AEGiS-Reuters: Researchers reveal key HIV virus protein section

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Researchers reveal key HIV virus protein section

Reuters NewMedia, Inc. - 11 July 1996


WASHINGTON - Researchers have revealed the "egg-like" structure enclosing the genetic material of the human immunodeficiency virus (HIV), potentially an important step to developing an AIDS-fighting drug, the journal Science reported on Thursday.

"Any scientist who wants to develop a new drug that interferes with HIV needs to know what the virus looks like, and we've provided the first look at one of HIV's closely held secrets," Michael Summers, a biochemistry professor at the University of Maryland-Baltimore County, said in a statement.

Capping six years of work, Summers and other reseachers at the University of Maryland-Baltimore County and the University of Utah in the July 12 edition of the journal gave a detailed molecular picture of a piece of the shell that holds HIV-1 enzymes needed for the virus to infect and reproduce.

The structure of the protein that binds with identical proteins to make up the shell is unlike any others previously seen, they said.

Called the p24 capsid protein, it has a single, exposed loop that contains an amino acid called Pro90 that binds to a protein called cyclophilin A in a process that researchers said appears to be necessary for a viral particle to become infectious.

In an interview, Summers described the capsid protein as a piece of a soccer ball that binds with other identical pieces.

Summers said the researchers speculated that for the viral information and enzymes inside to be released, that "soccer ball" must come apart, which may be triggered by cyclophilin A binding with the Pro90 amino acid.

With this information, he said experts in drug design may be able to develop a drug to block cyclophilin A binding with the Pro90 and the capsid protein, and possibly block the release of the viral material, he said.

Capsid proteins of other viruses have been targeted successfully in drug designs, he said.

"This important new information on the structure of the HIV p24 capsid protein suggests potential new targets for drug development, and provides new insights into the process of HIV replication," Jack Killen, director of the National Institue of Allergy and Infectious Diseases' AIDS division, said in a statement.

The National Institutes of Health, which includes NIAID, along with the Howard Hughes Medical Institute, where Summers is an associate investigator, funded the research.
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