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Displaying record number 1577

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MAb ID	P3E1
HXB2 Location	gp160(311-317) DNA(7155..7175)	gp160 Epitope Map
Author Location	gp41( SF162)
Research Contact	Nina Derby or Leo Stamatatos, Seattle Biomedical Research Institute, Seattle, WA, USA, leo.stamatotos@sbri.org
Epitope	`IGPGRAF`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG2aκ)
Patient
Immunogen	vaccine
Country	United States
Keywords	antibody binding site, binding affinity, escape, kinetics, neutralization, variant cross-reactivity

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade SF162
Vaccine component	gp140

Notes

Showing 6 of 6 notes.

P3E1: The effect of presence and absence of V1 loop was assessed using two approaches: remove V1 loop from the soluble trimeric gp140 construct (ΔV1SF162gp140) and second, substitute the V1 loop on SF162gp140 construct with four different V1 loops from 89.6, YU2, JRFL, and HxB2 (heterologous HIV-1 viruses). Deletion or substitution of V1 loop increased resistance to neutralization by P3E1 in 3 out of 5 V1-modified gp140 constructs, although it did not affect the binding to P3E1. D368R modification to SF162gp120 did not affect the binding to P3E1 but there was a decrease in neutralization activity by P3E1. Ching2010 (neutralization, binding affinity)
P3E1: Exogenous epitope tags were introduced in different parts of three variable regions, V1, V2 and V4, of two HIV isolates, SF162 and SF33. All SF162 tagged Envs were susceptible to neutralization by P3E1 and the majority was more susceptible than the wild type. All V4 tagged Envs were more susceptible to neutralization by P3E1, suggesting altered accessibility of epitopes within V3 loop following tagging of V4. Wallace2009 (antibody binding site, neutralization)
P3E1: The study explores how the V1 loop of Env influences the neutralization susceptibilities of heterologous viruses to antibodies elicited by the SF162gp140 immunogen. When the V1 loop of the heterologous isolates was replaced by the V1 loop present on the DF162go140 immunogen, these isolates became susceptible to neutralization by anti-V3 MAb P3E1, indicating that the V1 loop plays an important role in the resistance of heterologous viruses to neutralization. Ching2008 (antibody binding site, neutralization)
P3E1: The minimal epitope for this Ab is most probably located within the V3 crown IGPGRAF. The presence of F and R was important for P3E1 binding. Binding did not depend on the oligomerization state of Env. P3E1 neutralized SF162 and also exhibited cross-neutralizing activity with 89.6, SS1196.1 and 6535.3. On other primary isolates, V1 loop masked the exposure of the P3E1 epitope in V3 and affected neutralization. The SF162ΔV2 virus was significantly more susceptible to neutralization by P3E1 than the wildtype virus, while ΔV1 virus was neutralized with reduced potency. Glycans at positions 154 and 195 in V1V2 enhanced P3E1 neutralizing potency. Neutralization by P3E1 was also enhanced strongly by deletion of the V3 glycan at position 299, somewhat less by deletion at position 329, and not at all by deletion of the glycan at position 293. Glycans present in the V4-V5 region had only modest effects on the neutralizing potential of this Ab, where their removal resulted in a more neutralization resistant virus. Derby2007 (antibody binding site, neutralization, variant cross-reactivity, kinetics)
P3E1: 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). P3E1 recognized SF162gp140 and ΔV2gp140 equally and failed to recognize ΔV2ΔV3gp140 and ΔV3gp140. P3E1 neutralized SF162 efficiently while its neutralization potential was reduced by 93% in the presence of V3 peptides. 6% reduction in neutralization by P3E1 was observed by the presence of a scrambled V3 peptide used as a control for nonspecific binding by sera, although the scrambled peptide was not recognized by P3E1 in epitope mapping studies. Derby2006 (antibody binding site, neutralization)
P3E1: This is a new anti-V3 loop Ab isolated from mice immunized with SF162-derived gp140 proteins. Viruses from early and late infection of a macaque with SHIV SF162P4 were resistant to contemporaneous serum that had broadly reactive NAbs. SF162 was highly susceptible to neutralization by anti-V3 MAbs 447D and P3E1, as well as anti-V1 MAb P3C8, while envelopes cloned from this animal at 304 days and at 643 days (time of death) post infection had developed resistance to all three of these antibodies. Kraft2007 (neutralization, escape)

References

Showing 6 of 6 references.

Isolation Paper
Derby2007 Nina R. Derby, Sean Gray, Elizabeth Wayner, Dwayne Campogan, Giorgos Vlahogiannis, Zane Kraft, Susan W. Barnett, Indresh K. Srivastava, and Leonidas Stamatatos. Isolation and Characterization of Monoclonal Antibodies Elicited by Trimeric HIV-1 Env gp140 Protein Immunogens. Virology, 366(2):433-445, 30 Sep 2007. PubMed ID: 17560621. Show all entries for this 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. Show all entries for this paper.

Kraft2007 Zane Kraft, Nina R. Derby, Ruth A. McCaffrey, Rachel Niec, Wendy M. Blay, Nancy L. Haigwood, Eirini Moysi, Cheryl J. Saunders, Terri Wrin, Christos J. Petropoulos, M. Juliana McElrath, and Leonidas Stamatatos. Macaques Infected with a CCR5-Tropic Simian/Human Immunodeficiency Virus (SHIV) Develop Broadly Reactive Anti-HIV Neutralizing Antibodies. J. Virol., 81(12):6402-6411, Jun 2007. PubMed ID: 17392364. Show all entries for this paper.

Ching2008 Lance K. Ching, Giorgos Vlachogiannis, Katherine A. Bosch, and Leonidas Stamatatos. The First Hypervariable Region of the gp120 Env Glycoprotein Defines the Neutralizing Susceptibility of Heterologous Human Immunodeficiency Virus Type 1 Isolates to Neutralizing Antibodies Elicited by the SF162gp140 Immunogen. J. Virol., 82(2):949-956, Jan 2008. PubMed ID: 18003732. Show all entries for this paper.

Wallace2009 Aaron Wallace and Leonidas Stamatatos. Introduction of Exogenous Epitopes in the Variable Regions of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein: Effect on Viral Infectivity and the Neutralization Phenotype. J. Virol., 83(16):7883-7893, Aug 2009. PubMed ID: 19494007. Show all entries for this paper.

Ching2010 Lance Ching and Leonidas Stamatatos. Alterations in the Immunogenic Properties of Soluble Trimeric Human Immunodeficiency Virus Type 1 Envelope Proteins Induced by Deletion or Heterologous Substitutions of the V1 Loop. J. Virol., 84(19):9932-9946, Oct 2010. PubMed ID: 20660181. Show all entries for this paper.