Good fortune befell Michael Summers in a letter bearing the imprint of Howard Hughes.
Now Dr. Summers, an unassuming associate professor of biochemistry, is greeted on campus by shouts of "Hey, superstar."
An intense interest in the role of metals in proteins led the University of Maryland Baltimore County scientist to be the first to describe a key component of the virus that causes AIDS. That discovery, in turn, helped him win a position as an investigator with the Howard Hughes Medical Institute, the largest philanthropic foundation in the country.
Beginning next month, HHMI will underwrite his work, create a laboratory for him at UMBC and provide funding of as much as $800,000 a year.
"I still can't sleep at night," says Dr. Summers. "I'm really excited because I know that I'm going to be able to move much more quickly than I would without Hughes' support."
He celebrated by buying a new suit jacket.
Dr. Summers was among 44 biomedical investigators chosen this year by HHMI, the nation's wealthiest philanthropy, to join a team of 225 scientists that includes five Nobel laureates and 41 members of the National Academy of Sciences.
Ten Hughes investigators are at Johns Hopkins Medical Institutions, but Dr. Summers is the first one from the faculty of a public university in Maryland.
"He was identified, using a highly competitive process, as doing outstanding work, including discovering the structure of a protein in the AIDS virus," says Dr. Purnell W. Choppin, president of the foundation. "He is at the cutting edge of structural biology."
Under Dr. Summers, a research team developed a model of one of the proteins -- the nucleocapsid protein -- found in a human immunodeficiency virus (HIV) cell. Only three of dozens of such proteins have been described.
The team also showed that in test tubes, certain compounds eject zinc from this protein -- and render the HIV cells incapable of replicating. The discovery could lead to the development of treatments for AIDS and certain types of leukemia. Pharmaceutical companies are testing the compounds in animals.
Unlike other foundations, HHMI doesn't fund specific research projects. "We select the people we consider outstanding, then we support the careers of those individuals," Dr. Choppin says.
For the next five years, Dr. Summers will be an employee of HHMI, though he will remain at UMBC. In addition to his salary, the foundation will pay for a research team of two technicians, two research associates, a secretary, equipment, research supplies and an annual travel budget.
Also, by the end of the summer, HHMI will transform a wing of the 27-year-old UMBC chemistry-physics building, which houses classrooms, into a lab.
Though the amount spent by the foundation on each appointment varies, annual costs of packages range from $400,000 to $800,000.
At the end of five years, the appointment is renewable -- if a review panel finds that Dr. Summers' work is satisfactory -- for another five years and so on for an "indefinite" period, Dr. Choppin says.
Based in Chevy Chase, HHMI was founded partly as a tax shelter in 1953 by its namesake, the eccentric billionaire industrialist and aviation pioneer.
In the decade after his death in 1976, the foundation gained new trustees, settled a dispute with the Internal Revenue Service and emerged from the shadows of the Hughes empire.
The $5.2 billion sale of Hughes Aircraft Co. by the foundation provided the money that eventually made it the second-largest sponsor of basic medical research in the nation, behind the federal government.
Last year, the foundation spent $268 million -- about 20 percent of all money spent annually on biomedical research by private, nonprofit organizations.
Good investments in 1993 increased the endowment by $780 million, enabling HHMI to appoint 44 investigators this year -- 32 more than it had planned initially.
Dr. Summers and the others were chosen from a "highly competitive" field of 285 nominees from 200 medical schools and universities, Dr. Choppin says.
Dr. Summers lives in Ellicott City with his wife, Holly, who is a dentist, and their 3-year-old daughter.
He came to UMBC in 1987 after a three-year postdoctoral stint at the National Institutes of Health in Bethesda. Before that, he studied at the University of West Florida in Pensacola and at Atlanta's Emory University.
Initially, Dr. Summers, who spent vacations on his grandparents' farm in Wisconsin, considered farming as a career. But a third-grade teacher set him on the path toward biochemistry, he says. "It seems like all along in my career there were individuals who really cared about education [and] really sparked my interest in science."
Now his main thrust is to understand how metals are used by proteins -- a goal that Dr. Summers says "gets at basic biochemical principles."
His interest in HIV was piqued by a Johns Hopkins University researcher, Dr. Jeremy Berg, who speculated in 1986 that the nucleocapsid protein found in the virus needed zinc to function.
Using a nuclear magnetic resonance spectrometer (NMR), a $1 million machine that resembles a huge coffee urn and uses a powerful magnet, Dr. Summers and his graduate students developed a model of the protein.
Proteins are made of hundreds or thousands of amino acids "folded" together to form stable structures.
In building the model, the Summers team showed that the nucleocapsid protein has "fingers" of amino acids bound in place by zinc. They called these structures "zinc fingers."
Next, in conjunction with the Frederick Cancer Research and Development Center at Fort Detrick, the team showed that certain organic compounds, called C-nitroso compounds, could remove the zinc from the fingers. Without zinc, the protein loses its binder and its shape -- and the virus its ability to reproduce.
"Without zinc, the protein 'fingers' just flop around," Dr. Summers says.
"It's like having a car engine and the spark plugs fail -- it's a little part, but the engine won't run."
Dr. Summers also receives funding from the National Institutes of Health and the Office of Naval Research. His other projects include investigations of enzymes important to human development; and of proteins of bacteria that thrive in undersea volcanoes, in temperatures greater than 100 degrees C.
In addition, Dr. Summers says he and his graduate students are in "hot pursuit" of the fourth HIV protein. Using a combination of NMR techniques and computer graphics, the researchers will gradually plot the locations of the protons that make up the protein until they can construct a computerized model of the entire molecule.
They are working fast and hard -- a normal week for Dr. Summers is 70 hours -- because at least one other lab is conducting similar research.
"We are optimistic that we should be able to produce a three-dimensional image [of the protein] over the next few months," he says.
"There are many reasons to be in a hurry to get this information. The other labs are one of them. But, although we don't interact with them in our research, we get mail from patients constantly encouraging us to keep up the work."