An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids
African trypanosomes are evolutionarily highly divergent parasitic protozoa, and as a consequence the vast majority of trypanosome membrane proteins remain uncharacterised in terms of location, trafficking or function. Here we describe a novel family of type I membrane proteins which we designate ‘i...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Shared Science Publishers OG
2014-10-01
|
| Series: | Microbial Cell |
| Subjects: | |
| Online Access: | http://microbialcell.com/researcharticles/an-extensive-endoplasmic-reticulum-localised-glycoprotein-family-in-trypanosomatids/ |
| _version_ | 1826532035999563776 |
|---|---|
| author | Harriet Allison Amanda J. O’Reilly Jeremy Sternberg Mark C. Field |
| author_facet | Harriet Allison Amanda J. O’Reilly Jeremy Sternberg Mark C. Field |
| author_sort | Harriet Allison |
| collection | DOAJ |
| description | African trypanosomes are evolutionarily highly divergent parasitic protozoa, and as a consequence the vast majority of trypanosome membrane proteins remain uncharacterised in terms of location, trafficking or function. Here we describe a novel family of type I membrane proteins which we designate ‘invariant glycoproteins’ (IGPs). IGPs are trypanosome-restricted, with extensive, lineage-specific paralogous expansions in related taxa. In T. brucei three IGP subfamilies, IGP34, IGP40 and IGP48 are recognised; all possess a putative C-type lectin ectodomain and are ER-localised, despite lacking a classical ER-retention motif. IGPs exhibit highest expression in stumpy stage cells, suggesting roles in developmental progression, but gene silencing in mammalian infective forms suggests that each IGP subfamily is also required for normal proliferation. Detailed analysis of the IGP48 subfamily indicates a role in maintaining ER morphology, while the ER lumenal domain is necessary and sufficient for formation of both oligomeric complexes and ER retention. IGP48 is detected by antibodies from T. b. rhodesiense infected humans. We propose that the IGPs represent a trypanosomatid-specific family of ER-localised glycoproteins, with potential contributions to life cycle progression and immunity, and utilise oligomerisation as an ER retention mechanism. |
| first_indexed | 2024-12-21T04:44:28Z |
| format | Article |
| id | doaj.art-590b17d24a714e6b9d16e35f1d37e708 |
| institution | Directory Open Access Journal |
| issn | 2311-2638 |
| language | English |
| last_indexed | 2025-03-14T01:44:50Z |
| publishDate | 2014-10-01 |
| publisher | Shared Science Publishers OG |
| record_format | Article |
| series | Microbial Cell |
| spelling | doaj.art-590b17d24a714e6b9d16e35f1d37e7082025-03-12T13:46:43ZengShared Science Publishers OGMicrobial Cell2311-26382014-10-0111032534510.15698/mic2014.10.170An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatidsHarriet Allison0Amanda J. O’Reilly1Jeremy Sternberg2Mark C. Field3Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, Scotland, DD1 5EH.Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, Scotland, DD1 5EH.School of Biological Sciences, University of Aberdeen, Aberdeen, AB24 2TZ, UK.Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, Scotland, DD1 5EH.African trypanosomes are evolutionarily highly divergent parasitic protozoa, and as a consequence the vast majority of trypanosome membrane proteins remain uncharacterised in terms of location, trafficking or function. Here we describe a novel family of type I membrane proteins which we designate ‘invariant glycoproteins’ (IGPs). IGPs are trypanosome-restricted, with extensive, lineage-specific paralogous expansions in related taxa. In T. brucei three IGP subfamilies, IGP34, IGP40 and IGP48 are recognised; all possess a putative C-type lectin ectodomain and are ER-localised, despite lacking a classical ER-retention motif. IGPs exhibit highest expression in stumpy stage cells, suggesting roles in developmental progression, but gene silencing in mammalian infective forms suggests that each IGP subfamily is also required for normal proliferation. Detailed analysis of the IGP48 subfamily indicates a role in maintaining ER morphology, while the ER lumenal domain is necessary and sufficient for formation of both oligomeric complexes and ER retention. IGP48 is detected by antibodies from T. b. rhodesiense infected humans. We propose that the IGPs represent a trypanosomatid-specific family of ER-localised glycoproteins, with potential contributions to life cycle progression and immunity, and utilise oligomerisation as an ER retention mechanism.http://microbialcell.com/researcharticles/an-extensive-endoplasmic-reticulum-localised-glycoprotein-family-in-trypanosomatids/Trypanosoma bruceiprotein sortingexocytosisvariant surface glycoproteinendoplasmic reticulumevolutiontrypanosome |
| spellingShingle | Harriet Allison Amanda J. O’Reilly Jeremy Sternberg Mark C. Field An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids Microbial Cell Trypanosoma brucei protein sorting exocytosis variant surface glycoprotein endoplasmic reticulum evolution trypanosome |
| title | An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids |
| title_full | An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids |
| title_fullStr | An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids |
| title_full_unstemmed | An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids |
| title_short | An extensive endoplasmic reticulum-localised glycoprotein family in trypanosomatids |
| title_sort | extensive endoplasmic reticulum localised glycoprotein family in trypanosomatids |
| topic | Trypanosoma brucei protein sorting exocytosis variant surface glycoprotein endoplasmic reticulum evolution trypanosome |
| url | http://microbialcell.com/researcharticles/an-extensive-endoplasmic-reticulum-localised-glycoprotein-family-in-trypanosomatids/ |
| work_keys_str_mv | AT harrietallison anextensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT amandajoreilly anextensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT jeremysternberg anextensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT markcfield anextensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT harrietallison extensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT amandajoreilly extensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT jeremysternberg extensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids AT markcfield extensiveendoplasmicreticulumlocalisedglycoproteinfamilyintrypanosomatids |