Last update 01 Nov 2024

TSG101

Last update 01 Nov 2024

Basic Info

Synonyms

ESCRT-I complex subunit TSG101, TSG10, TSG101

+ [5]

Introduction

Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). It may also play a role in the extracellular release of microvesicles that differ from the exosomes (PubMed:22315426).

Drugs associated with TSG101

FGI-1011A6

Target

TSG101

Mechanism

TSG101 inhibitors

Active Org.-

Originator Org.

Gradalis, Inc.

Active Indication-

Inactive Indication

Influenza, Human [+2]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

FGI-102 series

Target

TSG101

Mechanism

TSG101 inhibitors

Active Org.-

Originator Org.

Functional Genetics, Inc.

Active Indication-

Inactive Indication

Virus Diseases

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with TSG101

NCT01299142 / Unknown statusPhase 1

Phase I Study of Human Monoclonal Antibody (FGI-101-1A6) in Normal Healthy Volunteers

The purpose of this study is to determine the safety and tolerability of the anti-TSG101 human monoclonal antibody (FGI-101-1A6)when administered intravenously to healthy volunteers.

Start Date01 Jan 2011

Sponsor / Collaborator

Functional Genetics, Inc.

[+1]

100 Clinical Results associated with TSG101

100 Translational Medicine associated with TSG101

0 Patents (Medical) associated with TSG101

982

Literatures (Medical) associated with TSG101

01 Jan 2025·Arquivos Brasileiros de Oftalmologia

Protein profile of purified plasma- and aqueous humor-derived extracellular vesicles from patients with ocular toxoplasmosis

Article

Author: Burnier, Miguel N ; Belfort, Rubens ; Pessuti, Carmen Luz ; Nascimento, Heloisa ; Commodaro, Alessandra G ; Tsering, Thupten ; Ribeiro, Kleber ; Burnier, Julia V ; Costa, Deise F ; Abdouh, Mohamed

PURPOSETo characterize the extracellular vesicle protein cargo in the aqueous humor and plasma of patients with ocular toxoplasmosis.METHODSAqueous humor and plasma were collected from six patients with active ocular toxoplasmosis and six patients with cataract. Extracellular vesicles were isolated, and western blotting and mass spectrometry were performed for protein analysis.RESULTSAll plasma samples from patients with ocular toxoplasmosis and cataract were positive for the tetraspanins CD63 and TSG101. However, the aqueous humor from patients with ocular toxoplasmosis was positive only for CD63. Sixty-seven new unreported proteins were identified in the aqueous humor and plasma of patients with the ocular toxoplasmosis and cataract. Of the 67 proteins, 10 and 7 were found only in the cataract and ocular toxoplasmosis groups, respectively. In general, these proteins were involved in immune system activation and retina homeostasis and were related to infections and retina-associated diseases.CONCLUSIONThe distinct protein signatures between ocular toxoplasmosis and cataract may be helpful in the differential diagnosis of ocular toxoplasmosis. However, more studies are needed to better understand the role of these proteins in the pathogenesis of ocular toxoplasmosis.

31 Dec 2024·Platelets

Storage of plasma-derived exosomes: evaluation of anticoagulant use and preserving temperatures

Article

Author: He, Yuyu ; Yang, Caiting ; Han, Jie ; Liu, Xiaochun ; Liu, Hai ; Dong, Li ; Zhang, Zhenhua ; Duan, Huiping ; He, Jing ; Zhang, Lizhong ; Waqas, Farooq

Exosomes carry large cargo of proteins, lipids, and nucleic acids, serving as versatile biomarkers for disease diagnosis and vehicles for drug delivery. However, up to date, no well recognized standard procedures for exosome storage were available for clinical application. This study aimed to determine the optimal storage conditions and the anticoagulants for plasma-derived exosome isolation. Fresh whole blood samples were collected from healthy participants and preserved in four different anticoagulants including sodium citrate (SC1/4), sodium citrate (SC1/9), lithium heparin (LH), or Ethylenediamine tetraacetic acid (EDTA), respectively. Exosomes were extracted from the plasma by differential ultracentrifugation and stored at three different temperatures, 4°C, -20°C or - 80°C for a duration ranging from one week to six months. All plasma samples for storage conditions comparison were pretreated with LH anticoagulant. Exosome features including morphological characteristics, pariticles size diameter, and surface protein profiles (TSG101, CD63, CD81, CD9, CALNEXIN) were assessed by transmission electron microscopy, Nanoparticle Tracking Analysis, and Western Blotting, respectively. Exosomes preserved in LH and SC1/4 group tended to remain intact microstructure with highly abundant protein biomarkers. Exosomes stored at 4°C for short time were prone to be more stable compared to thos at -80°C. Exosomes stored in plasma were superior in terms of ultrastructure, size diameter and surface protein expression to those stored in PBS. In conclusion, plasma-dervied exosome characteristics strictly depend on the anticoagulants and storage temperature and duration.

22 Oct 2024·Journal of Virology

Characterization of bi-segmented and tri-segmented recombinant Pichinde virus particles

Article

Author: Ly, Hinh ; Huang, Qinfeng ; Murphy, Hannah ; Weber, Noah ; Jensen, Jacob ; Liang, Yuying ; Mendonça, Luiza

ABSTRACTMammarenaviruses include several highly virulent pathogens (e.g., Lassa virus) capable of causing severe hemorrhagic fever diseases for which there are no approved vaccines and limited treatment options. Mammarenaviruses are enveloped, bi-segmented ambisense RNA viruses. There is limited knowledge about cellular proteins incorporated into progeny virion particles and their potential biological roles in viral infection. Pichinde virus (PICV) is a prototypic arenavirus used to characterize mammarenavirus replication and pathogenesis. We have developed a recombinant PICV with a tri-segmented RNA genome as a viral vector platform. Whether the tri-segmented virion differs from the wild-type bi-segmented one in viral particle morphology and protein composition has not been addressed. In this study, recombinant PICV (rPICV) virions with a bi-segmented (rP18bi) and a tri-segmented (rP18tri) genome were purified by density-gradient ultracentrifugation and analyzed by cryo-electron microscopy and mass spectrometry. Both virion types are pleomorphic with spherical morphology and have no significant difference in size despite rP18tri having denser particles. Both virion types also contain similar sets of cellular proteins. Among the highly enriched virion-associated cellular proteins are components of the endosomal sorting complex required for transport pathway and vesicle trafficking, such as ALIX, Tsg101, VPS, CHMP, and Ras-associated binding proteins, which have known functions in virus assembly and budding. Other enriched cellular proteins include peripheral and transmembrane proteins, chaperone proteins, and ribosomal proteins; their biological roles in viral infection warrant further analysis. Our study provides important insights into mammarenavirus particle formation and aids in the future development of viral vectors and antiviral discovery.IMPORTANCEMammarenaviruses, such as Lassa virus, are enveloped RNA viruses that can cause severe hemorrhagic fever diseases (Lassa fever) with no approved vaccine and limited therapeutic options. Cellular proteins incorporated into progeny virion particles and their biological roles in mammarenavirus infection have not been well characterized. Pichinde virus (PICV) is a prototypic mammarenavirus used as a surrogate model for Lassa fever. We used cryo-electron microscopy and proteomic analysis to characterize the morphology and protein contents of the purified PICV particles that package either two (bi-segmented) or three (tri-segmented) genomic RNA segments. Our results demonstrate a similar virion morphology but different particle density for the bi- and tri-segmented viral particles and reveal major virion-associated cellular proteins. This study provides important insights into the virus-host interactions that can be used for antiviral development and optimizing arenavirus-based vaccine vectors.

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TSG101

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