Rhesus monkeys were infected with mutant forms of simian immunodeficiency virus lacking dual combinations of the 4th, 5th, and 6th, sites for N-linked glycosylation in the external envelope glycoprotein of the virus When compared to sera from monkeys infected with the parental virus, sera from monkeys infected with the mutant viruses exhibited markedly increased antibody binding to specific peptides from this region and markedly increased neutralizing activity These results demonstrate a role for N-linked glycosylation in limiting the neutralizing antibody response to SIV and in shielding the virus from immune recognition PUBLICATIONS Reitter, JN, Means, RE, and Desrosiers, RC A role for carbohydrates in immune evasion in AIDS Nature Medicine 1998; 4:679-684

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Primate Research Center Grants (P51)
Project #
5P51RR000168-40
Application #
6453744
Study Section
Project Start
2001-05-01
Project End
2002-04-30
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
40
Fiscal Year
2001
Total Cost
$111,112
Indirect Cost
Name
Harvard University
Department
Type
DUNS #
082359691
City
Boston
State
MA
Country
United States
Zip Code
02115
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Ma, Qi; Ruan, Hongyu; Peng, Lisheng et al. (2017) Proteasome-independent polyubiquitin linkage regulates synapse scaffolding, efficacy, and plasticity. Proc Natl Acad Sci U S A 114:E8760-E8769
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