To mount a successful attack, it is sometimes useful to get a detailed overview of the target. Now researchers AIDS have an image of a potential career grained: an HIV envelope protein that helps the virus fuse with host cells. A crystal structure of a key part of the protein described in today's issue of Cell , suggests yet another target for people on the development of anti-HIV drugs.
Researchers have long known that HIV is based on the gp41 surface protein to fuse with and infect cells. But they did not know the specific regions of gp41 responsible for the fusion to occur. Peter Kim, David Chan and colleagues at the Massachusetts Institute of Technology Whitehead Institute for Biomedical Research in Cambridge crystallized the gp41 core and used X-rays to map its structure. The team reported that the core has a "striking similarity" to a part of the flu virus that allows it to infect cells.
The Whitehead group calls the basic structures of gp41 "a particularly attractive starting point" for drug designers. "Knowing [these] structures allows us to think of ways that we can inhibit the fusion," says Chan. Joseph Sodroski, an AIDS researcher at the Dana-Farber Cancer Institute in Boston who specializes in the entrance HIV, said the new study is "a great confirmation" of what the Whitehead group worked on. But there are at least a dozen other purposes for which there is still no anti-HIV drugs, and Sodroski warns that this finding, too, it will take years to implement. "As well as molecular information is, we do not yet have reached a point with the logic design we can just do a drug," says Sodroski. "There is still a futuristic thing."
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