRT@bionano.com.
This column is devoted to developments in legislative, judicial, and public policy matters concerning the science and technology areas of biotechnology, pharmacy, life sciences, and related arts.
Translation: The National Institutes of Health’s Office of Technology Transfer gets into the fast lane “pretty dang quick” with a new online resource that allows companies to license NIH materials. They are calling it the electronic Research Materials catalogue (eRMa), and the NIH says it can shorten a typical transaction from taking months to only a couple of days. This improvement may become very significant in light of the fact that the NIH OTT handles almost $100 million in royalty payments each year. You can learn more about this new system in the GenomeWeb article “NIH Launches Online Tech Transfer System” or at www.OTT.NIH.gov.
As companies like DeCode Genetics and 23andme make it easier to have one’s genome fully analyzed, more and more people are going to wrestle with the questions regarding whether their heredity or their personal life decisions make them what they are today. Science writer Lone Frank tackles this subject head-on in her new book, My Beautiful Genome: Exposing Our Genetic Future, One Quirk at a Time. Frank sent off her DNA to DeCode Genetics and received back a genetic profile. Throughout this book Frank reflects on the amazing information one can learn from one’s genome and the difficult questions it can pose regarding the extent to which it is in control. If you have questions regarding your own DNA but you’re not yet ready to have it sequenced, this book (on Amazon.com for under $10) may be a way for you to dip your toe in to the subject without getting completely wet. Lone Frank is also the author of The Neurotourist: Postcards from the Edge of Brain Science. She holds a PhD in neurobiology and was previously a research scientist in the biotechnology industry.
By the time you read this column it will be too late to submit comments regarding the Request for Information (RFI) recently put out by the Obama Administration soliciting input on building a twenty-first century “bioeconomy.” That said, you should still know that a National Bioeconomy Blueprint is being developed and that as the government works through the comments that have been received between October 7th and December 6th there may be further revision of aspects of the blueprint. Some of the “Grand Challenges” are identified as smart anticancer therapeutics, personalized medicine, universal vaccines, and regenerative medicine.
If your immediate thought is that this is what would be found in a restaurant for viruses or bacteria, it could be said that you have a strangely literal thought process but not that you are well focused on a serious communications issue with far-reaching impacts. In recent surveys over the last few years, the public indicates that it has heard little or nothing about nanotechnology, and yet public opinion ranges from neutral to cautiously optimistic regarding the perceived benefits versus the perceived risks of nanoinnovations. Unfortunately, all it may take is one highly publicized crisis involving a nanotech application in connection with a food product, and many of the efforts that researchers, companies, and governments are developing could be setback or undone. It is common for the public to fear that which they do not understand well, and there is still a tremendous amount of nanotech-related education that the public needs. This need will be doubly true as nanomaterials are related to food and food technologies because food plays such a central role in our lives. The interrelationship between engineered nanomaterials incorporated into food and food packaging and the communications issues with the public are further addressed in an excellent article entitled “The Communication Challenges resented by Nanofoods” in Volume 6 (November 2011) of Nature Nanotechnology.
Scientists have been studying single-cell organisms and cells in larger organisms for centuries, so how can there still be mysteries in these little things? Apparently there still are a lot of unanswered questions as Science magazine features in the cover story for its November 25th issue. For example, they ask “How Does a Cell Know Its Size?” Did you ever think about what makes a growing cell decide to stop growing at an appropriate size? Several researchers are studying proteins and enzymes to see how their concentrations and interactions with the cell environment can cause a cell to stop growing and even cause it to divide into two cells. If biomimicry teaches us that nanoscale factories of the future will operate in ways similar to cells, this research into cell size “sensing” may become very important. Another question asked in the article is “Does a Gene’s Location In the Nucleus Matter?” Strands of chromosomes do a pretty good impersonation of spaghetti in the way they appear in the nucleus, but current research is learning more about how there is a method to their madness. Studies indicate that active genes typically reside near the edges of chromosome regions, and silenced genes are found closer to the center of these regions. Nuclear location may play a role in the degree to which a gene is fully activated or whether it efficiently engages in transcription and RNA processing. These and similar interesting questions are asked in the previously mentioned article. Naturally, they attempt to answer the questions to the state of our current knowledge.
The current issue of Nature (December 8, 2012) has an article that suggest that studying proteomics is the way to go if you want to be known as the person who cured influenza (“Vaccine for all seasons–As researchers map the stable parts of the proteins that stud the surface of influenza, the decades-long quest for a universal flu vaccine is showing signs of progress.”) The flu virus is adept at changing parts of its surface so rapidly that it typically overwhelms the antibody defenses of the host that it has invaded. The surface of the virus particles is densely covered with two main proteins: neuraminidase and hemagglutinin. The top of the hemagglutinin is the shape-shifter, but the bottom or base portion tends to stay the same even after the virus mutates. Consequently much of current research is focused on finding ways to bind to the stable base. This is believed to be the way the recently discovered, broadly neutralizing Fi6 antibody manages to inactivate all 16 sub-types of the influenza type A virus. The normal immune response tends to overlook the stem or base of the viral protein, but broadly neutralizing antibodies tend to bind to one of the more stable sites of the stem. Although the lead researchers in this field say that there is lots of work still to be done, some of them are viewing current successes as a “proof of concept” for a universal influenza vaccine.