Article
Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.
The Journal of biological chemistry - 16 Jun 2017
Rathore Ujjwal, Saha Piyali, Kesavardhana Sannula, Kumar Aditya Arun, Datta Rohini, Devanarayanan Sivasankar, Das Raksha, Mascola John R, Varadarajan Raghavan
Abstract excerpt
The gp120 subunit of the HIV-1 envelope (Env) protein is heavily glycosylated at ∼25 glycosylation sites, of which ∼7-8 are located in the V1/V2 and V3 variable loops and the others in the remaining core gp120 region. Glycans partially shield Env from recognition by the host immune system and also are believed to be indispensable for proper folding of gp120 and for viral infectivity. Previous attempts to alter...
Topics
- Amino Acid Substitution
- Antibodies, Neutralizing
- Antibodies, Viral
- Antibody Specificity
- Asparagine
- Glycosylation
- HIV Envelope Protein gp120
- HIV Envelope Protein gp41
- HIV-1
- Humans