Recombinant HIV type 1 f gp41/gp120

Name: Recombinant HIV type 1 f gp41/gp120
SKU: DAG537
Rating: 5 (1 reviews)

HIV type 1 Glycoprotein 120 (gp120), recombinant protein from E. coli

COA

SDS

Datasheet

Summary

Product Overview

Recombinant Human Immunodeficiency Virus Type 1 (HIV-1) contains the C-terminus of gp120 and most of gp41. Does not contain a fusion partner, was expressed in E. coli.

Nature

Recombinant

Tag/Conjugate

Unconjugated

Purity

> 95% pure (10% PAGE, coomassie staining). S-Sepharose> Ceramic Hydroxyapatite> S-300

Format

Purified, Liquid

Concentration

1 mg/ml

Buffer

50mM Tris, pH 8.0, containing 0.1% SDS, 5mM DTT, 2.5mM EDTA

Preservative

None

Storage

2-8°C short term, -20°C long term

Introduction

Human immunodeficiency virus (HIV) is a lentivirus (a member of the retrovirus family) that causes 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. 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. The four major routes of transmission are unsafe sex, contaminated needles, breast milk, and transmission from an infected mother to her baby at birth (perinatal transmission). Screening of blood products for HIV has largely eliminated transmission through blood transfusions or infected blood products in the developed world.

Antigen Description

gp41/120 is the major HIV protein associated with the HIV envelope. It functions as the viral antireceptor or attachment protein. gp41 (or TM) traverses the envelope, whereas gp120 is present on the outer surface and is noncovalently attached to gp41. The precursor of gp120/41 (gp160) is synthesized in the endoplasmic reticulum and is transported via the golgi body to the cell surface. Upon activation of the envelope glycoprotein (gp120/41) by cellular receptors, gp41 undergoes conformational changes that mediate fusion of the viral and cellular membranes.

Keywords

HIV-1 gp120; HIV1 gp120; Envelope surface glycoprotein gp120; Glycoprotein 120; gp120; gp120 glycoprotein; Human Immunodeficiency Virus 1; SU; Surface protein; Retroviridae; Lentivirus; human immunodeficiency virus

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody

NATURE STRUCTURAL & MOLECULAR BIOLOGY

Authors: Yang, Zhi; Wang, Haoqing; Liu, Albert Z.; Gristick, Harry B.; Bjorkman, Pamela J.

Abstract

The human immunodeficiency virus (HIV-1) envelope (Env) glycoprotein, a (gp120-gp41)(3) trimer, mediates fusion of viral and host cell membranes after gp120 binding to host receptor CD4. Receptor binding triggers conformational changes allowing coreceptor (CCR5) recognition through CCR5's tyrosine-sulfated amino (N) terminus, release of the gp41 fusion peptide and fusion. We present 3.3 angstrom and 3.5 angstrom cryo-EM structures of E51, a tyrosine-sulfated coreceptor-mimicking antibody, complexed with a CD4-bound open HIV-1 native-like Env trimer. Two classes of asymmetric Env interact with E51, revealing tyrosine-sulfated interactions with gp120 mimicking CCR5 interactions, and two conformations of gp120-gp41 protomers (A and B protomers in AAB and ABB trimers) that differ in their degree of CD4-induced trimer opening and induction of changes to the fusion peptide. By integrating the new structural information with previous closed and open envelope trimer structures, we modeled the order of conformational changes on the path to coreceptor binding site exposure and subsequent viral-host cell membrane fusion.

Critical design criteria for engineering a nanoparticulate HIV-1 vaccine

JOURNAL OF CONTROLLED RELEASE

Authors: Thalhauser, Stefanie; Peterhoff, David; Wagner, Ralf; Breunig, Miriam

Abstract

Inducing a long-lasting as well as broad and potent immune response by generating broadly neutralizing antibodies is a major goal and at the same time the main challenge of preventive HIV-1 vaccine design. Immunization with soluble, stabilized and native-like envelope (Env) glycoprotein so far only led to low neu-tralization breadth and displayed low immunogenicity. A promising approach to generate a potent immune response is the presentation of Env on the surface of nanoparticles. In this review, we will focus on two key processes essential for the induction of immune response that can be addressed by specific features of nanoparticulate carriers: first, the trafficking to and within distinct compartments of the lymph node, and second, the use of multivalent Env display allowing for high avidity interactions. To optimize these pivotal steps critical design criteria should be considered for the presentation of Env on nanoparticles. These include an optimal particle size below 100 nm, distances between two adjacent Env antigens of approximately 10-15 nm, an appropriate orientation of Env, and finally, the stability of both the Env attachment and the nanoparticle platform. Hence, an interdisciplinary approach that combines a suitable delivery system and a straightforward presentation of the Env antigen may have the potential to drive the immune response towards increased breadth and potency.