CD317/Tetherin is an organiser of membrane microdomains

Billcliff, Peter G.; Rollason, Ruth; Prior, Ian A.; Owen, Dylan M.; Gaus, Katharina; Banting, George

doi:10.1242/jcs.112953

Cited by 45 publications

(64 citation statements)

References 86 publications

(116 reference statements)

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“…As has been reported previously, we show that tetherin-enriched regions resided as discrete areas, or microdomains, on the plasma membrane (Billcliff et al 2013;Hammonds et al 2012). The tetherin-containing regions were also closely associated with regions of HIV-1 VLP and virus assembly and budding.…”

Section: Three-dimensional Structure and Localization Informationsupporting

confidence: 86%

Native Immunogold Labeling of Cell Surface Proteins and Viral Glycoproteins for Cryo-Electron Microscopy and Cryo-Electron Tomography Applications

Strauss

et al. 2015

J Histochem Cytochem.

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SummaryNumerous methods have been developed for immunogold labeling of thick, cryo-preserved biological specimens. However, most of the methods are permutations of chemical fixation and sample sectioning, which select and isolate the immunolabeled region of interest. We describe a method for combining immunogold labeling with cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) of the surface proteins of intact mammalian cells or the surface glycoproteins of assembling and budding viruses in the context of virus-infected mammalian cells cultured on EM grids. In this method, the cells were maintained in culture media at physiologically relevant temperatures while sequentially incubated with the primary and secondary antibodies. Subsequently, the immunogold-labeled specimens were vitrified and observed under cryo-conditions in the transmission electron microscope. Cryo-EM and cryo-ET examination of the immunogold-labeled cells revealed the association of immunogold particles with the target antigens. Additionally, the cellular structure was unaltered by pre-immunolabeling chemical fixation and retained well-preserved plasma membranes, cytoskeletal elements, and macromolecular complexes. We think this technique will be of interest to cell biologists for cryo-EM and conventional studies of native cells and pathogen-infected cells. (J Histochem Cytochem 63:780-792, 2015) Keywords cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), immuno-electron microscopy (immuno-EM), transmission electron microscopy (TEM)

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Section: Three-dimensional Structure and Localization Informationsupporting

confidence: 86%

Native Immunogold Labeling of Cell Surface Proteins and Viral Glycoproteins for Cryo-Electron Microscopy and Cryo-Electron Tomography Applications

Strauss

et al. 2015

J Histochem Cytochem.

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“…It could be related to the described function of BST-2 as an organiser of membrane microdomains (i.e. lipid rafts) (25). Indeed, by acting on the organization of the cell membrane, oligomers of BST-2 may promote the function of other molecules, specifically expressed in ER-negative cancer cells compared to ER-positive ones, which are involved in brain or liver metastasis.…”

Section: Discussionmentioning

confidence: 99%

“…Identifying such partners of BST-2 would thus warrant further investigations. Clusterisation of BST-2 around the lipid rafts would also create patches of BST-2 associated glycans, including sLe x (25). Such organization would indeed enhance the ability of BST-2 borne sLe x to be recognised by selectin by improving the avidity of the interaction.…”

Section: Discussionmentioning

confidence: 99%

Two E-selectin ligands, BST-2 and LGALS3BP, predict metastasis and poor survival of ER-negative breast cancer

Woodman¹,

Pinder²,

Tajadura³

et al. 2016

International Journal of Oncology

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Abstract. Distant metastases account for the majority of cancer-related deaths in breast cancer. The rate and site of metastasis differ between estrogen receptor (ER)-negative and ER-positive tumours, and metastatic fate can be very diverse even within the ER-negative group. Characterisation of new pro-metastatic markers may help to identify patients with higher risk and improve their care accordingly. Selectin ligands aberrantly expressed by cancer cells promote metastasis by enabling interaction between circulating tumour cells and endothelial cells in distant organs. These ligands consist in carbohydrate molecules, such as sialyl-Lewis x antigen (sLe x ), borne by glycoproteins or glycolipids on the cancer cell surface. We have previously demonstrated that the molecular scaffold presenting sLe x to selectins (e.g. glycolipid vs. glycoproteins) was crucial for these interactions to occur. Moreover, we reported that detection of sLe x alone in breast carcinomas was only of limited prognostic value. However, since sLe x was found to be carried by several glycoproteins in cancer cells, we hypothesized that the combination of the carbohydrate with its carriers could be more relevant than each marker independently. In this study, we addressed this question by analysing sLe x expression together with two glycoproteins (BST-2 and LGALS3BP), shown to interact with E-selectin in a carbohydrate-dependent manner, in a cohort of 249 invasive breast cancers. We found both glycoproteins to be associated with distant metastasis risk and poorer survival. Importantly, concomitant high expression of BST-2 with sLe x defined a subgroup of patients with ER-negative tumours displaying higher risks of liver and brain metastasis and a 3-fold decreased survival rate.

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“…HIV-1 Gag specifically binds the acidic lipid phosphatidylinositol 4,5-bisphosphate, and its assembly appears to drive the coalescence of lipid rafts and TEMs (20 -22). BST2 appears to associate both with lipid rafts and TEMs (40). Moreover, due to its unusual topology, an N-terminal transmembrane domain and a C-terminal glycosylphosphatidylinositol anchor, BST2 has been proposed to crosslink lipid rafts.…”

Section: Discussionmentioning

confidence: 99%

“…has been proposed to link lipid rafts to each other and to the actin cytoskeleton (19,40), whereas HIV assembly sites are known to include both lipid rafts and TEMs (20 -22). In light of this, we wondered whether the displacement of BST2 from viral assembly sites by Vpu might disrupt the organization of membrane microdomains at assembly sites.…”

Section: Vpu Does Not Reorganize Membrane Microdomains During the Dismentioning

confidence: 99%

Membrane Anchoring by a C-terminal Tryptophan Enables HIV-1 Vpu to Displace Bone Marrow Stromal Antigen 2 (BST2) from Sites of Viral Assembly

Lewinski

Jafari²,

Zhang

et al. 2015

Journal of Biological Chemistry

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Background: HIV-1 Vpu displaces bone marrow stromal antigen 2 (BST2) from sites of viral assembly. Results: A tryptophan residue near the C terminus of Vpu is required for this activity and interacts with the lipid bilayer. Conclusion: Interaction of the C terminus of Vpu with the lipid bilayer helps HIV-1 escape restriction by BST2. Significance: The topology of the cytoplasmic domain of Vpu with respect to the lipid bilayer is a key aspect of BST2 antagonism.

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CD317/Tetherin is an organiser of membrane microdomains

Cited by 45 publications

References 86 publications

Native Immunogold Labeling of Cell Surface Proteins and Viral Glycoproteins for Cryo-Electron Microscopy and Cryo-Electron Tomography Applications

Native Immunogold Labeling of Cell Surface Proteins and Viral Glycoproteins for Cryo-Electron Microscopy and Cryo-Electron Tomography Applications

Two E-selectin ligands, BST-2 and LGALS3BP, predict metastasis and poor survival of ER-negative breast cancer

Membrane Anchoring by a C-terminal Tryptophan Enables HIV-1 Vpu to Displace Bone Marrow Stromal Antigen 2 (BST2) from Sites of Viral Assembly

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