Recombinant HIV type 1 (pREJO4541) Glycoprotein 120 (a.a. 34-518) [His]

Name: Recombinant HIV type 1 (pREJO4541) Glycoprotein 120 (a.a. 34-518) [His]
SKU: DAG2096
Rating: 5 (1 reviews)

HIV type 1 Glycoprotein 120 (aa 34 - 518) (pREJO4541) [His], recombinant protein from HEK 293 cells

COA

SDS

Datasheet

Summary

Product Overview

6xHis tagged HIV-1 gp120 (pREJO4541)(Clade B) protein (a.a.34-518)

Nature

Recombinant

Tag/Conjugate

His

Purity

≥ 95%

Format

Each vial contains 100 μg of purified protein in PBS containing 0.1% BSA and 25% glycerol.

Concentration

1 mg/ml

Preservative

None

Storage

2-8°C short term, -20°C long term

Introduction

The human immunodeficiency virus (HIV) is a lentivirus (slowly replicating retrovirus) that causes the acquired immunodeficiency syndrome (AIDS), a condition in humans in which progressive failure of the immune system allows life-threatening opportunistic infections and cancers to thrive. Without treatment, average survival time after infection with HIV is estimated to be 9 to 11 years, depending on the HIV subtype. Infection with HIV occurs by the transfer of blood, semen, vaginal fluid, pre-ejaculate, or breast milk. Within these bodily fluids, HIV is present as both free virus particles and virus within infected immune cells.

Antigen Description

The HIV-1 surface protein gp120, also known as Glycoprotein 120, SU, and gp120 is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. The surface protein gp120 attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Surface protein gp120 is a ligand for CD209 / DC-SIGN and CLEC4M / DC-SIGNR. It may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS.

Keywords

Glycoprotein 120; gp120; SU; Surface protein; HIV1 gp120; Human Immunodeficiency Virus 1 gp120

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Documents

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References

Isolation and Structure of an Antibody that Fully Neutralizes Isolate SIVmac239 Reveals Functional Similarity of SIV and HIV Glycan Shields

IMMUNITY

Authors: Gorman, Jason; Mason, Rosemarie D.; Nettey, Leonard; Cavett, Nicole; Chuang, Gwo-Yu; Peng, Dongjun; Tsybovsky, Yaroslav; Verardi, Raffaello; Nguyen, Richard; Ambrozak, David; Biris, Kristin; LaBranche, Celia C.; Ramesh, Akshaya; Schramm, Chaim A.; Zhou, Jing; Bailer, Robert T.; Kepler, Thomas B.; Montefiori, David C.; Shapiro, Lawrence; Douek, Daniel C.; Mascola, John R.; Roederer, Mario; Kwong, Peter D.

Abstract

HIV- and SIV-envelope (Env) trimers are both extensively glycosylated, and antibodies identified to date have been unable to fully neutralize SIVmac239. Here, we report the isolation, structure, and glycan interactions of antibody ITS90.03, a monoclonal antibody that completely neutralized the highly neutralization-resistant isolate, SIVmac239. The co-crystal structure of a fully glycosylated SIVmac239-gp120 core in complex with rhesus CD4 and the antigen-binding fragment of ITS90.03 at 2.5-angstrom resolution revealed that ITS90 recognized an epitope comprised of 45% glycan. SIV-gp120 core, rhesus CD4, and their complex could each be aligned structurally to their human counterparts. The structure revealed that glycans masked most of the SIV Env protein surface, with ITS90 targeting a glycan hole, which is occupied in similar to 83% of SIV strains by glycan N238. Overall, the SIV glycan shield appears to functionally resemble its HIV counterpart in coverage of spike, shielding from antibody, and modulation of receptor accessibility.

ADS-J1 disaggregates semen-derived amyloid fibrils

BIOCHEMICAL JOURNAL

Authors: Li, Jinqing; Yang, Zichao; Liu, Han; Qiu, Mengjie; Zhang, Tingting; Li, Wenjuan; Li, Zhaofeng; Qi, Tao; Qiu, Yurong; Li, Lin; Zhou, Xuefeng; Liu, Shuwen; Tan, Suiyi

Abstract

Semen-derived amyloid fibrils, comprising SEVI (semen-derived enhancer of viral infection) fibrils and SEM1 fibrils, could remarkably enhance HIV-1 sexual transmission and thus are potential targets for the development of an effective microbicide. Previously, we found that ADS-J1, apart from being an HIV-1 entry inhibitor, could also potently inhibit seminal amyloid fibrillization and block fibril-mediated enhancement of viral infection. However, the remodeling effects of ADS-J1 on mature seminal fibrils were unexplored. Herein, we investigated the capacity of ADS-J1 to disassemble seminal fibrils and the potential mode of action by applying several biophysical and biochemical measurements, combined with molecular dynamic (MD) simulations. We found that ADS-J1 effectively remodeled SEVI, SEM1(86-107) fibrils and endogenous seminal fibrils. Unlike epigallocatechin gallate (EGCG), a universal amyloid fibril breaker, ADS-J1 disaggregated SEVI fibrils into monomeric peptides, which was independent of oxidation reaction. MD simulations revealed that ADS-J1 displayed strong binding potency to the full-length PAP(248-286) via electrostatic interactions, hydrophobic interactions and hydrogen bonds. ADS-J1 might initially bind to the fibrillar surface and then occupy the amyloid core, which eventually lead to fibril disassembly. Furthermore, the binding of ADS-J1 with PAP(248-286) might induce conformational changes of PAP(248-286). Disassembled PAP(248-286) might not be favorable to re-aggregate into fibrils. ADS-J1 also exerts abilities to remodel a panel of amyloid fibrils, including A beta(1-42), hIAPP(1-37) and EP2 fibrils. ADS-J1 displays promising potential to be a combination microbicide and an effective lead-product to treat amyloidogenic diseases.