Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site Export

@article{citeulike:4733248, abstract = {<title>Author Summary</title> <p>Vaccination is an effective means to control worldwide human diseases caused by viruses and other pathogens. Most viral vaccines work by inducing the immune system to generate neutralizing antibodies. The human immunodeficiency virus (HIV) continues to cause huge tolls in terms of human death and disease. The generation of neutralizing antibodies against HIV remains a key but elusive goal for the development of an effective vaccine. Here, we describe a novel approach that uses atomic-level structures of the HIV surface protein, gp120, together with extensive biophysical analysis of this protein, to design modified vaccine candidates. Immunization with these modified gp120 proteins revealed a new relationship between structure-guided protein stability and the efficient elicitation of antibodies against the highly conserved co-receptor binding site of HIV. These data demonstrate the potential for using the design principles established here to develop improved antibody-generating HIV vaccines and for vaccines against other pathogens.</p>}, author = {Dey, Barna and Svehla, Krisha and Xu, Ling and Wycuff, Dianne and Zhou, Tongqing and Voss, Gerald and Phogat, Adhuna and Chakrabarti, Bimal K. and Li, Yuxing and Shaw, George and Kwong, Peter D. and Nabel, Gary J. and Mascola, John R. and Wyatt, Richard T.}, citeulike-article-id = {4733248}, citeulike-linkout-0 = {http://dx.doi.org/10.1371/journal.ppat.1000445}, day = {29}, doi = {10.1371/journal.ppat.1000445}, journal = {PLoS Pathog}, keywords = {envelope, hiv, vaccine}, month = {May}, number = {5}, pages = {e1000445+}, posted-at = {2009-06-03 14:47:53}, priority = {2}, publisher = {Public Library of Science}, title = {Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site}, url = {http://dx.doi.org/10.1371/journal.ppat.1000445}, volume = {5}, year = {2009} }

TY - JOUR ID - citeulike:4733248 L3 - citeulike-article-id:4733248 N2 - <title>Author Summary</title> <p>Vaccination is an effective means to control worldwide human diseases caused by viruses and other pathogens. Most viral vaccines work by inducing the immune system to generate neutralizing antibodies. The human immunodeficiency virus (HIV) continues to cause huge tolls in terms of human death and disease. The generation of neutralizing antibodies against HIV remains a key but elusive goal for the development of an effective vaccine. Here, we describe a novel approach that uses atomic-level structures of the HIV surface protein, gp120, together with extensive biophysical analysis of this protein, to design modified vaccine candidates. Immunization with these modified gp120 proteins revealed a new relationship between structure-guided protein stability and the efficient elicitation of antibodies against the highly conserved co-receptor binding site of HIV. These data demonstrate the potential for using the design principles established here to develop improved antibody-generating HIV vaccines and for vaccines against other pathogens.</p> IS - 5 JF - PLoS Pathog TI - Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site PB - Public Library of Science VL - 5 SP - e1000445 KW - envelope KW - hiv KW - vaccine AU - Dey, Barna AU - Svehla, Krisha AU - Xu, Ling AU - Wycuff, Dianne AU - Zhou, Tongqing AU - Voss, Gerald AU - Phogat, Adhuna AU - Chakrabarti, Bimal AU - Li, Yuxing AU - Shaw, George AU - Kwong, Peter AU - Nabel, Gary AU - Mascola, John AU - Wyatt, Richard PY - 2009/05/29/ UR - http://dx.doi.org/10.1371/journal.ppat.1000445 ER -