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Recombinant Human immunodeficiency virus type 1 group M subtype B Envelope glycoprotein gp160 (env), partial

Recombinant Human immunodeficiency virus type 1 group M subtype B Envelope glycoprotein gp160 (env), partial

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Code	CSB-EP361302HKP
Abbreviation	Recombinant Human immunodeficiency virus type 1 group M subtype B env protein, partial
MSDS	MSDS Datasheet
Size	$224
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Target Background

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

env

Uniprot No.

P04578

Research Area

Others

Alternative Names

envEnvelope glycoprotein gp160; Env polyprotein) [Cleaved into: Surface protein gp120; SU; Glycoprotein 120; gp120); Transmembrane protein gp41; TM; Glycoprotein 41; gp41)]

Species

Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)

Source

E.coli

Expression Region

33-511aa

Target Protein Sequence

KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKR
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

69.7 kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-SUMO-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

Amino acids 33-511 form the expressed segment for recombinant HIV-1 env. The calculated molecular weight for this env protein is 69.7 kDa. This env protein is produced using e.coli expression system. The N-terminal 6xHis-SUMO tag was smoothly integrated into the coding gene of env, which enables a simple process of detecting and purifying the env recombinant protein in the following steps.

The human immunodeficiency virus type 1 (HIV-1) group M subtype B Envelope glycoprotein gp160, commonly referred to as env, is a key structural protein of the HIV-1 virus. Env is initially synthesized as a precursor glycoprotein, gp160, which is subsequently cleaved into two subunits, gp120 and gp41, during viral maturation. Gp120 is responsible for binding to the CD4 receptor on the surface of host immune cells, initiating the viral entry process. Gp41 facilitates the fusion of the viral and host cell membranes, allowing the virus to enter the host cell. The env gene is highly variable, contributing to the extensive diversity of HIV-1, and its genetic variation poses challenges for vaccine development. Understanding the structure and function of the HIV-1 Env glycoprotein is crucial for developing strategies to combat HIV/AIDS, including the design of antiretroviral drugs and vaccines aimed at preventing viral entry and infection.

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Target Background

Function

Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.; 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. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells.; Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.

Gene References into Functions

Data show that the cleavage-independent HIV envelope glycoprotein (Env) trimers exhibit quaternary protein structure. PMID: 29769533
Extracellular vesicles that carry Env seem to facilitate HIV infection. PMID: 28490736
Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers. PMID: 29222332
sequence coverage for Env provides semi-quantitative analysis of the glycosylation status at each glycosite. PMID: 28348411
Binding stability to beta2-microglobulin may confer to HLA-C the ability to preferentially act either as a conventional immune-competent molecule or as an accessory molecule involved in HIV-1 infectivity via viral envelope glycoprotein binding. PMID: 28051183
heptad region 1 connecting loop is a key determinant of HIV-1 trimer metastability PMID: 27349805
These findings highlight regions of cross talk between gp120 and gp41 and identify heptad repeat region 1(HR1) residues that play important roles in regulating CD4-induced conformational changes in Env. PMID: 29875245
Solution structure and membrane interaction of the cytoplasmic tail of HIV-1 gp41 protein has been described. PMID: 29056482
effective antibody that prevents immune escape must selectively bind to high escape cost residues that are surrounded by those where mutations incur a low fitness cost PMID: 29311326
Conserved residues from the signal peptide and residues downstream of the canonical cleavage site form an extended alpha-helix in the endoplasmic reticulum membrane, which covers the cleavage site, thus preventing cleavage. PMID: 28753126
In this study, the authors found the expression of MARCH2 to be upregulated upon HIV-1 infection. MARCH2 inhibits the production and infection of HIV-1 through ligase activity-dependent envelope protein degradation and/or intracellular retention. PMID: 29573664
These data indicate that GPI-scFvs can inhibit Env processing and function, thereby restricting production and infectivity of newly synthesized HIV. PMID: 29321330
Study uses molecular dynamics to provide insight into its structural dynamics and into how both protomer and glycan movements coordinate to shield the Env protein surface; results provide a microsecond-based understanding of the Env glycan shield. PMID: 28890362
The alpha helix 1 from the first conserved region of HIV1 gp120 is reconstructed in the short NQ21 peptide. PMID: 29273432
gp120IIIB promotes the downregulation of CHRFAM7A in neuronal cells. PMID: 26567012
These observations suggest that modulation of N332 glycan occupancy by the second amino acid position of the canonical glycosylation motif Asn-X-Ser plays a previously unappreciated role in viral escape from immune responses. PMID: 27258397
Study reported that DPF1, a short-degraded peptide fragment derived from native gp120-loaded rat hepatocytes, immediately forms fibrils by self-assembly and thus enhances HIV-1 infection. Furthermore, DPF1 accelerates the formation of seminal amyloid fibrils by PAP248-286 and SEM186-107. The newly formed amyloid fibrils retain the ability to enhance HIV-1 infection PMID: 28978437
Data suggest that, beyond hydrophobicity, preserving sequence order (the tandem repeat of the FLGFLG tripeptide) is an important feature for defining the secondary structures and oligomeric states adopted in membranes by the HIV fusion peptide of gp41. (Note that gp41 is coded with gp120 as one gp160 by the env gene of HIV.) PMID: 28930470
crystal structures of trimeric HIV envelope with entry inhibitors BMS-378806 and BMS-626529 PMID: 28825711
Upon gp120 binding to DC-SIGN, cellular NF-kappaB signaling was triggered, leading to the induction of matrix metalloproteinases, which subsequently degraded tight junction proteins and disrupted the blood-retinal barrier integrity. PMID: 27605665
The data data suggest that interactions between HIV-1 gp120 and A2 exist, though this interaction may be indirect. PMID: 27863502
Env regions that respond to CCR5 binding was located in the gp120 alpha1 helix and in the gp41 HR1 heptad repeat and membrane-proximal external region. PMID: 28521215
Glycosylation of V1V2 domain of HIV envelope protein determined its binding to alpha4ss7 integrin. PMID: 28577856
study revealed that while HIV-1 gp120 and Staph aureus LukED both target CCR5, they bind to different regions of the receptor, highlighting the divergence of the pathogens PMID: 27965453
Data suggest that core glycans of gp120 form of HIV-1 envelope protein are not essential for protein folding or viral infectivity; thus, the likely primary role of glycosylation of gp120 is enabling immune evasion. PMID: 28446609
The HIV gp160 envelope protein carries out two major functions, membrane fusion and immune suppression. (Review) PMID: 27793589
The transferred nuclear Overhauser effect (TRNOE) crosspeaks in the ternary complex were assigned to the specific Tyr protons in the human C-C chemokine receptor 5 (CCR5) chemokine receptor peptide and to methyl protons, predominantly of isoleucine residues, and also of leucine and/or valine residues of HIV-1 gp120 envelope protein. PMID: 27701820
initial contact of CD4 with the HIV-1 Env trimer at 6.8-A resolution, is reported. PMID: 28218750
Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein.( PMID: 28283570
The increased HIV-1 sensitivity to anti-gp41 antibodies and peptides suggests that SER5 also delays refolding of the remaining fusion-competent Env trimers. PMID: 28179429
Broadly neutralizing antibodies (bnAbs) PGT145 recognizes a quaternary epitope at the apical 3-fold symmetry axis of the envelope (Env) trimer. PMID: 28423342
Key features of the HIV-1 envelope protein that are associated with viral resistance to the IFITM3 protein. PMID: 28100616
The GP120 Phe 43 cavity modulates recognition of CRF01_AE HIV-1-infected cells by serum antibodies isolated from RV144 vaccinees. PMID: 28100618
The authors have found that the hydrophobicity of residue 69 is important for Env processing, CD4 binding, and its transition to the CD4-bound conformation. PMID: 27384653
We report on the production and analysis of HIV-1 Env-specific human monoclonal antibodies. PMID: 27630232
the bilayer curvature modifying properties of a synthetic variant of the HIV-1 gp41 fusion peptide with lipid bilayer vesicles composed of a mixture of dimyristoyl phosphatidylcholine (DMPC) and dimyristoyl phosphatidylserine (DMPS) were studied PMID: 28104377
Ficolin-2 protein could bind with HIV-1 envelope glycoprotein gp120, and subsequently induce complement dependent cytotoxicity. PMID: 27576476
Residue 22 in the envelope glycoprotein V3 region of HIV-1B significantly influences the infectivity of the virus. PMID: 27815696
These results provide evidence that cytoplasmic domains can induce conformational changes in functional regions of gp120 and determine receptor tropism but do not modulate HIV-1 co-receptor specificity. PMID: 27488878
Study presents the 3.4 A structure of a fully glycosylated HIV-1 pre-fusion trimer from clade G and characterize the organization of glycans and clustering of oligomannose residues. Additionally, the 3.7 A structures of fully glycosylated HIV-1 pre-fusion trimers from clades A and B are presented and carried out molecular dynamics simulations and other analyses to provide insight into antibody-glycan interactions. PMID: 27114034
N-linked glycans may impact the infectivity of HIV-1; the distribution of potential N-linked glycosylation sites in gp120 differs among major HIV-1 subtypes circulating in China. PMID: 26384088
The authors provide the first evidence that shows CCR5 interaction with a dual-tropic HIV-1 Env played a significant role in Env-induced depletion of CD4 T cells. PMID: 27026376
These results show how a transmembrane domain anchors, stabilizes, and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design. PMID: 27338706
findings suggested that HIV-1 gp41-I90 ectodomain can enhance the transmigration of THP-1 through Cn-infected BBB, which may be mediated by CD44. PMID: 26897523
mechanism by which gp41's function alternates from membrane fusion facilitation to suppression of TCR activation. PMID: 26823547
Taken together, these results suggest that HIV-1 gp120 induces hippocampal neuron apoptosis by enhancement of the Ik, which might be associated with increased Kv2.1 expression via the p38 MAPK pathway. PMID: 26393286
Data suggest that HIV-1 gp41 transmembrane domain (TMD) directly interacts with TMDs of the T-cell receptor and it's CD3-antigen co-receptors (delta, gamma, and epsilon); these interactions appear to be involved in immune evasion mechanism of HIV-1. PMID: 26828096
IFITM2 and IFITM3 specifically antagonize the HIV-1 envelope glycoprotein (Env), thereby inhibiting viral infection. PMID: 26387945
HIV-1 JRCSF variant makes functionally critical contacts with human CCR5 coreceptor amino terminus and extracellular loop 1 (ECL1) and adaptation to murine ECL1 requires multiple mutations in the crown of gp120's V3 loop. PMID: 26114311
Here, the authors show that a highly conserved tryptophan at position 69 of the gp120 inner domain is important for antibody-dependent cellular cytotoxicity mediated by anti-cluster A antibodies and sera from HIV-1-infected individuals. PMID: 26637462

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Subcellular Location

[Surface protein gp120]: Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein. Host endosome membrane; Single-pass type I membrane protein.; [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein.

Protein Families

HIV-1 env protein family

Database Links

KEGG: vg:155971

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