scholarly journals Late ESCRT machinery mediates the recycling and Rescue of Invariant Surface Glycoprotein 65 in Trypanosoma brucei

2020 ◽  
Vol 22 (11) ◽  
Author(s):  
Khan Umaer ◽  
James D. Bangs
Keyword(s):  
Trypanosoma Brucei ◽  
Surface Glycoprotein ◽  
Invariant Surface ◽  
Escrt Machinery

scholarly journals Late ESCRT Machinery Mediates The Recycling And Rescue of Invariant Surface Glycoprotein 65 in Trypanosoma brucei

2020 ◽  
Author(s):  
Khan Umaer ◽  
James D. Bangs
Keyword(s):  
Trypanosoma Brucei ◽  
Protein Trafficking ◽  
Protein Complexes ◽  
Surface Glycoprotein ◽  
Invariant Surface ◽  
Accelerated Degradation ◽  
Escrt Machinery ◽  
Cargo Delivery ◽  
Late Endosomes

ABSTRACTThe Endosomal Sorting Complex Required for Transport machinery consists of four protein complexes (ESCRT 0-IV) and the post ESCRT ATPase Vps4. ESCRT mediates cargo delivery for lysosomal degradation via formation of multivesicular bodies. Trypanosoma brucei contains orthologues of ESCRT I-III and Vps4. Trypanosomes also have a ubiquitinylated invariant surface glycoprotein (ISG65) that is delivered to the lysosome by ESCRT, however, we previously implicated TbVps4 in rescue and recycling of ISG65. Here we use conditional silencing to investigate the role of TbVps24, a phosphoinositide-binding ESCRT III component, on protein trafficking. TbVps24 localizes to the TbRab7+ late endosome, and binds PI(3,5)P2, the product of the TbFab1 kinase, both of which also localize to late endosomes. TbVps24 silencing is lethal, and negatively affects biosynthetic trafficking of the lysosomal markers p67 and TbCathepsin L. However, the major phenotype of silencing is accelerated degradation and depletion of the surface pool of ISG65. Thus, TbVps24 silencing phenocopies that of TbVps4 in regard to ISG65 trafficking. This presents a paradox since we have previously found that depletion of TbFab1 completely blocks ISG65 turnover. We propose a model in which late ESCRT components operate at two sites, one PI(3,5)P2-dependent (degradation) and one PI(3,5)P2-independent (recycling), to regulate ISG65 homeostasis.

Genomic organization of an invariant surface glycoprotein gene family of Trypanosoma brucei

1995 ◽  
Vol 69 (1) ◽  
pp. 53-63 ◽  
Author(s):  
Karl Ziegelbauer ◽  
Gloria Rudenko ◽  
Rudo Kieft ◽  
Peter Overath
Keyword(s):  
Gene Family ◽  
Trypanosoma Brucei ◽  
Genomic Organization ◽  
Surface Glycoprotein ◽  
Invariant Surface ◽  
Glycoprotein Gene

scholarly journals The crystal structure and localization of Trypanosoma brucei invariant surface glycoproteins suggest a more permissive VSG coat in the tsetse-transmitted metacyclic stage

2018 ◽  
Author(s):  
Aitor Casas-Sánchez ◽  
Samïrah Perally ◽  
Raghavendran Ramaswamy ◽  
Lee R. Haines ◽  
Clair Rose ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Trypanosoma Brucei ◽  
Fluorescent Microscopy ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Surface Glycoprotein ◽  
Invariant Surface ◽  
Helical Bundle ◽  
N Terminus ◽  
Key Features

AbstractTrypanosoma brucei spp. develop into mammalian-infectious metacyclic trypomastigotes inside the tsetse salivary glands. Besides acquiring a variant surface glycoprotein (VSG) coat, nothing is known about expression of invariant surface antigens by the metacyclic stage. Proteomic analysis of saliva from T. brucei-infected flies revealed a novel family of hypothetical GPI-anchored surface proteins herein named Metacyclic Invariant Surface Proteins (MISP). MISP are encoded by five homolog genes and share ~80% protein identity. The crystal structure of MISP N-terminus at 1.82 Å resolution revealed a triple helical bundle that shares key features with other trypanosome surface proteins. However, molecular modelling combined with live fluorescent microscopy suggest that MISP N-termini are extended above the metacyclic VSG coat, exposing immunogenic epitopes. Collectively, we suggest that the metacyclic cell surface architecture appears more permissive than bloodstream forms in terms of expression of invariant GPI-anchored glycoproteins, which could be exploited for the development of novel vaccines against African trypanosomiases.

Bloodstream form trypanosome plasma membrane proteins: antigenic variation and invariant antigens

Parasitology ◽  
2010 ◽  
Vol 137 (14) ◽  
pp. 2029-2039 ◽  
Author(s):  
ANGELA SCHWEDE ◽  
MARK CARRINGTON
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Brucei ◽  
Antigenic Variation ◽  
Adaptive Immune System ◽  
Surface Proteins ◽  
Surface Glycoprotein ◽  
Invariant Surface ◽  
Adaptive Immune ◽  
External Face

SUMMARYTrypanosoma bruceiis exposed to the adaptive immune system and complement in the blood of its mammalian hosts. The aim of this review is to analyse the role and regulation of the proteins present on the external face of the plasma membrane in the long-term persistence of an infection and transmission. In particular, the following are addressed: (1) antigenic variation of the variant surface glycoprotein (VSG), (2) the formation of an effective VSG barrier shielding invariant surface proteins, and (3) the rapid uptake of VSG antibody complexes combined with degradation of the immunoglobulin and recycling of the VSG.

Trypanosoma brucei: Immunisation with plasmid DNA encoding invariant surface glycoprotein gene is able to induce partial protection in experimental African trypanosomiasis

2011 ◽  
Vol 127 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Andreia Sofia Cruz Lança ◽  
Karina Pires de Sousa ◽  
Jorge Atouguia ◽  
Duarte Miguel F. Prazeres ◽  
Gabriel Amaro Monteiro ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Plasmid Dna ◽  
Surface Glycoprotein ◽  
African Trypanosomiasis ◽  
Dna Encoding ◽  
Invariant Surface ◽  
Partial Protection ◽  
Glycoprotein Gene

scholarly journals The phospholipase A1 of Trypanosoma brucei does not release myristate from the variant surface glycoprotein.

1986 ◽  
Vol 261 (7) ◽  
pp. 3229-3232
Author(s):  
P N Hambrey ◽  
C M Forsberg ◽  
A Mellors
Keyword(s):  
Trypanosoma Brucei ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Phospholipase A1

scholarly journals Synchronous expression of individual metacyclic variant surface glycoprotein genes in Trypanosoma brucei

2015 ◽  
Vol 200 (1-2) ◽  
pp. 1-4 ◽  
Author(s):  
Kiantra Ramey-Butler ◽  
Elisabetta Ullu ◽  
Nikolay G. Kolev ◽  
Christian Tschudi
Keyword(s):  
Trypanosoma Brucei ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein

Depletion of 14-3-3 proteins in bloodstream-form Trypanosoma brucei inhibits variant surface glycoprotein recycling

2010 ◽  
Vol 40 (5) ◽  
pp. 629-634 ◽  
Author(s):  
Corinna Benz ◽  
Markus Engstler ◽  
Stefan Hillmer ◽  
Christine Clayton
Keyword(s):  
Trypanosoma Brucei ◽  
Bloodstream Form ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein

scholarly journals Subnuclear localization of the active variant surface glycoprotein gene expression site in Trypanosoma brucei

1998 ◽  
Vol 95 (21) ◽  
pp. 12328-12333 ◽  
Author(s):  
I. Chaves ◽  
J. Zomerdijk ◽  
A. Dirks-Mulder ◽  
R. W. Dirks ◽  
A. K. Raap ◽  
...  
Keyword(s):  
Gene Expression ◽  
Trypanosoma Brucei ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Subnuclear Localization ◽  
Glycoprotein Gene ◽  
Expression Site ◽  
Active Variant
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