Recombinant HIV type 1 gp120 (AC10.0) (a.a. 36-514) [His]

Name: Recombinant HIV type 1 gp120 (AC10.0) (a.a. 36-514) [His]
SKU: DAG2030
Rating: 5 (1 reviews)

Recombinant HIV type 1 gp120 (AC10.0) (a.a. 36-514) from HEK293 cells [His]

COA

SDS

Datasheet

Summary

Product Overview

6xHis tagged HIV-1 gp120 (AC10.0)(Clade B) protein (a.a.36-514)

Nature

Recombinant

Tag/Conjugate

His

Alternative Names

Human Immunodeficiency Virus; HIV gp120; HIV; HIV-1 gp120; HIV-1; HIV type 1 gp120

Purity

≥ 95%

Format

Liquid

Concentration

1 mg/ml

Buffer

PBS containing 0.1% BSA and 25% glycerol

Preservative

None

Storage

After reconstitution, stable for a month at 4?C. For long term storage, split it into small aliquots and keep at -80°C. Avoid repeated freezing and thawing.

Introduction

HIV GP120 protein (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. HIV gp120 protein is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. Approximately 50% of the mass of HIV gp120 protein is due to glycosylation, the high level of which may prevent gp120 from being recognised by the human immune response. gp120 binds to the human cell surface antigen CD4, which is primarily expressed by Helper T lymphocytes and monocytes/macrophages.

Keywords

Human Immunodeficiency Virus; HIV gp120; HIV; HIV-1 gp120; HIV-1; HIV type 1 gp120

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Documents

pdf COA

pdf SDS

pdf Datasheet

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Customer Reviews

References

Rational Design of DNA-Expressed Stabilized Native-Like HIV-1 Envelope Trimers

CELL REPORTS

Authors: Aldon, Yoann; McKay, Paul F.; Allen, Joel; Ozorowski, Gabriel; Levai, Reka Felfodine; Tolazzi, Monica; Rogers, Paul; He, Linling; de Val, Natalia; Fabian, Katalin; Scarlatti, Gabriella; Zhu, Jiang; Ward, Andrew B.; Crispin, Max; Shattock, Robin J.

Abstract

The HIV-1-envelope glycoprotein (Env) is the main target of antigen design for antibody-based prophylactic vaccines. The generation of broadly neutralizing antibodies (bNAb) likely requires the appropriate presentation of stabilized trimers preventing exposure of non-neutralizing antibody (nNAb) epitopes. We designed a series of membrane-bound Envs with increased trimer stability through the introduction of key stabilization mutations. We derived a stabilized HIV-1 trimer, ConSOSL.UFO.750, which displays a dramatic reduction in nNAb binding while maintaining high quaternary and MPER-specific bNAb binding. Its soluble counterpart, ConSOSL.UFO.664, displays similar antigenicity, and its native-like Env structure is confirmed by negative stain-EM and glycosylation profiling of the soluble ConSOSL.UFO.664 trimer. A rabbit immunization study demonstrated that the ConSOSL.UFO.664 can induce autologous tier 2 neutralization. We have successfully designed a stabilized native-like Env trimer amenable to nucleic acid or viral vector-based vaccination strategies.

Characterization of HIV-1 Nucleoside-Modified mRNA Vaccines in Rabbits and Rhesus Macaques

MOLECULAR THERAPY-NUCLEIC ACIDS

Authors: Pardi, Norbert; LaBranche, Celia C.; Ferrari, Guido; Cain, Derek W.; Tombacz, Istvan; Parks, Robert J.; Muramatsu, Hiromi; Mui, Barbara L.; Tam, Ying K.; Kariko, Katalin; Polacino, Patricia; Barbosa, Christopher J.; Madden, Thomas D.; Hope, Michael J.; Haynes, Barton F.; Montefiori, David C.; Hu, Shiu-Lok; Weissman, Drew

Abstract

Despite the enormous effort in the development of effective vaccines against HIV-1, no vaccine candidate has elicited broadly neutralizing antibodies in humans. Thus, generation of more effective anti-HIV vaccines is critically needed. Here we characterize the immune responses induced by nucleoside-modified and purified mRNA-lipid nanoparticle (mRNA-LNP) vaccines encoding the clade C transmitted/founder HIV-1 envelope (Env) 1086C. Intradermal vaccination with nucleoside-modified 1086C Env mRNA-LNPs elicited high levels of gp120-specific antibodies in rabbits and rhesus macaques. Antibodies generated in rabbits neutralized a tier 1 virus, but no tier 2 neutralization activity could be measured. Importantly, three of six non-human primates developed antibodies that neutralized the autologous tier 2 strain. Despite stable anti-gp120 immunoglobulin G (IgG) levels, tier 2 neutralization titers started to drop 4 weeks after booster immunizations. Serum from both immunized rabbits and non-human primates demonstrated antibody-dependent cellular cytotoxicity activity. Collectively, these results are supportive of continued development of nucleoside-modified and purified mRNA-LNP vaccines for HIV. Optimization of Env immunogens and vaccination protocols are needed to increase antibody neutralization breadth and durability.