Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Outcomes for persons with triple-class resistant HIV and a history of virologic failure.

International journal of antimicrobial agents·2026
Same author

CD4+ cell count trends after common cancers in people with HIV: a multicohort collaboration.

AIDS (London, England)·2026
Same author

[Vaccination of immunocompromised individuals: Expert opinion - update 2026].

Wiener klinische Wochenschrift·2026
Same author

Mechanistic Explanations of Manual Therapy Do Not Influence Outcomes in Healthy Individuals: A Randomized Controlled Trial.

Health science reports·2026
Same author

Preclinical development of a mutant KRAS targeting therapeutic cancer vaccine.

Cancer gene therapy·2026
Same author

Bifunctional glycolipids targeting TLR4·MD-2 and short pentraxins.

RSC chemical biology·2026

Related Experiment Video

Updated: May 12, 2026

Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay
06:15

Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay

Published on: September 7, 2018

TIM-3 does not act as a receptor for galectin-9.

Judith Leitner1, Armin Rieger, Winfried F Pickl

  • 1Division of Immune Receptors and T Cell Activation, Institute of Immunology, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.

Plos Pathogens
|April 5, 2013
PubMed
Summary

T cell immunoglobulin and mucin protein 3 (TIM-3) does not appear to interact with galectin-9 or regulate human T cell activation. Unlike PD-1, TIM-3 antibodies did not restore anti-HIV T cell responses, suggesting PD-1 is a better target for T cell exhaustion.

Related Experiment Videos

Last Updated: May 12, 2026

Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay
06:15

Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay

Published on: September 7, 2018

Area of Science:

  • Immunology
  • Cell Biology
  • Virology

Background:

  • T cell immunoglobulin and mucin protein 3 (TIM-3) is a cell surface protein implicated in T cell regulation and exhaustion.
  • Previous studies suggested TIM-3 negatively regulates T cell responses and binds galectin-9, similar to PD-1.

Purpose of the Study:

  • To investigate the interaction between TIM-3 and galectin-9 in human T cells.
  • To evaluate the role of TIM-3 in human T cell activation and exhaustion, particularly in HIV-1 infection.
  • To compare the efficacy of TIM-3 blockade versus PD-1 blockade in restoring T cell function.

Main Methods:

  • Assessed human T cell activation in the presence of galectin-9 or TIM-3 antibodies.
  • Studied the binding interaction between human and murine TIM-3 and galectin-9.
  • Analyzed TIM-3 and PD-1 expression on T cells from HIV-1-infected individuals.
  • Tested the effect of TIM-3 and PD-L antibodies on anti-HIV T cell responses in vitro.

Main Results:

  • Human T cell activation was unaffected by galectin-9 or TIM-3 antibodies.
  • No specific binding was observed between human/murine TIM-3 and galectin-9.
  • TIM-3 expression was lower and on different T cell subsets compared to PD-1 in HIV-1 infection.
  • TIM-3 antibodies failed to restore anti-HIV T cell responses, while PD-L antibodies were effective.

Conclusions:

  • Results do not support a TIM-3 and galectin-9 interaction or a functional role for TIM-3 in human T cell activation.
  • PD-1, not TIM-3, appears to be a more promising target for ameliorating T cell exhaustion in HIV-1 infection.