GP5 is a glycosylated envelope protein encoded by the ORF5 gene of the Porcine Reproductive and Respiratory Syndrome Virus (PRRSV). It is also implicated in human breast cancer progression. Key characteristics include:
Feature
Description
Molecular Weight
~25 kDa (viral GP5); ~39 kDa (human GP5 in breast cancer)
Glycosylation Sites
N34, N44, N51 (PRRSV GP5)
Structural Domains
Signal peptide, transmembrane region, antigenic determinants (e.g., epitope B)
Biological Roles
Viral entry, immune evasion, tumor metastasis
GP5 Antibodies in Virology
GP5 is a primary target for neutralizing antibodies in PRRSV research.
Key Findings:
Neutralizing Epitopes:
Epitope B (amino acids 36–52) induces neutralizing antibodies, while epitope A suppresses their production.
Monoclonal antibodies (mAbs) against GP5 exhibit strain-specific neutralization.
Example: mAb BNW7p5c4 neutralizes homologous PRRSV strains (e.g., ATP) but fails against heterologous strains (e.g., VR2332).
Glycosylation Impact:
N-linked glycosylation at N44 is critical for PRRSV infectivity. Mutations at N34/N51 enhance antibody neutralization sensitivity.
Table 1: GP5 Antibody Neutralization Efficacy in PRRSV
Antibody Type
Target Epitope
Neutralization Efficiency
Reference
BNW7p5c4 (mAb)
GP5 epitope B
50% neutralization at 34.4 µg/mL (ATP strain)
Anti-GP4 mAbs
GP4
Limited cross-strain efficacy
Polyclonal antisera
GP5 ectodomain
Enhanced immunogenicity in glycosylation mutants
GP5 in Breast Cancer and Antibody Applications
GP5 overexpression in breast cancer (BC) correlates with tumor progression via the PI3K/AKT/EMT pathway.
Research Highlights:
Expression Levels:
GP5 mRNA is 3–5× higher in BC tissues compared to paracancerous tissues.
Associated with higher TNM stages and HER2 negativity.
Functional Studies:
GP5 knockdown reduces BC cell proliferation and invasion by 40–60%.
Anti-GP5 antibodies (e.g., A03425) are used to detect GP5 in IHC and WB assays.
Mechanistic Insights from Proteomics
GP5 interacts with host proteins to modulate immune responses:
GGP5 Antibody plays a crucial role in glucosinolate biosynthesis. It acts as a hydrolase, cleaving the gamma-glutamyl peptide bond within various glutathione (GSH) conjugates. This process generates Cys-Gly conjugates, which are essential intermediates in the synthesis of glucosinolates. The gamma-Glu-Cys-Gly-GSH conjugates serve as sulfur donors in this biosynthetic pathway.