Estimated secondary structure propensities within V1/V2 region of HIV gp120 are an important global antibody neutralization sensitivity determinant.
Neutralization sensitivity of HIV-1 virus to antibodies and anti-sera varies greatly between the isolates. Significant role of V1/V2 domain as a global neutralization sensitivity regulator has been suggested. Recent X-ray structures revealed presence of well-defined tertiary structure within this do...
Main Author: | Maxim Totrov |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3976368?pdf=render |
Similar Items
-
Allosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivity.
by: Heidi E Drummer, et al.
Published: (2013-01-01) -
Fusion Complexes and CD4-independent gp120s for the Induction of HIV-1 Neutralizing Antibodies
by: Lopalco L, et al.
Published: (2005-12-01) -
Engineering of HIV gp120 by yeast surface display for neutralizing antibody characterization and immunogen design
by: Mata-Fink, Jordi
Published: (2013) -
Characterization of a Large Panel of Rabbit Monoclonal Antibodies against HIV-1 gp120 and Isolation of Novel Neutralizing Antibodies against the V3 Loop.
by: Yali Qin, et al.
Published: (2015-01-01) -
A short segment in the HIV-1 gp120 V1/V2 region is a major determinant of neutralization resistance to PG9-like antibodies
by: Doria-Rose NA, et al.
Published: (2012-09-01)