The Revised Authoritative Guide To Vaccine Legal Exemptions

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The HIV-1 envelope glycoprotein demonstrates an unusual degree of complex posttranslational glycosylation with both high-mannose and complex-type N-linked oligosaccharides. The relative conservation of these sites on gp 120/41 may indicate an evolutionarily important function for carbohydrate moieties. These functions may involve the protection of the viral protein from nonspecific proteolysis. In addition, carbohydrate expression affects the tertiary and quaternary structure of monomers and oligomers. These changes may affect cell tropism and/or immune escape. Glycans play a critical role in both humoral and cellular immune responses to viruses. During mutation and selection, sites can be added or deleted, resulting in antigenic variation and effectively masking or directing antibody responses to nonneutralizing sites. Carbohydrates have been shown to interfere with peptide presentation by antigen-presenting cells. Therefore it is also plausible that the heavy glycosylation of HIV-1 interferes with (1) proteolytic degradation into peptides, (2) peptide binding to MHC, and (3) recognition of the MHC peptide complex by T lymphocytes. Glycosylation should also result in tolerance for HIV-1. Consequently, following exposure, there is an inability to evoke a specific immune response to viral epitopes that are protective in nature. These aspects point out the importance of targeting carbohydrate antigens on HIV-1 in vaccine strategies or redirecting immune responses. In vaccine design for HIV-1, carbohydrates, while having profound biological and immunological roles in the pathophysiology of HIV infection, have been understudied and basically forgotten entities.


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