Improved Immuno-Detection of a Low-Abundance Cyclophilin Allows the Confirmation of its Expression in a Protozoan Parasite

Abstract

Protein samples can be challenging to analyze due to the presence of high-abundance proteins masking lowabundance proteins of interest, such as biomarkers and novel physiological mediators. Cyclophilins are chaperones involved in the cis/trans isomerization of peptidyl-prolyl bonds in peptides or proteins and have been found in every organism sequenced to date. Although considerable progress has been made in the characterization of some cyclophilins expressed in diverse parasites invading humans, the main aspects of low-abundance members of this family remain unknown. In the present work, we present that the combined strategy of using more specific antibodies and increasing the presence of subcellular proteins in the sample, allowed us to confirm the expression of a 21.1 kDa cyclophilin for the first time in Trypanosoma cruzi.

Insights Into Peptidyl-Prolyl Cis-Trans Isomerases From Clinically Important Protozoans: From Structure to Potential Biotechnological Applications

“…Moreover, TcCyP21, a low-abundance protein with an SP (Figure 6A), was identified in a membrane-enriched fraction [136]. TcCyP22, a homolog of mammalian CyPD, localizes to the mitochondria in all three stages of the T. cruzi life cycle and is involved in parasite cell death under oxidative stress.…”