Antibody-Based HIV-1 Vaccines Recent Developments and Future Directions 英文参考文献.docVIP

Policy Forum Antibody-Based HIV-1 Vaccines: Recent Developments and Future Directions A summary report from a Global HIV Vaccine Enterprise Working Group David Monte?ori , Quentin Sattentau, Jorge Flores, José Esparza, John Mascola on behalf of a Working Group convened * by the Global HIV Vaccine Enterprise T he Global HIV Vaccine Enterprise convened a two-day workshop in May of 2007 to neutralization will predict protection in vaccine recipients, it is clear that current vaccine immunogens elicit antibodies that neutralize only a minority of circulating isolates. Thus, much progress needs to be made in this area. Also, though virus neutralization is considered a critical benchmark for a vaccine, this may not be the only benchmark for predicting success with antibody-based HIV-1 vaccine immunogens. The main targets for neutralizing antibodies to HIV-1 are the surface gp120 and trans-membrane gp41 envelope glycoproteins (Env) that mediate receptor and coreceptor binding and the subsequent membrane fusion events that allow the virus to gain entry into cells [3]. Antibodies neutralize the virus by binding these viral spikes and blocking virus entry Structure-Assisted Immunogen Design Clinical studies have demonstrated that immunization with the gp120 surface unit of the HIV-1 envelope protein does not lead to the induction of discuss humoral immune responses to HIV and approaches to design vaccines that induce viral neutralizing and other potentially protective antibody responses. The goals of this workshop were to identify key scienti?c issues, gaps, and opportunities that have emerged since the Enterprise Strategic Plan was ?rst published in 2005 [1], and to make recommendations that Enterprise stakeholders can use to plan new activities. potent or broadly reactive neutralizing antibodies. In order to develop better immunogens, it is likely that we will need a more detailed understanding of the atomic level structure of epitopes on the native envelope glycoprotein.