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Displaying record number 1647
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MAb ID |
LE311 |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 (V3) |
Research Contact |
James Robinson, Tulane University, New Orleans, LA, USA |
Epitope |
|
Ab Type |
|
Neutralizing |
|
Species
(Isotype)
|
|
Patient |
AC033 |
Immunogen |
|
Keywords |
antibody binding site, antibody generation, assay or method development, binding affinity, neutralization, structure, vaccine antigen design, variant cross-reactivity |
Notes
Showing 5 of
5 notes.
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LE311: Sera from both gp120 DNA prime-protein boost immunized rabbits and from protein-only immunized rabbits competed for binding to LE311, indicating elicitation of LE311-like Abs by both immunization regimens. Competitive virus capture assay revealed higher titers of LE311-like Abs in animals immunized with DNA prime-protein boost than in protein-only immunized animals.
Vaine2008
(vaccine antigen design)
-
LE311: LE311 neutralized three of the 15 subtype B isolates tested. Binding affinity of MAb LE311 to gp120 was strongly reduced upon substitutions of His308, Pro313, or K305 to Ala, suggesting that the LE311 epitope overlaps mostly with the N-terminal flank of the V3 region and that a precise conformation of the V3 β hairpin turn may be critical for Ab binding. Thus, LE311 may need to interact with V3 from an angle, which does not permit access to V3 on many different primary viruses.LE311 inability to neutralize 6 of the 15 viruses tested could not be explained by substitution of important contact residues. The fine specificity of LE311 was mapped onto V3 in the structural context of gp120. This showed that the residues important for LE311 binding form a nearly linear arrangement on the V3 structure.
Pantophlet2008
(antibody binding site, neutralization, variant cross-reactivity, binding affinity, structure)
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LE311: Guinea pigs were immunized with gp120 protein, or with three types of VLPs containing disulfide-shackled functional trimers (SOS-VLP), uncleaved nonfunctional Env (UNC-VLP), naked VLP bearing no Env. LE311 was used in a capture assay showing that most of the SOS-VLP and UNC-VLP sera contained high titers of anti-V3 Abs. gp120 sera showed only moderate titers of V3 competing Abs.
Crooks2007
(neutralization)
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LE311: LE311 was investigated in different neutralization formats, including the standard format that measures activity over the entire infection period and several formats that emphasize various stages of infection. LE311 dramatically neutralized in the post-CD4 format but did not have any activity in the standard format. LE311 did not have any activity in the post-CD4/CCR5 format. This suggests that the post-CD4, pre-CCR5 phase of infection is a narrow window of opportunity for neutralization of JR-FL by LE311 Ab. Addition of a disulfide bridge linking gp120 and gp41 resulted in detectable activity of LE311 in the standard format. Visualization of Env-Ab binding was conducted by BN-PAGE band shifts.
Crooks2005
(antibody binding site, assay or method development, neutralization)
-
LE311: Macaques were immunized with SF162gp140, ΔV2gp140, ΔV2ΔV3gp140 and ΔV3gp140 constructs and their antibody responses were compared to the broadly reactive NAb responses in a macaque infected with SHIV SF162P4, and with pooled sera from humans infected with heterologous HIV-1 isolates (HIVIG). LE311-like Abs were present in low titers in sera from gp140 immunized animals and in higher titers in the SHIV-infected animal. LE311 captured JRFL more efficiently when the virus was pre-incubated with sCD4.
Derby2006
(antibody generation, neutralization)
References
Showing 5 of
5 references.
Isolation Paper
Derby2006
Nina R. Derby, Zane Kraft, Elaine Kan, Emma T. Crooks, Susan W. Barnett, Indresh K. Srivastava, James M. Binley, and Leonidas Stamatatos. Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection. J. Virol., 80(17):8745-8762, Sep 2006. PubMed ID: 16912322.
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Crooks2005
Emma T. Crooks, Penny L. Moore, Douglas Richman, James Robinson, Jeffrey A. Crooks, Michael Franti, Norbert Schülke, and James M. Binley. Characterizing Anti-HIV Monoclonal Antibodies and Immune Sera by Defining the Mechanism of Neutralization. Hum Antibodies, 14(3-4):101-113, 2005. PubMed ID: 16720980.
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Crooks2007
Emma T. Crooks, Penny L. Moore, Michael Franti, Charmagne S. Cayanan, Ping Zhu, Pengfei Jiang, Robbert P. de Vries, Cheryl Wiley, Irina Zharkikh, Norbert Schülke, Kenneth H. Roux, David C. Montefiori, Dennis R. Burton, and James M. Binley. A Comparative Immunogenicity Study of HIV-1 Virus-Like Particles Bearing Various Forms of Envelope Proteins, Particles Bearing no Envelope and Soluble Monomeric gp120. Virology, 366(2):245-262, 30 Sep 2007. PubMed ID: 17580087.
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Pantophlet2008
Ralph Pantophlet, Terri Wrin, Lisa A. Cavacini, James E. Robinson, and Dennis R. Burton. Neutralizing Activity of Antibodies to the V3 Loop Region of HIV-1 gp120 Relative to Their Epitope Fine Specificity. Virology, 381(2):251-260, 25 Nov 2008. PubMed ID: 18822440.
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Vaine2008
Michael Vaine, Shixia Wang, Emma T. Crooks, Pengfei Jiang, David C. Montefiori, James Binley, and Shan Lu. Improved Induction of Antibodies against Key Neutralizing Epitopes by Human Immunodeficiency Virus Type 1 gp120 DNA Prime-Protein Boost Vaccination Compared to gp120 Protein-Only Vaccination. J. Virol., 82(15):7369-7378, Aug 2008. PubMed ID: 18495775.
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