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Abstract This document contains the instructions for preparing a camera-ready manuscript for the proceedings of EACL-06. The document itself conforms to its own specifications, and is therefore an example of what your manuscript should look like. Authors are asked to conform to all the directions reported in this document.
A vital part of the renewed hope for a vaccine against the human immunodeficiency virus (HIV-1) is based on recent studies that have highlighted major sites of HIV-1 vulnerability that could be effectively targeted by a preventive vaccine. One of these potential vulnerabilities includes the dense cluster of carbohydrates surrounding HIV-1's envelope glycoproteins gp120 and gp41, typically referred to as the ''glycan shield.'' Recent data from several laboratories have shown that glycans on the HIV-1 envelope form key epitopes for broadly neutralizing antibodies (bNAb). Moreover, HIV-1 envelope glycans play an important role in viral transmission, antigenicity, and immu-nogenicity. The recent availability of novel tools and technologies has now allowed investigators to leverage gly-comic structure–function relationships in the design of candidate HIV-1 vaccines. Additionally, glycans modulate the immune response, playing an essential role in Fc receptor and complement activity. To promote cross-disciplinary collaboration and promote synergistic HIV-1-glycomics research, the National Institutes of Health (NIH) co-sponsored and convened a 1.5-day workshop entitled ''Functional Glycomics in HIV-1 Vaccine Design.'' The meeting focused on the role of glycan interactions with neutralizing antibodies, the influence of immunoglobulin G (IgG) Fc receptor glycosylation, newly available glycomics technologies, and how new information on the role of glycans could be applied in HIV-1 immunogen design strategies. This report summarizes the discussions of this workshop.
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