Thursday, October 31, 2013

NIH-funded scientists reveal structure of HIV protein key to cell entry

NIH-funded scientists reveal structure of HIV protein key to cell entry


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31-Oct-2013



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Contact: NIAID Office of Communications
niaidnews@niaid.nih.gov
301-402-1663
NIH/National Institute of Allergy and Infectious Diseases



Finding holds promise for HIV vaccine development





Using protein engineering and two different cutting-edge structural biology imaging techniques, researchers have developed a detailed picture of the protein largely responsible for enabling HIV to enter human immune cells and cause infection. An in-depth understanding of the atomic structure of the HIV envelope trimeror Env, the three-component protein found on HIV's surfaceis critical to better understanding how HIV gains entry into cells and for creating potential HIV vaccines.


Atomic-resolution imaging of the Env protein has previously been elusive because of the protein's complex, delicate structure. To capture the image, a team of scientists at The Scripps Research Institute and Weill Medical College of Cornell University engineered a more stable version of the protein. Then, in separate studies, using first cryo-electron microscopy and then X-ray crystallography, the researchers were able to reveal the structure of the Env trimer, how it assembles and how it interacts with broadly neutralizing antibodies that target HIV.


Their research, described in two papers published online today in Science Express, received major support from the National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health.


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ARTICLES:
D. Lyumkis et al. Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Env Trimer. Science Express DOI: 10.1126/science.1245627 (2013).


J.P. Julien et al. Crystal Structure of a Soluble Dleaved HIV-1 Envelope Trimer. Science Express DOI: 10.1126/science.1245625 (2013).



NIAID Director Anthony S. Fauci, M.D, is available to comment on both papers.



To schedule interviews, please contact the NIAID News Office, (301) 402-1663, niaidnews@niaid.nih.gov.


NIAID conducts and supports researchat NIH, throughout the United States, and worldwideto study the causes of infectious and immune-mediated diseases, and to develop better means of preventing, diagnosing and treating these illnesses. News releases, fact sheets and other NIAID-related materials are available on the NIAID Web site at http://www.niaid.nih.gov.


About the National Institutes of Health (NIH): NIH, the nation's medical research agency, includes 27 Institutes and Centers and is a component of the U.S. Department of Health and Human Services. NIH is the primary federal agency conducting and supporting basic, clinical, and translational medical research, and is investigating the causes, treatments, and cures for both common and rare diseases. For more information about NIH and its programs, visit http://www.nih.gov/.



NIH...Turning Discovery Into Health




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NIH-funded scientists reveal structure of HIV protein key to cell entry


[ Back to EurekAlert! ]

PUBLIC RELEASE DATE:

31-Oct-2013



[


| E-mail

]


Share Share

Contact: NIAID Office of Communications
niaidnews@niaid.nih.gov
301-402-1663
NIH/National Institute of Allergy and Infectious Diseases



Finding holds promise for HIV vaccine development





Using protein engineering and two different cutting-edge structural biology imaging techniques, researchers have developed a detailed picture of the protein largely responsible for enabling HIV to enter human immune cells and cause infection. An in-depth understanding of the atomic structure of the HIV envelope trimeror Env, the three-component protein found on HIV's surfaceis critical to better understanding how HIV gains entry into cells and for creating potential HIV vaccines.


Atomic-resolution imaging of the Env protein has previously been elusive because of the protein's complex, delicate structure. To capture the image, a team of scientists at The Scripps Research Institute and Weill Medical College of Cornell University engineered a more stable version of the protein. Then, in separate studies, using first cryo-electron microscopy and then X-ray crystallography, the researchers were able to reveal the structure of the Env trimer, how it assembles and how it interacts with broadly neutralizing antibodies that target HIV.


Their research, described in two papers published online today in Science Express, received major support from the National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health.


###


ARTICLES:
D. Lyumkis et al. Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Env Trimer. Science Express DOI: 10.1126/science.1245627 (2013).


J.P. Julien et al. Crystal Structure of a Soluble Dleaved HIV-1 Envelope Trimer. Science Express DOI: 10.1126/science.1245625 (2013).



NIAID Director Anthony S. Fauci, M.D, is available to comment on both papers.



To schedule interviews, please contact the NIAID News Office, (301) 402-1663, niaidnews@niaid.nih.gov.


NIAID conducts and supports researchat NIH, throughout the United States, and worldwideto study the causes of infectious and immune-mediated diseases, and to develop better means of preventing, diagnosing and treating these illnesses. News releases, fact sheets and other NIAID-related materials are available on the NIAID Web site at http://www.niaid.nih.gov.


About the National Institutes of Health (NIH): NIH, the nation's medical research agency, includes 27 Institutes and Centers and is a component of the U.S. Department of Health and Human Services. NIH is the primary federal agency conducting and supporting basic, clinical, and translational medical research, and is investigating the causes, treatments, and cures for both common and rare diseases. For more information about NIH and its programs, visit http://www.nih.gov/.



NIH...Turning Discovery Into Health




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AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.




Source: http://www.eurekalert.org/pub_releases/2013-10/nioa-nsr103113.php
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