Related Experiment Video
Updated: Aug 14, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
A conservative domain shared by HIV gp120 and EIAV gp90: implications for HIV vaccine design
Huiguang Li1, Xiaoyan Zhang, Xiujuan Fan
1Department of Virus and Immunology, Chinese Center for STD and HIV Control and Prevention, 27 Nanwei Road, Xuanwu District, Beijing, 100050, Peoples Republic of China.
Abstract:
Both HIV and EIAV belong to the retroviridae family and lentivirus genus. Two variable regions (V3 and V4) of equine infectious anemia virus (EIAV) gp90 and two variable regions (V1 and V2) of HIV gp120 possibly adopt the same topology. We have studied the N-glycosylation properties and B cell linear epitope distribution profile of these two regions. Our results indicated that V3 and V4 of EIAV gp90 are very similar to V1 and V2 of HIV gp120. The differences between EIAV virulent and vaccine strains are mainly located at these two regions. Vaccine strains lose two N-glycosylation sites at these two regions. Because of the conservative domain shared by EIAV gp90 and HIV gp120, V1 and V2 of HIV gp120 and their glycosylation properties should be the regions preferably considered for HIV vaccine design.
More Related Videos
10:50Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 15, 2010
13:36Utilizing the Antigen Capsid-Incorporation Strategy for the Development of Adenovirus Serotype 5-Vectored Vaccine Approaches
Published on: May 6, 2015
Related Concept Videos
Inhibitors of Virion Maturation and Assembly
Retroviruses
Size and Structure of Viral Genomes
Inhibitors Of Virion Release
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...