Journal
CHEMISTRY & BIOLOGY
Volume 17, Issue 4, Pages 357-370Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2010.03.012
Keywords
-
Categories
Funding
- NIGMS [GM062116]
- Natural Sciences and Engineering Research Council of Canada
- Canadian Institutes of Health Research
- International AIDS Vaccine Initiative
- Skaggs Institute for Chemical Biology
- National Institutes of Health [AI33292, AI060425, GM083658]
- Ragon Institute
Ask authors/readers for more resources
The broadly neutralizing antibody 2G12 recognizes a conserved cluster of high-mannose glycans on the surface envelope spike of HIV, suggesting that the glycan shield defense of the virus can be breached and may, under the right circumstances, serve as a vaccine target. In an attempt to recreate features of the glycan shield semisynthetically, oligomannosides were coupled to surface lysines on the icosahedral capsids of bacteriophage Q beta and cowpea mosaic virus (CPMV). The Q beta glycoconjugates, but not CPMV, presented oligomannose clusters that bind the antibody 2G12 with high affinity. However, antibodies against these 2G12 epitopes were not detected in immunized rabbits. Rather, alternative oligomannose epitopes on the conjugates were immunodominant and elicited high titers of anti-mannose antibodies that do not crossreact with the HIV envelope. The results presented reveal important design considerations for a carbohydrate-based vaccine component for HIV.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available