RPL27

RPL27 is a Toxoplasma gondii ribosomal protein identified as a candidate binding target of the antiparasitic trithiolato arene ruthenium complex 9, recovered by affinity chromatography and mass spectrometry alongside translation elongation factor 1α and RPS18 (PMID:28652238). Beyond this single affinity-based identification, no molecular function, structural detail, or functional validation of RPL27 has been characterized in the available corpus.

1. 2017 Low

   To identify the parasite targets of an antiparasitic ruthenium complex, affinity capture was used, placing RPL27 among candidate binding proteins and implicating the translation machinery as a possible drug interaction site.

   Evidence Affinity chromatography with compound-coupled Sepharose followed by mass spectrometry in T. gondii

   PMID:28652238

   Open questions at the time

   • Binding inferred from MS identification only, not confirmed by reciprocal or orthogonal method
   • No functional validation or mutagenesis linking RPL27 to compound activity
   • No characterization of RPL27's role in ribosome function or translation

• Whether RPL27 is a genuine functional target of the ruthenium complex, and what its molecular role in the parasite ribosome and translation is, remains unresolved.
• No orthogonal confirmation of the RPL27-compound interaction
• No structural or biochemical characterization of RPL27
• No genetic or phenotypic evidence of RPL27 function