Recombinant Junin arenavirus Pre-glycoprotein polyprotein GP complex (GPC)

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Description

Structure and Processing of GPC

The GPC is processed into three chains :

  • Stable Signal Peptide (SSP) Association of the SSP is essential for intracellular trafficking and proteolytic maturation of the GPC complex . The SSP interacts with the cytosolic domain of GP2 and is retained as part of the mature GPC .

  • Glycoprotein G1 (GP1)

  • Glycoprotein G2 (GP2) GP2 facilitates the virus's entry into host cells through pH-induced fusion of the viral and endosomal membranes .

Role of Glycosylation

Specific N-linked glycans on the arenavirus surface glycoprotein (GP) mask important epitopes and help the virus evade antibody responses . The N-linked glycosylation profiles of arenavirus glycoproteins are viable targets for designing attenuated viruses for vaccine development against arenavirus-associated illnesses . Glycans facilitate the virus to evade neutralizing antibodies .

Functional Significance

The GPC complex is essential for the virus's infectivity . The stable signal peptide (SSP) plays a crucial role in intracellular trafficking and proteolytic maturation of the GPC complex . A charged residue in SSP, lysine 33, is specifically required for the fusion activity of the GPC complex .

GPC as a Vaccine Target

The GPC is a key target for vaccine development against arenaviruses . Mutations within GPC can attenuate the virus and increase immunogenicity . Antibodies directed against the GPC can neutralize the virus by altering virion binding/fusion . Specific mutations acquired early during serial passaging attenuate visceral disease while not impacting the neurovirulence of the Junin virus .

GPC and SKI-1/S1P Protease

Arenaviruses, including Junin virus, utilize the SKI-1/S1P protease for GPC processing, which is essential for virus growth in cell culture . The SKI-1/S1P protease mediates the major cleavage step for generating mature surface glycoproteins .

Research Findings on GPC Mutations

Virus CloneGPC MutationsVisceral DiseaseNeurovirulenceAttenuation
rRomNoneLethalYesNo
rRom/GPC-R484GR484GLethalYesNo
rRom/GPC-XJ13XJ13-specificNoYesPartial
rRom/GPC-XJ44XJ44-specificDelayed onsetYesYes
rRom/GPC-T168AT168ADelayed onsetYesYes

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your preferred format in order notes for customized preparation.
Lead Time
Delivery times vary depending on the purchase method and location. Contact your local distributor for precise delivery estimates.
Note: All proteins are shipped with standard blue ice packs. Dry ice shipping requires advance notice and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to collect the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard glycerol concentration is 50% and serves as a guideline.
Shelf Life
Shelf life depends on storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized forms have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquot for multiple uses to prevent repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing.
The tag type is determined during the production process. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
GPC; GP-C; Pre-glycoprotein polyprotein GP complex; Pre-GP-C
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
252-485
Protein Length
Full Length of Mature Protein
Species
Junin mammarenavirus (JUNV) (Junn mammarenavirus)
Target Names
GPC
Target Protein Sequence
AFFSWSLTDSSGKDTPGGYCLEEWMLVAAKMKCFGNTAVAKCNLNHDSEFCDMLRLFDYN KNAIKTLNDETKKQVNLMGQTINALISDNLLMKNKIRELMSVPYCNYTKFWYVNHTLSGQ HSLPRCWLIKNNSYLNISDFRNDWILESDFLISEMLSKEYSDRQGKTPLTLVDICFWSTV FFTASLFLHLVGIPTHRHIRGEACPLPHRLNSLGGCRCGKYPNLKKPTVWRRGH
Uniprot No.

Target Background

Function
The Recombinant Junin arenavirus Pre-glycoprotein polyprotein GP complex (GPC) is a class I viral fusion protein. It facilitates fusion between viral and host endosomal membranes, enabling nucleocapsid delivery into the cytoplasm. Membrane fusion occurs through irreversible conformational changes triggered by endosomal acidification. The stable signal peptide (SSP) is cleaved, functioning as a signal peptide and remaining as a component of the GP complex. The SSP is crucial for efficient glycoprotein expression, post-translational maturation (GP1 and GP2 cleavage), glycoprotein transport to the cell surface, infectious virion formation, and acid pH-dependent cell fusion mediated by the glycoprotein. The GPC interacts with the host transferrin receptor (TFRC), mediating viral attachment and subsequent internalization primarily via clathrin-mediated endocytosis.
Protein Families
Arenaviridae GPC protein family
Subcellular Location
[Glycoprotein G1]: Virion membrane; Peripheral membrane protein. Host endoplasmic reticulum membrane; Peripheral membrane protein. Host Golgi apparatus membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein.; [Glycoprotein G2]: Virion membrane; Single-pass membrane protein. Host endoplasmic reticulum membrane; Single-pass membrane protein. Host Golgi apparatus membrane; Single-pass membrane protein. Host cell membrane; Single-pass membrane protein.; [Stable signal peptide]: Virion membrane; Multi-pass membrane protein. Host endoplasmic reticulum membrane; Multi-pass membrane protein. Host Golgi apparatus membrane; Multi-pass membrane protein. Host cell membrane; Multi-pass membrane protein.

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