Recombinant HIV type 1 (ML274.W0M.ENV.F1) Glycoprotein 120 (a.a. 32-523) [His]

Name: Recombinant HIV type 1 (ML274.W0M.ENV.F1) Glycoprotein 120 (a.a. 32-523) [His]
SKU: DAG2077
Rating: 5 (1 reviews)

HIV type 1 Glycoprotein 120 (aa 32 - 523) (ML274.W0M.ENV.F1) [His], recombinant protein from HEK 293 cells

COA

SDS

Datasheet

Summary

Product Overview

6xHis tagged HIV-1 gp120 (MK184.W0M, ENV.G3)(Clade A) protein (a.a.35-500)

Nature

Recombinant

Tag/Conjugate

His

Purity

≥ 95%

Format

Each vial contains 100 μg purified protein in PBS.

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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References

HIV gp120-mediated CD4(+)T cell activation is inhibited by non-neutralizing gp120-V2 loop antibodies

JOURNAL OF THE INTERNATIONAL AIDS SOCIETY

Authors: Cicala, C.; Goes, L.; Sajani, A.; Nawaz, F.; Van Ryk, D.; Yolitz, J.; Wei, D.; Mason, R.; Roederer, M.; Kong, X. -P.; Arthos, J.; Fauci, A. S.

Abstract

Analysis of interaction between sulfated polysaccharides and HIV oligopeptides by surface plasmon resonance

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

Authors: Battulga, Tungalag; Tumurbaatar, Oyunjargal; Ganzorig, Oyundelger; Ishimura, Takahisa; Kanamoto, Taisei; Nakashima, Hideki; Miyazaki, Kensuke; Yoshida, Takashi

Abstract

This study aims to quantitatively investigate the interaction between sulfated polysaccharides with potent anti HIV activity, dextran and curdlan sulfates with negatively charged sulfate groups, and poly-L-lysine as a model protein and oligopeptides from a HIV surface glycoprotein gp120 with positively charged amino acids using surface plasmon resonance (SPR) and dynamic light scattering (DLS) to elucidate the anti-HIV mechanism of sulfated polysaccharides. The apparent association- (k(a)) and dissociation rate (k(d)) constants of dextran and curdlan sulfates against poly-L-lysine were k(a) = 6.92 x 10(4)-2.17 x 10(6) 1/Ms and k(d) = 4.29 x 10(-5)-2.22 x 10(-4) 1/s; these kinetic constants were dependent on the molecular weights and degree of sulfation of sulfated polysaccharides. For interaction, the three oligopeptides from the HIV gp120 were peptide A (297)TRPNNNTRKRIRIQRGPGRA(316) with several lysine (K) and arginine (R) in the V3 loop region, peptide B (493)PLGVAPTKAKRRVVQREKR(511) with several K and R in the C-terminus region, and oligopeptide C (362)KQSSGGDPEIVTHSFNCGG(380) with few basic amino acids in the CD4 binding domain. Sulfated polysaccharides exhibited strong interaction against oligopeptides A and B, (k(a) = 5.48 x 10(4)-2.96 x 10(6) 1/Ms. and k(d) = 1.74 x 10(-4)-6.24 x 10(-3) 1/s), no interaction was noted against oligopeptide C. Moreover, the particle size and zeta potential by DLS indicated the interaction between sulfated polysaccharides and oligopeptides A and B, suggesting the anti-HIV mechanism of sulfated polysaccharides to be the electrostatic interaction of negatively charged sulfated polysaccharides and HIV at the positively charged amino acid regions. (C) 2018 Elsevier B.V. All rights reserved.