Role of O-Glycosylation and Expression of CD43 and CD45 on the Surfaces of Effector T Cells in Human T Cell Leukemia Virus Type 1 Cell-to-Cell Infection

Mazurov, Dmitriy; Ilinskaya, Anna; Heidecker, Gisela; Filatov, Alexander

doi:10.1128/jvi.06993-11

Cited by 35 publications

(33 citation statements)

References 52 publications

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“…Using a panel of lectins and MAbs these authors have also determined glycoproteins that are concentrated at viral assemblies, particularly, the extracellular matrix proteins collagen and agrin, the linker proteins tetherin and galectin-3. In our previous study, we have shown the importance of O-glycan bearing molecules, CD43 and CD45, for cell adhesiveness and transmission of HTLV-1 (Mazurov et al, 2012). As VB structures are enriched with highly glycosylated proteins, we believe that our published data support the model of virus transmission via VB.…”

Section: Introductionsupporting

confidence: 67%

Monoclonal antibody profiling of cell surface proteins associated with the viral biofilms on HTLV-1 transformed cells

Tarasevich¹,

Filatov²,

Пичугин³

et al. 2015

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Summary. -Human T lymphotropic virus 1 (HTLV-1) is a pathogenic retrovirus that spreads predominantly via cell-to-cell contact. Two models of cell-to-cell virus transmission are proposed: virological synapse (VS) and viral biofilms (VB). Both infectious structures can be involved in transmission and synergistically enhance HTLV-1 spread between cells. Although transmission of virus via VB has been reported, the molecular composition of VB remains poorly understood. In this study we generated new anti-VB monoclonal antibodies (MAbs) and screened them along with a panel of anti-human cluster of differentiation (CD) MAbs to select antigens associated with VB. Among four MAbs generated against VB, two MAbs were identified as anti-CD25 (IL-2RA). We found that antigens CD4, CD150, CD25, CD70, and CD80 were enriched in VB. We also determined that expression of viral protein Tax, a central molecule in HTLV-1 transmission, upregulates intercellular adhesion molecule 1 (ICAM-1), CD95, CD25, CD70, and CD80. Whether these antigens are essential for VB formation and HTLV-1 infection remains unknown and will be determined in further experiments.Keywords: monoclonal antibody; CD antigen; HTLV-1; biofilms * Corresponding author. E-mail: dvmazurov@yandex.ru; phone: +74996128854. Abbreviations: CD = cluster of differentiation; HIV-1 = human immunodeficiency virus 1; HTLV-1 = human T cell lymphotropic virus 1; ICAM-1 = intercellular adhesion molecule 1; IL-2-RA = interleukin 2 receptor subunit A; IP = immunoprecipitation; MAb(s) = monoclonal antibody(ies); MS = mass-spectrometry; PE = phycoerythrin; TM4SF = transmembrane 4 superfamily proteins; VB = viral biofilms; VS = virological synapse; WB = Western blot; Wt = wild type

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Section: Introductionsupporting

confidence: 67%

Monoclonal antibody profiling of cell surface proteins associated with the viral biofilms on HTLV-1 transformed cells

Tarasevich¹,

Filatov²,

Пичугин³

et al. 2015

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“…Nonetheless, it is conceivable that a specific UDM protein modulates HIV-1 release or cell-to-cell transmission. For example, a recent study showed that increased expression of the UDM protein CD43 correlates with enhanced cell-to-cell transmission of HTLV-1, another retrovirus that replicates in T cells (100). Thus, although it is not known whether association of CD43 and HTLV-1 in microdomains plays a role in this increase of cell-tocell transmission, it is conceivable that specific UDMs or UDMassociated proteins contribute to cell-to-cell transmission of HIV-1.…”

Section: Discussionmentioning

confidence: 99%

HIV-1 Gag Associates with Specific Uropod-Directed Microdomains in a Manner Dependent on Its MA Highly Basic Region

Llewellyn

Grover

Olety

et al. 2013

J Virol

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In polarized T cells, HIV-1 Gag localizes to a rear-end protrusion known as the uropod in a multimerization-dependent manner. Gag-laden uropods participate in formation of virological synapses, intercellular contact structures that play a key role in cell-tocell HIV-1 transmission. Our previous observations suggest that Gag associates with uropod-directed microdomains (UDMs) that eventually comigrate with Gag to the uropod over the cell surface. However, the nature of Gag multimerization required for this movement, the composition of the UDMs, and the molecular determinants for Gag association with these microdomains remain unknown. In this study, we found that Gag multimerization prior to budding but beyond dimerization is necessary for Gag localization to the uropods, indicating that uropod localization occurs early in the assembly process. We also found that prior to membrane curvature, Gag multimers associate with a specific subset of UDMs containing PSGL-1, CD43, and CD44 but not ICAM-1, ICAM-3, or CD59. Notably, upon association, Gag excludes ICAM-3 from this subset of UDMs, revealing an active and selective reorganization of these microdomains by Gag. This specific association between Gag and UDMs is dependent on the highly basic region (HBR) in the Gag matrix (MA) domain. The overall positive charge of the HBR was needed for the interaction with the specific UDM subset, while the exact HBR sequence was not, unlike that seen for MA binding to the plasma membrane phospholipid phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P 2 ]. Taken totogether, these findings revealed that HIV-1 Gag associates with specific microdomains present in polarized T cells in an MA-dependent manner, which results in modification of the microdomain constituents.

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“…The cell coculture infection assay was performed in lymphoid cells as described previously (9,13). Briefly, 10 6 CEM cells were electroporated with 3 g of pUCHR-inGFPt and/or 3 g of pUCHR-inmCherry vector DNA and 2 g of pCMV⌬8.2R plasmid DNA in the presence or absence of 0.8 g of the pIIINL-4env plasmid, which expresses Env from HIV-1 strain NL4-3 (16).…”

Section: Methodsmentioning

confidence: 99%

“…Vector pGIPZ-P1 containing shRNA targeting phosphoprotein-1 (P1) of respiratory syncytial virus (RSV) has been described previously (13) and was used as a control. The DNA sequences of the miR30-based shRNAs were amplified from the pGIPZ plasmids by PCR with primers 5=-CGTCTAGATGTTTGAATGAGGCTTCAGTA C-3= and 5=-CGTCTAGAAGTGATTTAATTTATACCATTTTAATTC-3= and inserted into the intron at the XbaI site.…”

Section: Methodsmentioning

confidence: 99%

Improvement of HIV-1 and Human T Cell Lymphotropic Virus Type 1 Replication-Dependent Vectors via Optimization of Reporter Gene Reconstitution and Modification with Intronic Short Hairpin RNA

Shunaeva

Potashnikova

Пичугин

et al. 2015

J Virol

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Cell-to-cell transmission is an efficient mechanism to disseminate human immunodeficiency virus type 1 (HIV-1) and human T cell lymphotropic virus type 1 (HTLV-1). However, it has been challenging to quantify the level of cell-to-cell transmission because the virus-producing cells cannot be easily distinguished from infected target cells. We have previously described replication-dependent vectors that can quantify infection events in cocultured cells. These vectors contain an antisense-oriented promoter and reporter gene interrupted by a sense-oriented intron from the human gamma-globin gene. This strategy prevents expression of the reporter gene in the transfected cells but permits its expression in target cells after infection. However, the gamma-globin intron is not efficiently removed by splicing in the aforementioned vectors, thereby reducing the level of reporter gene expression after transduction into target cells. Here, we used two approaches to improve the replication-dependent vectors. First, we improved the splicing events that remove the gamma-globin intron by optimizing the intron insertion site within the reporter gene. Second, we improved the packaging of the spliced RNA without the gamma-globin intron by targeting the introncontaining RNA via microRNA 30 (miR30)-based short hairpin RNAs. Using two optimized fluorescent reporter vectors and flow cytometry, we determined that multiply HIV-1-infected cells were generated at a higher frequency in coculture than in cellfree infection; furthermore, this increase was dependent upon viruses bearing HIV-1 Env. Compared with previously described vectors, these improved vectors can quantify the infection in lymphocytes and in primary cells with a higher sensitivity and allow the detection and quantitation of multiply infected cells, providing better tools to study retroviral cell-mediated infection. IMPORTANCEThe human-pathogenic retroviruses HTLV-1 and HIV-1 can be transmitted more efficiently in vivo via direct contact of infected cells with healthy target cells than through cell-free virion-mediated infection. Despite its importance, cell-to-cell transmission has been difficult to quantify because the previously infected cells and the newly infected cells are mixed together in the same culture. In the current study, we generated vectors that are significantly improved over the previously described replication-dependent vectors. As a result, these improved vectors can efficiently detect and quantify cell-to-cell transmission or new infection events in cells in mixed culture. These luciferase-or fluorescence protein-based reporter vectors can be used to quantify and study HIV-1 or HTLV-1 cell-mediated infection in a simple one-step transfection/infection assay.

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Role of O-Glycosylation and Expression of CD43 and CD45 on the Surfaces of Effector T Cells in Human T Cell Leukemia Virus Type 1 Cell-to-Cell Infection

Cited by 35 publications

References 52 publications

Monoclonal antibody profiling of cell surface proteins associated with the viral biofilms on HTLV-1 transformed cells

Monoclonal antibody profiling of cell surface proteins associated with the viral biofilms on HTLV-1 transformed cells

HIV-1 Gag Associates with Specific Uropod-Directed Microdomains in a Manner Dependent on Its MA Highly Basic Region

Improvement of HIV-1 and Human T Cell Lymphotropic Virus Type 1 Replication-Dependent Vectors via Optimization of Reporter Gene Reconstitution and Modification with Intronic Short Hairpin RNA

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