Recombinant Taenia solium 60S acidic ribosomal protein P2

Overview of Acidic Ribosomal Protein P2

The 60S acidic ribosomal protein P2 is a key component of the ribosomal stalk, critical for GTPase activity during translation elongation. Unlike most ribosomal proteins, it is acidic and forms heterodimers with P1 proteins, anchoring to the P0 protein to create the pentameric P-complex [(P1–P2)–P0–(P1–P2)] . This complex recruits elongation factors (e.g., EF-2) to the ribosome .

Key Features:

• Molecular Weight: ~14–15 kDa (e.g., human RPLP2: 14.2 kDa) .

• Structure:

  • Conserved C-terminal domain (CTD) for interaction with elongation factors.

  • N-terminal domain for oligomerization (e.g., tetramerization in Plasmodium falciparum) .

• Function: Facilitates translation and ribosome biogenesis; non-ribosomal roles include cell signaling and pathogen-host interactions .

Recombinant Production of Ribosomal P2

Recombinant P2 proteins are typically expressed in Escherichia coli or eukaryotic systems (e.g., HEK-293 cells) with tags (e.g., His, GST) for purification . Below is a generalized protocol based on homologous systems:

Interaction with Toxins and Elongation Factors

• Ricin A Chain (RTA): Binds to the CTD of P2 with a dissociation constant ($K_D$) of ~86 nM in humans. Truncated P2 (lacking CTD) shows reduced binding ($K_D$ = 533 nM) .

• GCN2 Kinase Activation: The ribosomal P-stalk (uL10/P1/P2) activates GCN2 during nutrient stress, inducing phosphorylation of eIF2α .

Pathogen-Specific Roles

• Cryptosporidium parvum: Recombinant CpP2 (CTD) is used in ELISA for serologic surveillance (89% sensitivity, 92% specificity) .

• Plasmodium falciparum: Oligomeric P2 translocates to infected erythrocyte surfaces, regulating nuclear division and nutrient import .

Hypothetical Applications for Taenia solium P2

While no studies on Taenia solium P2 exist, insights from homologs suggest potential research directions:

Data Gaps and Future Directions

• Sequence Analysis: No Taenia solium P2 sequence or structural data is available in the provided sources.

• Oligomerization: Studies in Plasmodium suggest pH-dependent tetramerization ; similar analyses are needed for T. solium.

• Host Interaction: Investigate whether T. solium P2 interacts with host proteins (e.g., Band3 in erythrocytes) .

References to Explore (Outside Provided Sources)

1. GenBank: Search for Taenia solium RPLP2 (Accession: Not found in provided data).

2. Structural Databases: Use AlphaFold or cryo-EM to model T. solium P2.

3. Parasitology Studies: Review Taenia-specific ribosomal protein studies in journals like PLoS Neglected Tropical Diseases.