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Evolutionarily Diverged TRAPP Components in Giardia lamblia That Lacks a Classical Golgi
Avishikta Chatterjee1, Kuladip Jana1, Sandipan Ganguly2
1Department of Biological Sciences, Bose Institute, Kolkata, West Bengal, India.
Molecular Microbiology
|January 14, 2026
Summary
Giardia lamblia lacks a Golgi, but possesses a unique TRAPP complex. This TRAnsport Protein Particle complex aids in cargo sorting and has unique interactions and functions in Giardia.
Area of Science:
- Cell Biology
- Parasitology
- Molecular Biology
Background:
- The intestinal pathogen Giardia lamblia lacks a Golgi compartment, raising questions about its intracellular cargo sorting mechanisms.
- While Golgi-associated proteins like SNAREs and Rabs are known in Giardia, the TRAPP complex remains uncharacterized.
Purpose of the Study:
- To investigate the presence and function of the TRAPP complex in Giardia lamblia.
- To understand how cargo sorting occurs in the absence of a canonical Golgi apparatus.
Main Methods:
- Identified and characterized TRAPP complex components (GlBet3, GlBet5, GlTrs23, GlTrs31) in Giardia.
- Assessed interactions between TRAPP components, Rabs (GlRab1a, GlRab11), and COPII proteins (GlSec23).
- Utilized colocalization and coimmunoprecipitation techniques.
Main Results:
- Giardia expresses a minimal set of TRAPP components, forming a functional complex with a distinct architecture compared to yeast.
- TRAPP components interact with GlRab1a, GlRab11, and GlSec23, suggesting a role in vesicle trafficking.
- TRAPP genes are upregulated during encystation, with components found on specific vesicles.
Conclusions:
- A functional TRAPP complex exists in Giardia, albeit with a unique structure and interactions.
- The TRAPP complex likely plays a role in Giardia's unique cellular processes, including encystation and the function of structures like the ventral disc and median body.
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