Scientists have uncovered new information that may help guide design of vaccines for HIV-1, the virus that causes AIDS. A new detailed structural analysis of the complex formed by an anti-HIV antibody called 4E10 and its specific target provides insight into why this particular antibody is so broadly effective, a rare characteristic for HIV discovered thus far. The research is published in the February issue of Immunity.
Vaccination has been a successful strategy for protecting humans from many potentially harmful viruses. However, designing a suitable vaccine for HIV-1 has been a highly challenging and thus far unsuccessful endeavor. HIV-1 is enormously variable and it has been difficult to isolate antibodies that will recognize the many different strains of the virus. The antibody 4E10 was derived from HIV-1 infected patients by Dr. Hermann Katinger in Vienna and is the broadest acting neutralizing antibody against HIV-1 that is currently known. This antibody recognizes a protein called gp41 that is found on the surface of the virus. The gp41 protein is thought to play a key role in mediating entry of HIV-1 into human cells.
A research group led by Drs. Dennis R. Burton and Ian A. Wilson from The Scripps Research Institute in La Jolla, California performed a study examining the detailed molecular structure of the complex formed when 4E10 binds to gp41 and determining how interaction of 4E10 with gp41 influences the virus.